A family of proteins that share the F-BOX MOTIF and are involved in protein-protein interactions. They play an important role in process of protein ubiquition by associating with a variety of substrates and then associating into SCF UBIQUITIN LIGASE complexes. They are held in the ubiquitin-ligase complex via binding to SKP DOMAIN PROTEINS.
A subset of ubiquitin protein ligases that are formed by the association of a SKP DOMAIN PROTEIN, a CULLIN DOMAIN PROTEIN and a F-BOX DOMAIN PROTEIN.
A family of RNA plant viruses infecting disparate plant families. They are transmitted by specific aphid vectors. There are three genera: LUTEOVIRUS; Polerovirus; and Enamovirus.
A family of F-box domain proteins that contain sequences that are homologous to the beta subunit of transducin (BETA-TRANSDUCIN). They play an important role in the protein degradation pathway by becoming components of SKP CULLIN F-BOX PROTEIN LIGASES, which selectively act on a subset of proteins including beta-catenin and IkappaBbeta.
A family of structurally related proteins that were originally discovered for their role in cell-cycle regulation in CAENORHABDITIS ELEGANS. They play important roles in regulation of the CELL CYCLE and as components of UBIQUITIN-PROTEIN LIGASES.
A family of structurally-related proteins that were originally identified by their ability to complex with cyclin proteins (CYCLINS). They share a common domain that binds specifically to F-BOX MOTIFS. They take part in SKP CULLIN F-BOX PROTEIN LIGASES, where they can bind to a variety of F-BOX PROTEINS.
A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.
Protein structural motifs that play a role in protein-protein binding. The motifs are comprised of approximately 50 residues. Their name derives from the fact that they were found in cyclin F.
Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.
A multifunctional protein that is both a DEAD-box RNA helicase and a component of the SMN protein complex.
A large family of RNA helicases that share a common protein motif with the single letter amino acid sequence D-E-A-D (Asp-Glu-Ala-Asp). In addition to RNA helicase activity, members of the DEAD-box family participate in other aspects of RNA metabolism and regulation of RNA function.
A family of proteins that promote unwinding of RNA during splicing and translation.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
A 24-kDa HMGB protein that binds to and distorts the minor grove of DNA.
A subclass of winged helix DNA-binding proteins that share homology with their founding member fork head protein, Drosophila.
A conserved A-T rich sequence which is contained in promoters for RNA polymerase II. The segment is seven base pairs long and the nucleotides most commonly found are TATAAAA.
Enzymes that catalyze the template-directed incorporation of ribonucleotides into an RNA chain. EC 2.7.7.-.
A sequence-specific DNA-binding protein that plays an essential role as a global regulator of yeast cell cycle control. It contains a 56 amino acid MADS-box domain within the N-terminal of the protein and is one of the four founder proteins that structurally define the superfamily of MADS DOMAIN PROTEINS.
A family of low-molecular weight, non-histone proteins found in chromatin.
Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.
A superfamily of proteins that share a highly conserved MADS domain sequence motif. The term MADS refers to the first four members which were MCM1 PROTEIN; AGAMOUS 1 PROTEIN; DEFICIENS PROTEIN; and SERUM RESPONSE FACTOR. Many MADS domain proteins have been found in species from all eukaryotic kingdoms. They play an important role in development, especially in plants where they have an important role in flower development.
F344 rats are an inbred strain of albino laboratory rats (Rattus norvegicus) that have been widely used in biomedical research due to their consistent and reliable genetic background, which facilitates the study of disease mechanisms and therapeutic interventions.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
A family of sequence-related proteins similar to HMGB1 PROTEIN that contains specific HMG-BOX DOMAINS.
A plasmid whose presence in the cell, either extrachromosomal or integrated into the BACTERIAL CHROMOSOME, determines the "sex" of the bacterium, host chromosome mobilization, transfer via conjugation (CONJUGATION, GENETIC) of genetic material, and the formation of SEX PILI.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Proteins that bind to RNA molecules. Included here are RIBONUCLEOPROTEINS and other proteins whose function is to bind specifically to RNA.
Isoprostanes derived from the free radical oxidation of ARACHIDONIC ACID. Although similar in structure to enzymatically synthesized prostaglandin F2alpha (DINOPROST), they occur through non-enzymatic oxidation of cell membrane lipids.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A nuclear RNA-protein complex that plays a role in RNA processing. In the nucleoplasm, the U2 snRNP along with other small nuclear ribonucleoproteins (U1, U4-U6, and U5) assemble into SPLICEOSOMES that remove introns from pre-mRNA by splicing. The U2 snRNA forms base pairs with conserved sequence motifs at the branch point, which associates with a heat- and RNAase-sensitive factor in an early step of splicing.
DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
A forkhead transcription factor that is an essential activator of GLUCAGON gene expression.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
A subclass of closely-related SOX transcription factors. Members of the group have been found expressed in developing neuronal tissue, LYMPHOCYTES, and during EMBRYONIC DEVELOPMENT.
A transcription factor that plays an essential role in the development of the TESTES. It is encoded by a gene on the Y chromosome and contains a specific HMG-BOX DOMAIN that is found within members of the SOX family of transcription factors.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.
A family of structurally related proteins that are induced by CYTOKINES and negatively regulate cytokine-mediated SIGNAL TRANSDUCTION PATHWAYS. SOCS proteins contain a central SH2 DOMAIN and a C-terminal region of homology known as the SOCS box.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.
Established cell cultures that have the potential to propagate indefinitely.
CD4-positive T cells that inhibit immunopathology or autoimmune disease in vivo. They inhibit the immune response by influencing the activity of other cell types. Regulatory T-cells include naturally occurring CD4+CD25+ cells, IL-10 secreting Tr1 cells, and Th3 cells.
Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
The reproductive organs of plants.
A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.
The ultimate exclusion of nonsense sequences or intervening sequences (introns) before the final RNA transcript is sent to the cytoplasm.
Proteins prepared by recombinant DNA technology.
The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.
Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.
Proteins found in any species of fungus.

Evidence for F-actin-dependent and -independent mechanisms involved in assembly and stability of the medial actomyosin ring in fission yeast. (1/845)

Cell division in a number of eukaryotes, including the fission yeast Schizosaccharomyces pombe, is achieved through a medially placed actomyosin-based contractile ring. Although several components of the actomyosin ring have been identified, the mechanisms regulating ring assembly are still not understood. Here, we show by biochemical and mutational studies that the S.pombe actomyosin ring component Cdc4p is a light chain associated with Myo2p, a myosin II heavy chain. Localization of Myo2p to the medial ring depended on Cdc4p function, whereas localization of Cdc4p at the division site was independent of Myo2p. Interestingly, the actin-binding and motor domains of Myo2p are not required for its accumulation at the division site although the motor activity of Myo2p is essential for assembly of a normal actomyosin ring. The initial assembly of Myo2p and Cdc4p at the division site requires a functional F-actin cytoskeleton. Once established, however, F-actin is not required for the maintenance of Cdc4p and Myo2p medial rings, suggesting that the attachment of Cdc4p and Myo2p to the division site involves proteins other than actin itself.  (+info)

The abundance of cell cycle regulatory protein Cdc4p is controlled by interactions between its F box and Skp1p. (2/845)

Posttranslational modification of a protein by ubiquitin usually results in rapid degradation of the ubiquitinated protein by the proteasome. The transfer of ubiquitin to substrate is a multistep process. Cdc4p is a component of a ubiquitin ligase that tethers the ubiquitin-conjugating enzyme Cdc34p to its substrates. Among the domains of Cdc4p that are crucial for function are the F-box, which links Cdc4p to Cdc53p through Skp1p, and the WD-40 repeats, which are required for binding the substrate for Cdc34p. In addition to Cdc4p, other F-box proteins, including Grr1p and Met30p, may similarly act together with Cdc53p and Skp1p to function as ubiquitin ligase complexes. Because the relative abundance of these complexes, known collectively as SCFs, is important for cell viability, we have sought evidence of mechanisms that modulate F-box protein regulation. Here we demonstrate that the abundance of Cdc4p is subject to control by a peptide segment that we term the R-motif (for "reduced abundance"). Furthermore, we show that binding of Skp1p to the F-box of Cdc4p inhibits R-motif-dependent degradation of Cdc4p. These results suggest a general model for control of SCF activities.  (+info)

The Cdc6 protein is ubiquitinated in vivo for proteolysis in Saccharomyces cerevisiae. (3/845)

The Saccharomyces cerevisiae Cdc6 protein is necessary for the formation of pre-replicative complexes that are required for firing DNA replication at origins at the beginning of S phase. Cdc6p protein levels oscillate during the cell cycle. In a normal cell cycle the presence of this protein is restricted to G1, partly because the CDC6 gene is transcribed only during G1 and partly because the Cdc6p protein is rapidly degraded at late G1/early S phase. We report here that the Cdc6p protein is degraded in a Cdc4-dependent manner, suggesting that phosphorylated Cdc6 is specifically recognized by the ubiquitin-mediated proteolysis machinery. Indeed, we have found that Cdc6 is ubiquitinated in vivo and degraded by a Cdc4-dependent mechanism. Our data, together with previous observations regarding Cdc6 stability, suggest that under physiological conditions budding yeast cells degrade ubiquitinated Cdc6 every cell cycle at the beginning of S phase.  (+info)

Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase. (4/845)

The von Hippel-Lindau (VHL) tumor suppressor gene is mutated in most human kidney cancers. The VHL protein is part of a complex that includes Elongin B, Elongin C, and Cullin-2, proteins associated with transcriptional elongation and ubiquitination. Here it is shown that the endogenous VHL complex in rat liver also includes Rbx1, an evolutionarily conserved protein that contains a RING-H2 fingerlike motif and that interacts with Cullins. The yeast homolog of Rbx1 is a subunit and potent activator of the Cdc53-containing SCFCdc4 ubiquitin ligase required for ubiquitination of the cyclin-dependent kinase inhibitor Sic1 and for the G1 to S cell cycle transition. These findings provide a further link between VHL and the cellular ubiquitination machinery.  (+info)

Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1. (5/845)

Control of cyclin levels is critical for proper cell cycle regulation. In yeast, the stability of the G1 cyclin Cln1 is controlled by phosphorylation-dependent ubiquitination. Here it is shown that this reaction can be reconstituted in vitro with an SCF E3 ubiquitin ligase complex. Phosphorylated Cln1 was ubiquitinated by SCF (Skp1-Cdc53-F-box protein) complexes containing the F-box protein Grr1, Rbx1, and the E2 Cdc34. Rbx1 promotes association of Cdc34 with Cdc53 and stimulates Cdc34 auto-ubiquitination in the context of Cdc53 or SCF complexes. Rbx1, which is also a component of the von Hippel-Lindau tumor suppressor complex, may define a previously unrecognized class of E3-associated proteins.  (+info)

ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. (6/845)

We have identified two highly conserved RING finger proteins, ROC1 and ROC2, that are homologous to APC11, a subunit of the anaphase-promoting complex. ROC1 and ROC2 commonly interact with all cullins while APC11 specifically interacts with APC2, a cullin-related APC subunit. YeastROC1 encodes an essential gene whose reduced expression resulted in multiple, elongated buds and accumulation of Sic1p and Cln2p. ROC1 and APC11 immunocomplexes can catalyze isopeptide ligations to form polyubiquitin chains in an E1- and E2-dependent manner. ROC1 mutations completely abolished their ligase activity without noticeable changes in associated proteins. Ubiquitination of phosphorylated I kappa B alpha can be catalyzed by the ROC1 immunocomplex in vitro. Hence, combinations of ROC/APC11 and cullin proteins proteins potentially constitute a wide variety of ubiquitin ligases.  (+info)

Phosphorylation of the myosin-II light chain does not regulate the timing of cytokinesis in fission yeast. (7/845)

Proper coordination of cytokinesis with chromosome separation during mitosis is crucial to ensure that each daughter cell inherits an equivalent set of chromosomes. It has been proposed that one mechanism by which this is achieved is through temporally regulated myosin regulatory light chain (RLC) phosphorylation (Satterwhite, L. L., and Pollard, T. D. (1992) Curr. Opin. Cell Biol. 4, 43-52). A variety of evidence is consistent with this model. A direct test of the importance of RLC phosphorylation in vivo has been done only in Dictyostelium and Drosophila; phosphorylation of the RLC is essential in Drosophila (Jordan, P., and Karess, R. (1997) J. Cell Biol. 139, 1805-1819) but not essential in Dictyostelium (Ostrow, B. D., Chen, P., and Chisholm, R. L. (1994) J. Cell Biol. 127, 1945-1955). The Schizosaccharomyces pombe myosin light chain Cdc4p is essential for cytokinesis, but it was unknown whether phosphorylation played a role in its regulation. Here we show that the S. pombe myosin light chain Cdc4p is phosphorylated in vivo on either serine 2 or 6 but not both. Mutation of either or both of these sites to alanine did not effect the ability of Cdc4p to bind the type II myosin Myo2p, and cells expressing only these mutated versions of Cdc4p grew and divided normally. Similarly, mutation of Ser-2, Ser-6, or both residues to aspartic acid did not affect growth or division of cells. Thus we conclude that phosphorylation of Cdc4p is not essential in vivo for the function of the protein.  (+info)

Identification of cold-sensitive mutations in the Schizosaccharomyces pombe actin locus. (8/845)

In recent years, the actin cytoskeleton in Schizosaccharomyces pombe has become the subject of intense scrutiny. However, to date, only a single actin mutation has been identified. Described here is the isolation and characterization of four new cold-sensitive actin mutations. Sequence analysis of the mutant actin genes indicated that each of these mutations caused alterations in single amino acids that are conserved in all actin sequences. These mutants differ in their phenotypes. One of these mutations (act1-48) was identified as an extragenic suppressor of a mutation in the cdc4 gene, which is required for actin ring formation and cytokinesis. Interestingly, when act1-48 mutant cells were shifted to the restrictive temperature, actin patches were not detected but the actin ring formation and stability was unaffected. The three other mutations, act1-16, act1-32 and act1-67, primarily affected the actin ring formation or stability while F-actin patches did not seem to be substantially different in appearance. Given that the ultrastructural architectures of F-actin patches and the F-actin ring are presently unclear, these mutations, which affect one structure or the other, should be useful for future studies on the role of actin itself in the function of these F-actin-containing structures in S. pombe.  (+info)

F-box proteins are a family of proteins that are characterized by the presence of an F-box domain, which is a motif of about 40-50 amino acids. This domain is responsible for binding to Skp1, a component of the SCF (Skp1-Cul1-F-box protein) E3 ubiquitin ligase complex. The F-box proteins serve as the substrate recognition subunit of this complex and are involved in targeting specific proteins for ubiquitination and subsequent degradation by the 26S proteasome.

There are multiple types of F-box proteins, including FBXW (also known as β-TrCP), FBXL, and FBLX, each with different substrate specificities. These proteins play important roles in various cellular processes such as cell cycle regulation, signal transduction, and DNA damage response by controlling the stability of key regulatory proteins.

Abnormal regulation of F-box proteins has been implicated in several human diseases, including cancer, developmental disorders, and neurodegenerative diseases.

SKP (S-phase kinase associated protein) Cullin F-box protein ligases, also known as SCF complexes, are a type of E3 ubiquitin ligase that play a crucial role in the ubiquitination and subsequent degradation of proteins. These complexes are composed of several subunits: SKP1, Cul1 (Cullin 1), Rbx1 (Ring-box 1), and an F-box protein. The F-box protein is a variable component that determines the substrate specificity of the SCF complex.

The ubiquitination process mediated by SCF complexes involves the sequential transfer of ubiquitin molecules to a target protein, leading to its degradation by the 26S proteasome. This pathway is essential for various cellular processes, including cell cycle regulation, signal transduction, and DNA damage response.

Dysregulation of SCF complexes has been implicated in several diseases, such as cancer and neurodegenerative disorders, making them potential targets for therapeutic intervention.

Luteoviridae is a family of positive-strand RNA viruses that primarily infect plants. The name "luteo" comes from Latin and means "yellow," which refers to the yellowing symptoms often caused by these viruses in infected plants. The virions are non-enveloped and icosahedral in shape, with a diameter of about 25-30 nanometers.

The genome of Luteoviridae viruses is monopartite and contains one molecule of linear, single-stranded, positive-sense RNA. The genome is encapsidated within the virion and protected by a capsid protein. The genome encodes several proteins, including a readthrough protein that functions as a movement protein, allowing the virus to move from cell to cell within the plant.

Luteoviridae viruses are transmitted by aphids in a persistent, circulative manner. Once an aphid ingests virus particles while feeding on an infected plant, the virus moves through the insect's body and accumulates in its salivary glands. When the aphid feeds on a healthy plant, it injects the virus into the plant tissue along with its saliva.

Some notable members of Luteoviridae include Barley yellow dwarf virus (BYDV), Cereal yellow dwarf virus (CYDV), and Potato leafroll virus (PLRV). These viruses can cause significant economic losses in agriculture, particularly in cereal crops and potatoes.

Beta-transducin repeat-containing proteins (β-TrCP) are a group of proteins that are involved in the regulation of various cellular processes, including protein degradation and signal transduction. They are named after their structural similarity to the beta subunit of transducin, a G protein that plays a role in visual signaling.

β-TrCP proteins contain multiple repeats of a specific motif known as a WD40 domain, which is involved in protein-protein interactions. They function as substrate recognition components of an E3 ubiquitin ligase complex, which targets specific proteins for degradation by the proteasome.

One well-studied function of β-TrCP is its role in the regulation of the cell cycle and DNA damage response. It recognizes and binds to phosphorylated forms of certain proteins, leading to their ubiquitination and subsequent degradation. This helps to ensure proper progression through the cell cycle and prevents the accumulation of damaged or mutated proteins that could lead to cancer or other diseases.

Other functions of β-TrCP include regulating gene transcription, modulating immune responses, and controlling cell survival and death pathways. Dysregulation of β-TrCP has been implicated in various human diseases, including cancer, neurodegenerative disorders, and inflammatory conditions.

Cullin proteins are a family of structurally related proteins that play a crucial role in the function of E3 ubiquitin ligase complexes. These complexes are responsible for targeting specific cellular proteins for degradation by the proteasome, which is a key process in maintaining protein homeostasis within cells.

Cullin proteins act as scaffolds that bring together different components of the E3 ubiquitin ligase complex, including RING finger proteins and substrate receptors. There are several different cullin proteins identified in humans (CUL1, CUL2, CUL3, CUL4A, CUL4B, CUL5, and CUL7), each of which can form distinct E3 ubiquitin ligase complexes with unique substrate specificities.

The regulation of cullin proteins is critical for normal cellular function, and dysregulation of these proteins has been implicated in various diseases, including cancer. For example, mutations in CUL1 have been found in certain types of breast and ovarian cancers, while alterations in CUL3 have been linked to neurodegenerative disorders such as Parkinson's disease.

Overall, cullin proteins are essential components of the ubiquitin-proteasome system, which plays a critical role in regulating protein turnover and maintaining cellular homeostasis.

S-phase kinase-associated proteins (Skp2) are a group of proteins that are associated with the S-phase kinase, which is a type of enzyme that helps to regulate the cell cycle. Specifically, Skp2 is involved in the ubiquitination and degradation of certain proteins that play a role in controlling the progression of the cell cycle.

Skp2 is a member of the F-box protein family, which are components of the Skp1-Cul1-F-box (SCF) complex, a type of E3 ubiquitin ligase. The SCF complex recognizes and binds to specific proteins, tagging them for ubiquitination and subsequent degradation by the proteasome.

One of the key targets of Skp2 is the tumor suppressor protein p27, which inhibits the activity of cyclin-dependent kinases (CDKs) and helps to regulate the transition from the G1 phase to the S phase of the cell cycle. By targeting p27 for degradation, Skp2 promotes the progression of the cell cycle and has been implicated in the development of various types of cancer.

Overall, Skp2 plays a critical role in regulating the cell cycle and has important implications for the development and treatment of various diseases, including cancer.

Ubiquitin-protein ligases, also known as E3 ubiquitin ligases, are a group of enzymes that play a crucial role in the ubiquitination process. Ubiquitination is a post-translational modification where ubiquitin molecules are attached to specific target proteins, marking them for degradation by the proteasome or for other regulatory functions.

Ubiquitin-protein ligases catalyze the final step in this process by binding to both the ubiquitin protein and the target protein, facilitating the transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to the target protein. There are several different types of ubiquitin-protein ligases, each with their own specificity for particular target proteins and regulatory functions.

Ubiquitin-protein ligases have been implicated in various cellular processes such as protein degradation, DNA repair, signal transduction, and regulation of the cell cycle. Dysregulation of ubiquitination has been associated with several diseases, including cancer, neurodegenerative disorders, and inflammatory responses. Therefore, understanding the function and regulation of ubiquitin-protein ligases is an important area of research in biology and medicine.

F-box motifs are protein domains that are approximately 40-50 amino acids in length and are found in a variety of eukaryotic proteins. They are named after the first identified protein containing this domain, called F-box protein, which was discovered in fission yeast.

The F-box motif is characterized by a conserved sequence known as the F-box, which interacts with other proteins to form a larger complex called the Skp1-Cul1-F-box (SCF) protein complex. This complex plays a critical role in ubiquitination and subsequent degradation of specific target proteins by the 26S proteasome.

The F-box motif is typically found at the N-terminus of F-box proteins, which are themselves part of a larger family of proteins called F-box containing proteins (FBPs). There are three main types of FBPs: FBXWs, FBXLs, and FBXOs. Each type contains a different domain that recognizes specific motifs or sequences in target proteins, allowing for selective ubiquitination and degradation.

In summary, the F-box motif is a protein domain found in FBPs that plays a critical role in the regulation of protein stability through ubiquitination and subsequent degradation by the 26S proteasome.

Cell cycle proteins are a group of regulatory proteins that control the progression of the cell cycle, which is the series of events that take place in a eukaryotic cell leading to its division and duplication. These proteins can be classified into several categories based on their functions during different stages of the cell cycle.

The major groups of cell cycle proteins include:

1. Cyclin-dependent kinases (CDKs): CDKs are serine/threonine protein kinases that regulate key transitions in the cell cycle. They require binding to a regulatory subunit called cyclin to become active. Different CDK-cyclin complexes are activated at different stages of the cell cycle.
2. Cyclins: Cyclins are a family of regulatory proteins that bind and activate CDKs. Their levels fluctuate throughout the cell cycle, with specific cyclins expressed during particular phases. For example, cyclin D is important for the G1 to S phase transition, while cyclin B is required for the G2 to M phase transition.
3. CDK inhibitors (CKIs): CKIs are regulatory proteins that bind to and inhibit CDKs, thereby preventing their activation. CKIs can be divided into two main families: the INK4 family and the Cip/Kip family. INK4 family members specifically inhibit CDK4 and CDK6, while Cip/Kip family members inhibit a broader range of CDKs.
4. Anaphase-promoting complex/cyclosome (APC/C): APC/C is an E3 ubiquitin ligase that targets specific proteins for degradation by the 26S proteasome. During the cell cycle, APC/C regulates the metaphase to anaphase transition and the exit from mitosis by targeting securin and cyclin B for degradation.
5. Other regulatory proteins: Several other proteins play crucial roles in regulating the cell cycle, such as p53, a transcription factor that responds to DNA damage and arrests the cell cycle, and the polo-like kinases (PLKs), which are involved in various aspects of mitosis.

Overall, cell cycle proteins work together to ensure the proper progression of the cell cycle, maintain genomic stability, and prevent uncontrolled cell growth, which can lead to cancer.

DEAD-Box Protein 20 (DDX20) is a member of the DEAD-box protein family, which are named for the conserved amino acid sequence "Asp-Glu-Ala-Asp" within their helicase domains. These proteins are involved in various aspects of RNA metabolism, including splicing, transport, translation, and degradation.

DDX20, also known as p68 or DP103, is a DNA/RNA helicase that plays a role in transcriptional regulation, pre-mRNA processing, and RNA export. It has been implicated in several cellular processes, including cell cycle progression, differentiation, and apoptosis. DDX20 can interact with various proteins involved in transcription, such as RNA polymerase II and the basal transcription factor TFIID, as well as components of the spliceosome and other RNA-binding proteins.

Mutations or dysregulation of DDX20 have been associated with several human diseases, including cancer, neurodevelopmental disorders, and autoimmune diseases. For example, increased expression of DDX20 has been observed in various types of cancer, such as breast, lung, and ovarian cancers, and may contribute to tumor progression by promoting cell proliferation and inhibiting apoptosis. Additionally, mutations in the gene encoding DDX20 have been identified in patients with intellectual disability, epilepsy, and autism spectrum disorder.

DEAD-box RNA helicases are a family of proteins that are involved in unwinding RNA secondary structures and displacing proteins bound to RNA molecules. They get their name from the conserved amino acid sequence motif "DEAD" (Asp-Glu-Ala-Asp) found within their catalytic core, which is responsible for ATP-dependent helicase activity. These enzymes play crucial roles in various aspects of RNA metabolism, including pre-mRNA splicing, ribosome biogenesis, translation initiation, and RNA decay. DEAD-box helicases are also implicated in a number of human diseases, such as cancer and neurological disorders.

RNA helicases are a class of enzymes that are capable of unwinding RNA secondary structures using the energy derived from ATP hydrolysis. They play crucial roles in various cellular processes involving RNA, such as transcription, splicing, translation, ribosome biogenesis, and RNA degradation. RNA helicases can be divided into several superfamilies based on their sequence and structural similarities, with the two largest being superfamily 1 (SF1) and superfamily 2 (SF2). These enzymes typically contain conserved motifs that are involved in ATP binding and hydrolysis, as well as RNA binding. By unwinding RNA structures, RNA helicases facilitate the access of other proteins to their target RNAs, thereby enabling the coordinated regulation of RNA metabolism.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Transcription factors are proteins that play a crucial role in regulating gene expression by controlling the transcription of DNA to messenger RNA (mRNA). They function by binding to specific DNA sequences, known as response elements, located in the promoter region or enhancer regions of target genes. This binding can either activate or repress the initiation of transcription, depending on the properties and interactions of the particular transcription factor. Transcription factors often act as part of a complex network of regulatory proteins that determine the precise spatiotemporal patterns of gene expression during development, differentiation, and homeostasis in an organism.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

High Mobility Group Box 1 (HMGB1) protein is a non-histone chromosomal protein that is widely expressed in various cell types, including immune cells and nucleated cells. It plays a crucial role in the maintenance of nucleosome structure and stability, regulation of gene transcription, and DNA replication and repair. HMGB1 can be actively secreted by activated immune cells or passively released from necrotic or damaged cells. Once outside the cell, it functions as a damage-associated molecular pattern (DAMP) molecule that binds to various receptors, such as Toll-like receptors and the receptor for advanced glycation end products (RAGE), on immune cells, leading to the activation of inflammatory responses and the induction of innate and adaptive immunity. HMGB1 has been implicated in various physiological and pathological processes, including inflammation, infection, autoimmunity, cancer, and neurological disorders.

Forkhead transcription factors (FOX) are a family of proteins that play crucial roles in the regulation of gene expression through the process of binding to specific DNA sequences, thereby controlling various biological processes such as cell growth, differentiation, and apoptosis. These proteins are characterized by a conserved DNA-binding domain, known as the forkhead box or FOX domain, which adopts a winged helix structure that recognizes and binds to the consensus sequence 5'-(G/A)(T/C)AA(C/A)A-3'.

The FOX family is further divided into subfamilies based on the structure of their DNA-binding domains, with each subfamily having distinct functions. For example, FOXP proteins are involved in brain development and function, while FOXO proteins play a key role in regulating cellular responses to stress and metabolism. Dysregulation of forkhead transcription factors has been implicated in various diseases, including cancer, diabetes, and neurodegenerative disorders.

I'm sorry for any confusion, but "TATA box" is actually a term used in molecular biology, specifically in the field of genetics and gene regulation. It does not have a direct medical definition.

The TATA box is a DNA sequence located in the promoter region of many genes, which serves as a binding site for certain proteins involved in the initiation of transcription. Transcription is the first step in gene expression, where the information in a gene is used to create a corresponding protein or RNA molecule.

The TATA box is typically found about 25-30 base pairs upstream of the transcription start site and has the consensus sequence "TATAAA". It is recognized by the TATA-binding protein (TBP), which is a component of the transcription factor II D (TFIIB) complex. The binding of TBP to the TATA box helps to position the RNA polymerase enzyme properly for the initiation of transcription.

While not a medical term per se, understanding the function of the TATA box and other cis-acting elements in gene regulation is important for understanding how genes are turned on and off in various cellular processes and how this can go awry in certain diseases.

RNA nucleotidyltransferases are a class of enzymes that catalyze the template-independent addition of nucleotides to the 3' end of RNA molecules, using nucleoside triphosphates as substrates. These enzymes play crucial roles in various biological processes, including RNA maturation, quality control, and regulation.

The reaction catalyzed by RNA nucleotidyltransferases involves the formation of a phosphodiester bond between the 3'-hydroxyl group of the RNA substrate and the alpha-phosphate group of the incoming nucleoside triphosphate. This results in the elongation of the RNA molecule by one or more nucleotides, depending on the specific enzyme and context.

Examples of RNA nucleotidyltransferases include poly(A) polymerases, which add poly(A) tails to mRNAs during processing, and terminal transferases, which are involved in DNA repair and V(D)J recombination in the immune system. These enzymes have been implicated in various diseases, including cancer and neurological disorders, making them potential targets for therapeutic intervention.

Minichromosome Maintenance 1 Protein (MCM1) is a protein that belongs to the minichromosome maintenance proteins complex, which is essential for the initiation and regulation of eukaryotic DNA replication. MCM1 is a crucial component of this complex, and it functions as a transcription factor that regulates the expression of genes involved in various cellular processes such as cell cycle progression, DNA repair, and development. In addition to its role in DNA replication and gene regulation, MCM1 has also been implicated in the development of certain types of cancer, making it an important area of research in cancer biology.

High mobility group proteins (HMG proteins) are a family of nuclear proteins that are characterized by their ability to bind to DNA and influence its structure and function. They are named "high mobility" because of their rapid movement in gel electrophoresis. HMG proteins are involved in various nuclear processes, including chromatin remodeling, transcription regulation, and DNA repair.

There are three main classes of HMG proteins: HMGA, HMGB, and HMGN. Each class has distinct structural features and functions. For example, HMGA proteins have a unique "AT-hook" domain that allows them to bind to the minor groove of AT-rich DNA sequences, while HMGB proteins have two "HMG-box" domains that enable them to bend and unwind DNA.

HMG proteins play important roles in many physiological and pathological processes, such as embryonic development, inflammation, and cancer. Dysregulation of HMG protein function has been implicated in various diseases, including neurodegenerative disorders, diabetes, and cancer. Therefore, understanding the structure, function, and regulation of HMG proteins is crucial for developing new therapeutic strategies for these diseases.

Arabidopsis proteins refer to the proteins that are encoded by the genes in the Arabidopsis thaliana plant, which is a model organism commonly used in plant biology research. This small flowering plant has a compact genome and a short life cycle, making it an ideal subject for studying various biological processes in plants.

Arabidopsis proteins play crucial roles in many cellular functions, such as metabolism, signaling, regulation of gene expression, response to environmental stresses, and developmental processes. Research on Arabidopsis proteins has contributed significantly to our understanding of plant biology and has provided valuable insights into the molecular mechanisms underlying various agronomic traits.

Some examples of Arabidopsis proteins include transcription factors, kinases, phosphatases, receptors, enzymes, and structural proteins. These proteins can be studied using a variety of techniques, such as biochemical assays, protein-protein interaction studies, and genetic approaches, to understand their functions and regulatory mechanisms in plants.

MADS domain proteins are a family of transcription factors that play crucial roles in various developmental processes in plants, including flower development and organ formation. The name "MADS" is an acronym derived from the initial letters of four founding members: MCM1 from Saccharomyces cerevisiae, AGAMOUS from Arabidopsis thaliana, DEFICIENS from Antirrhinum majus, and SRF from Homo sapiens.

These proteins share a highly conserved DNA-binding domain called the MADS-box, which binds to specific sequences in the promoter regions of their target genes. The MADS domain proteins often form higher-order complexes through protein-protein interactions, leading to the regulation of gene expression involved in developmental transitions and cell fate determination. In plants, MADS domain proteins have been implicated in various aspects of reproductive development, such as floral meristem identity, floral organ specification, and ovule development.

F344 is a strain code used to designate an outbred stock of rats that has been inbreeded for over 100 generations. The F344 rats, also known as Fischer 344 rats, were originally developed at the National Institutes of Health (NIH) and are now widely used in biomedical research due to their consistent and reliable genetic background.

Inbred strains, like the F344, are created by mating genetically identical individuals (siblings or parents and offspring) for many generations until a state of complete homozygosity is reached, meaning that all members of the strain have identical genomes. This genetic uniformity makes inbred strains ideal for use in studies where consistent and reproducible results are important.

F344 rats are known for their longevity, with a median lifespan of around 27-31 months, making them useful for aging research. They also have a relatively low incidence of spontaneous tumors compared to other rat strains. However, they may be more susceptible to certain types of cancer and other diseases due to their inbred status.

It's important to note that while F344 rats are often used as a standard laboratory rat strain, there can still be some genetic variation between individual animals within the same strain, particularly if they come from different suppliers or breeding colonies. Therefore, it's always important to consider the source and history of any animal model when designing experiments and interpreting results.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

DNA-binding proteins are a type of protein that have the ability to bind to DNA (deoxyribonucleic acid), the genetic material of organisms. These proteins play crucial roles in various biological processes, such as regulation of gene expression, DNA replication, repair and recombination.

The binding of DNA-binding proteins to specific DNA sequences is mediated by non-covalent interactions, including electrostatic, hydrogen bonding, and van der Waals forces. The specificity of binding is determined by the recognition of particular nucleotide sequences or structural features of the DNA molecule.

DNA-binding proteins can be classified into several categories based on their structure and function, such as transcription factors, histones, and restriction enzymes. Transcription factors are a major class of DNA-binding proteins that regulate gene expression by binding to specific DNA sequences in the promoter region of genes and recruiting other proteins to modulate transcription. Histones are DNA-binding proteins that package DNA into nucleosomes, the basic unit of chromatin structure. Restriction enzymes are DNA-binding proteins that recognize and cleave specific DNA sequences, and are widely used in molecular biology research and biotechnology applications.

High Mobility Group Box (HMGB) proteins are a family of nuclear proteins that are highly conserved and expressed in eukaryotic cells. They play a crucial role in the regulation of gene expression, DNA repair, and maintenance of nucleosome structure. HMGB proteins contain two positively charged DNA-binding domains (HMG boxes) and a negatively charged acidic tail. These proteins can bind to DNA in a variety of ways, bending it and altering its structure, which in turn affects the binding of other proteins and the transcriptional activity of genes. HMGB proteins can also be released from cells under conditions of stress or injury, where they act as damage-associated molecular patterns (DAMPs) and contribute to the inflammatory response.

I'm not aware of a widely recognized or established medical term called "F factor." It is possible that it could be a term specific to certain medical specialties, research, or publications. In order to provide an accurate and helpful response, I would need more context or information about where you encountered this term.

If you meant to ask about the F-plasmid, which is sometimes referred to as the "F factor" in bacteriology, it is a type of plasmid that can be found in certain strains of bacteria and carries genes related to conjugation (the process by which bacteria transfer genetic material between each other). The F-plasmid can exist as an independent circular DNA molecule or integrate into the chromosome of the host bacterium.

If this is not the term you were looking for, please provide more context so I can give a better answer.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

RNA-binding proteins (RBPs) are a class of proteins that selectively interact with RNA molecules to form ribonucleoprotein complexes. These proteins play crucial roles in the post-transcriptional regulation of gene expression, including pre-mRNA processing, mRNA stability, transport, localization, and translation. RBPs recognize specific RNA sequences or structures through their modular RNA-binding domains, which can be highly degenerate and allow for the recognition of a wide range of RNA targets. The interaction between RBPs and RNA is often dynamic and can be regulated by various post-translational modifications of the proteins or by environmental stimuli, allowing for fine-tuning of gene expression in response to changing cellular needs. Dysregulation of RBP function has been implicated in various human diseases, including neurological disorders and cancer.

F2-isoprostanes are a type of prostaglandin-like compound that is formed in the body through the free radical-catalyzed peroxidation of arachidonic acid, a polyunsaturated fatty acid found in cell membranes. They are produced in response to oxidative stress and are often used as a biomarker for lipid peroxidation and oxidative damage in various diseases, including atherosclerosis, cancer, and neurodegenerative disorders. F2-isoprostanes are chemically stable and can be measured in biological fluids such as blood, urine, and breath condensate. They have been shown to cause vasoconstriction, platelet aggregation, and inflammation, which may contribute to the pathogenesis of various diseases.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

A ribonucleoprotein, U2 small nuclear (U2 snRNP) is a type of spliceosomal small nuclear ribonucleoprotein (snRNP) complex that plays a crucial role in the pre-messenger RNA (pre-mRNA) splicing process during gene expression in eukaryotic cells.

Pre-mRNA splicing is the removal of non-coding sequences, called introns, from the pre-mRNA molecule and the joining together of the remaining coding sequences, or exons, to form a continuous mRNA sequence that can be translated into protein. U2 snRNPs are essential components of the spliceosome, the large ribonucleoprotein complex responsible for pre-mRNA splicing.

The U2 snRNP is composed of several proteins and a small nuclear RNA (snRNA) molecule called U2 small nuclear RNA (U2 snRNA). The U2 snRNA binds to specific sequences within the pre-mRNA, forming part of the intron's branch site, which helps define the boundaries of the exons and introns. This interaction facilitates the recognition and assembly of other spliceosomal components, ultimately leading to the precise excision of introns and ligation of exons in the mature mRNA molecule.

In summary, U2 snRNP is a ribonucleoprotein complex involved in pre-mRNA splicing, where it plays a critical role in recognizing and processing intron-exon boundaries during gene expression in eukaryotic cells.

Promoter regions in genetics refer to specific DNA sequences located near the transcription start site of a gene. They serve as binding sites for RNA polymerase and various transcription factors that regulate the initiation of gene transcription. These regulatory elements help control the rate of transcription and, therefore, the level of gene expression. Promoter regions can be composed of different types of sequences, such as the TATA box and CAAT box, and their organization and composition can vary between different genes and species.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Hepatocyte Nuclear Factor 3-alpha (HNF-3α), also known as FoxA1, is a transcription factor that plays a crucial role in the development and function of the liver. It belongs to the forkhead box (Fox) family of proteins, which are characterized by a conserved DNA-binding domain called the forkhead box or winged helix domain.

HNF-3α is primarily expressed in the liver, pancreas, and intestine, where it regulates the expression of various genes involved in glucose and lipid metabolism, bile acid synthesis, and other liver-specific functions. It acts by binding to specific DNA sequences called FOX or HNF-3 response elements, thereby modulating the transcriptional activity of target genes.

Mutations in the gene encoding HNF-3α have been associated with several human diseases, including maturity-onset diabetes of the young (MODY) and liver dysfunction. In MODY, mutations in HNF-3α impair its ability to regulate glucose metabolism, leading to impaired insulin secretion and hyperglycemia. In the liver, HNF-3α plays a critical role in maintaining the differentiated state of hepatocytes and regulating their response to various hormonal and metabolic signals.

Genetic transcription is the process by which the information in a strand of DNA is used to create a complementary RNA molecule. This process is the first step in gene expression, where the genetic code in DNA is converted into a form that can be used to produce proteins or functional RNAs.

During transcription, an enzyme called RNA polymerase binds to the DNA template strand and reads the sequence of nucleotide bases. As it moves along the template, it adds complementary RNA nucleotides to the growing RNA chain, creating a single-stranded RNA molecule that is complementary to the DNA template strand. Once transcription is complete, the RNA molecule may undergo further processing before it can be translated into protein or perform its functional role in the cell.

Transcription can be either "constitutive" or "regulated." Constitutive transcription occurs at a relatively constant rate and produces essential proteins that are required for basic cellular functions. Regulated transcription, on the other hand, is subject to control by various intracellular and extracellular signals, allowing cells to respond to changing environmental conditions or developmental cues.

SOXC transcription factors are a subgroup of the SOX (SRY-related HMG box) family of proteins, which are involved in various developmental processes. The SOXC group includes SOX4, SOX11, and SOX12, which share similar structures and functions. These transcription factors play crucial roles in regulating gene expression during embryonic development and in adult tissues. They are particularly known for their involvement in neural crest cell development, neurogenesis, and oncogenesis.

SOXC proteins contain a highly conserved HMG (High Mobility Group) box DNA-binding domain that allows them to recognize and bind to specific DNA sequences, thereby influencing the transcription of target genes. Dysregulation of SOXC transcription factors has been implicated in several human diseases, including various types of cancer.

The Sex-Determining Region Y (SRY) protein is a transcription factor that plays a critical role in male sex determination. It is encoded by the SRY gene, which is located on the Y chromosome in humans and many other mammal species. The primary function of the SRY protein is to initiate the development of the testes during embryonic development.

In the absence of a functional SRY protein, the gonads will develop into ovaries. With a functional SRY protein, the gonads will develop into testes, which then produce androgens, including testosterone, that are necessary for the development of male secondary sexual characteristics. Mutations in the SRY gene can lead to sex reversal, where an individual with a Y chromosome develops as a female due to non-functional or absent SRY protein.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Nuclear proteins are a category of proteins that are primarily found in the nucleus of a eukaryotic cell. They play crucial roles in various nuclear functions, such as DNA replication, transcription, repair, and RNA processing. This group includes structural proteins like lamins, which form the nuclear lamina, and regulatory proteins, such as histones and transcription factors, that are involved in gene expression. Nuclear localization signals (NLS) often help target these proteins to the nucleus by interacting with importin proteins during active transport across the nuclear membrane.

Suppressors of Cytokine Signaling (SOCS) proteins are a family of intracellular signaling molecules that play a crucial role in regulating cytokine signaling pathways. They function as negative feedback inhibitors, helping to control the duration and intensity of cytokine responses.

There are eight known members of the SOCS family (SOCS1-7 and CIS), all of which share a similar structure consisting of:

1. An N-terminal domain, which varies among different SOCS proteins and is involved in specific target recognition.
2. A central SH2 (Src homology 2) domain, responsible for binding to phosphorylated tyrosine residues on cytokine receptors or other signaling molecules.
3. A C-terminal SOCS box, which serves as a protein-protein interaction module that recruits E3 ubiquitin ligases, leading to the degradation of target proteins via the ubiquitin-proteasome pathway.

SOCS proteins regulate cytokine signaling by inhibiting key components of the JAK-STAT (Janus kinase-signal transducer and activator of transcription) pathway, one of the major intracellular signaling cascades activated by cytokines. Specifically, SOCS1 and SOCS3 bind directly to the activated JAK kinases, preventing their interaction with STAT proteins and thus inhibiting downstream signal transduction. Additionally, SOCS proteins can also target receptors or JAKs for degradation via ubiquitination, further dampening cytokine signaling.

Dysregulation of SOCS protein expression has been implicated in various pathological conditions, including inflammatory diseases, autoimmune disorders, and cancer.

Saccharomyces cerevisiae proteins are the proteins that are produced by the budding yeast, Saccharomyces cerevisiae. This organism is a single-celled eukaryote that has been widely used as a model organism in scientific research for many years due to its relatively simple genetic makeup and its similarity to higher eukaryotic cells.

The genome of Saccharomyces cerevisiae has been fully sequenced, and it is estimated to contain approximately 6,000 genes that encode proteins. These proteins play a wide variety of roles in the cell, including catalyzing metabolic reactions, regulating gene expression, maintaining the structure of the cell, and responding to environmental stimuli.

Many Saccharomyces cerevisiae proteins have human homologs and are involved in similar biological processes, making this organism a valuable tool for studying human disease. For example, many of the proteins involved in DNA replication, repair, and recombination in yeast have human counterparts that are associated with cancer and other diseases. By studying these proteins in yeast, researchers can gain insights into their function and regulation in humans, which may lead to new treatments for disease.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

'Gene expression regulation' refers to the processes that control whether, when, and where a particular gene is expressed, meaning the production of a specific protein or functional RNA encoded by that gene. This complex mechanism can be influenced by various factors such as transcription factors, chromatin remodeling, DNA methylation, non-coding RNAs, and post-transcriptional modifications, among others. Proper regulation of gene expression is crucial for normal cellular function, development, and maintaining homeostasis in living organisms. Dysregulation of gene expression can lead to various diseases, including cancer and genetic disorders.

A conserved sequence in the context of molecular biology refers to a pattern of nucleotides (in DNA or RNA) or amino acids (in proteins) that has remained relatively unchanged over evolutionary time. These sequences are often functionally important and are highly conserved across different species, indicating strong selection pressure against changes in these regions.

In the case of protein-coding genes, the corresponding amino acid sequence is deduced from the DNA sequence through the genetic code. Conserved sequences in proteins may indicate structurally or functionally important regions, such as active sites or binding sites, that are critical for the protein's activity. Similarly, conserved non-coding sequences in DNA may represent regulatory elements that control gene expression.

Identifying conserved sequences can be useful for inferring evolutionary relationships between species and for predicting the function of unknown genes or proteins.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

A two-hybrid system technique is a type of genetic screening method used in molecular biology to identify protein-protein interactions within an organism, most commonly baker's yeast (Saccharomyces cerevisiae) or Escherichia coli. The name "two-hybrid" refers to the fact that two separate proteins are being examined for their ability to interact with each other.

The technique is based on the modular nature of transcription factors, which typically consist of two distinct domains: a DNA-binding domain (DBD) and an activation domain (AD). In a two-hybrid system, one protein of interest is fused to the DBD, while the second protein of interest is fused to the AD. If the two proteins interact, the DBD and AD are brought in close proximity, allowing for transcriptional activation of a reporter gene that is linked to a specific promoter sequence recognized by the DBD.

The main components of a two-hybrid system include:

1. Bait protein (fused to the DNA-binding domain)
2. Prey protein (fused to the activation domain)
3. Reporter gene (transcribed upon interaction between bait and prey proteins)
4. Promoter sequence (recognized by the DBD when brought in proximity due to interaction)

The two-hybrid system technique has several advantages, including:

1. Ability to screen large libraries of potential interacting partners
2. High sensitivity for detecting weak or transient interactions
3. Applicability to various organisms and protein types
4. Potential for high-throughput analysis

However, there are also limitations to the technique, such as false positives (interactions that do not occur in vivo) and false negatives (lack of detection of true interactions). Additionally, the fusion proteins may not always fold or localize correctly, leading to potential artifacts. Despite these limitations, two-hybrid system techniques remain a valuable tool for studying protein-protein interactions and have contributed significantly to our understanding of various cellular processes.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Regulatory T-lymphocytes (Tregs), also known as suppressor T cells, are a subpopulation of T-cells that play a critical role in maintaining immune tolerance and preventing autoimmune diseases. They function to suppress the activation and proliferation of other immune cells, thereby regulating the immune response and preventing it from attacking the body's own tissues.

Tregs constitutively express the surface markers CD4 and CD25, as well as the transcription factor Foxp3, which is essential for their development and function. They can be further divided into subsets based on their expression of other markers, such as CD127 and CD45RA.

Tregs are critical for maintaining self-tolerance by suppressing the activation of self-reactive T cells that have escaped negative selection in the thymus. They also play a role in regulating immune responses to foreign antigens, such as those encountered during infection or cancer, and can contribute to the immunosuppressive microenvironment found in tumors.

Dysregulation of Tregs has been implicated in various autoimmune diseases, including type 1 diabetes, rheumatoid arthritis, and multiple sclerosis, as well as in cancer and infectious diseases. Therefore, understanding the mechanisms that regulate Treg function is an important area of research with potential therapeutic implications.

Repressor proteins are a type of regulatory protein in molecular biology that suppress the transcription of specific genes into messenger RNA (mRNA) by binding to DNA. They function as part of gene regulation processes, often working in conjunction with an operator region and a promoter region within the DNA molecule. Repressor proteins can be activated or deactivated by various signals, allowing for precise control over gene expression in response to changing cellular conditions.

There are two main types of repressor proteins:

1. DNA-binding repressors: These directly bind to specific DNA sequences (operator regions) near the target gene and prevent RNA polymerase from transcribing the gene into mRNA.
2. Allosteric repressors: These bind to effector molecules, which then cause a conformational change in the repressor protein, enabling it to bind to DNA and inhibit transcription.

Repressor proteins play crucial roles in various biological processes, such as development, metabolism, and stress response, by controlling gene expression patterns in cells.

Adenosine triphosphatases (ATPases) are a group of enzymes that catalyze the conversion of adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and inorganic phosphate. This reaction releases energy, which is used to drive various cellular processes such as muscle contraction, transport of ions across membranes, and synthesis of proteins and nucleic acids.

ATPases are classified into several types based on their structure, function, and mechanism of action. Some examples include:

1. P-type ATPases: These ATPases form a phosphorylated intermediate during the reaction cycle and are involved in the transport of ions across membranes, such as the sodium-potassium pump and calcium pumps.
2. F-type ATPases: These ATPases are found in mitochondria, chloroplasts, and bacteria, and are responsible for generating a proton gradient across the membrane, which is used to synthesize ATP.
3. V-type ATPases: These ATPases are found in vacuolar membranes and endomembranes, and are involved in acidification of intracellular compartments.
4. A-type ATPases: These ATPases are found in the plasma membrane and are involved in various functions such as cell signaling and ion transport.

Overall, ATPases play a crucial role in maintaining the energy balance of cells and regulating various physiological processes.

Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.

"Saccharomyces cerevisiae" is not typically considered a medical term, but it is a scientific name used in the field of microbiology. It refers to a species of yeast that is commonly used in various industrial processes, such as baking and brewing. It's also widely used in scientific research due to its genetic tractability and eukaryotic cellular organization.

However, it does have some relevance to medical fields like medicine and nutrition. For example, certain strains of S. cerevisiae are used as probiotics, which can provide health benefits when consumed. They may help support gut health, enhance the immune system, and even assist in the digestion of certain nutrients.

In summary, "Saccharomyces cerevisiae" is a species of yeast with various industrial and potential medical applications.

Complementary DNA (cDNA) is a type of DNA that is synthesized from a single-stranded RNA molecule through the process of reverse transcription. In this process, the enzyme reverse transcriptase uses an RNA molecule as a template to synthesize a complementary DNA strand. The resulting cDNA is therefore complementary to the original RNA molecule and is a copy of its coding sequence, but it does not contain non-coding regions such as introns that are present in genomic DNA.

Complementary DNA is often used in molecular biology research to study gene expression, protein function, and other genetic phenomena. For example, cDNA can be used to create cDNA libraries, which are collections of cloned cDNA fragments that represent the expressed genes in a particular cell type or tissue. These libraries can then be screened for specific genes or gene products of interest. Additionally, cDNA can be used to produce recombinant proteins in heterologous expression systems, allowing researchers to study the structure and function of proteins that may be difficult to express or purify from their native sources.

I'm sorry for any confusion, but "flowers" is not a term that has a medical definition. The term "flowers" is commonly used to refer to the reproductive structures of flowering plants (angiosperms), which are characterized by having both male and female reproductive organs or separate male and female flowers.

If you have any questions related to medical terminology or health conditions, I would be happy to try to help answer those for you!

Ligases are a group of enzymes that catalyze the formation of a covalent bond between two molecules, usually involving the joining of two nucleotides in a DNA or RNA strand. They play a crucial role in various biological processes such as DNA replication, repair, and recombination. In DNA ligases, the enzyme seals nicks or breaks in the phosphodiester backbone of the DNA molecule by catalyzing the formation of an ester bond between the 3'-hydroxyl group and the 5'-phosphate group of adjacent nucleotides. This process is essential for maintaining genomic integrity and stability.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

HeLa cells are a type of immortalized cell line used in scientific research. They are derived from a cancer that developed in the cervical tissue of Henrietta Lacks, an African-American woman, in 1951. After her death, cells taken from her tumor were found to be capable of continuous division and growth in a laboratory setting, making them an invaluable resource for medical research.

HeLa cells have been used in a wide range of scientific studies, including research on cancer, viruses, genetics, and drug development. They were the first human cell line to be successfully cloned and are able to grow rapidly in culture, doubling their population every 20-24 hours. This has made them an essential tool for many areas of biomedical research.

It is important to note that while HeLa cells have been instrumental in numerous scientific breakthroughs, the story of their origin raises ethical questions about informed consent and the use of human tissue in research.

RNA splicing is a post-transcriptional modification process in which the non-coding sequences (introns) are removed and the coding sequences (exons) are joined together in a messenger RNA (mRNA) molecule. This results in a continuous mRNA sequence that can be translated into a single protein. Alternative splicing, where different combinations of exons are included or excluded, allows for the creation of multiple proteins from a single gene.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Nucleic acid conformation refers to the three-dimensional structure that nucleic acids (DNA and RNA) adopt as a result of the bonding patterns between the atoms within the molecule. The primary structure of nucleic acids is determined by the sequence of nucleotides, while the conformation is influenced by factors such as the sugar-phosphate backbone, base stacking, and hydrogen bonding.

Two common conformations of DNA are the B-form and the A-form. The B-form is a right-handed helix with a diameter of about 20 Å and a pitch of 34 Å, while the A-form has a smaller diameter (about 18 Å) and a shorter pitch (about 25 Å). RNA typically adopts an A-form conformation.

The conformation of nucleic acids can have significant implications for their function, as it can affect their ability to interact with other molecules such as proteins or drugs. Understanding the conformational properties of nucleic acids is therefore an important area of research in molecular biology and medicine.

'Drosophila proteins' refer to the proteins that are expressed in the fruit fly, Drosophila melanogaster. This organism is a widely used model system in genetics, developmental biology, and molecular biology research. The study of Drosophila proteins has contributed significantly to our understanding of various biological processes, including gene regulation, cell signaling, development, and aging.

Some examples of well-studied Drosophila proteins include:

1. HSP70 (Heat Shock Protein 70): A chaperone protein involved in protein folding and protection from stress conditions.
2. TUBULIN: A structural protein that forms microtubules, important for cell division and intracellular transport.
3. ACTIN: A cytoskeletal protein involved in muscle contraction, cell motility, and maintenance of cell shape.
4. BETA-GALACTOSIDASE (LACZ): A reporter protein often used to monitor gene expression patterns in transgenic flies.
5. ENDOGLIN: A protein involved in the development of blood vessels during embryogenesis.
6. P53: A tumor suppressor protein that plays a crucial role in preventing cancer by regulating cell growth and division.
7. JUN-KINASE (JNK): A signaling protein involved in stress response, apoptosis, and developmental processes.
8. DECAPENTAPLEGIC (DPP): A member of the TGF-β (Transforming Growth Factor Beta) superfamily, playing essential roles in embryonic development and tissue homeostasis.

These proteins are often studied using various techniques such as biochemistry, genetics, molecular biology, and structural biology to understand their functions, interactions, and regulation within the cell.

Fungal proteins are a type of protein that is specifically produced and present in fungi, which are a group of eukaryotic organisms that include microorganisms such as yeasts and molds. These proteins play various roles in the growth, development, and survival of fungi. They can be involved in the structure and function of fungal cells, metabolism, pathogenesis, and other cellular processes. Some fungal proteins can also have important implications for human health, both in terms of their potential use as therapeutic targets and as allergens or toxins that can cause disease.

Fungal proteins can be classified into different categories based on their functions, such as enzymes, structural proteins, signaling proteins, and toxins. Enzymes are proteins that catalyze chemical reactions in fungal cells, while structural proteins provide support and protection for the cell. Signaling proteins are involved in communication between cells and regulation of various cellular processes, and toxins are proteins that can cause harm to other organisms, including humans.

Understanding the structure and function of fungal proteins is important for developing new treatments for fungal infections, as well as for understanding the basic biology of fungi. Research on fungal proteins has led to the development of several antifungal drugs that target specific fungal enzymes or other proteins, providing effective treatment options for a range of fungal diseases. Additionally, further study of fungal proteins may reveal new targets for drug development and help improve our ability to diagnose and treat fungal infections.

F-box proteins are proteins containing at least one F-box domain. The first identified F-box protein is one of three components ... interacts directly with the SCF protein Skp1. F-box domains commonly exist in proteins in cancer with other protein-protein ... F-box domain is a protein structural motif of about 50 amino acids that mediates protein-protein interactions. It has consensus ... F-box proteins are involved in many plant vegetative and reproduction growth and development. For example, F-box protein-FOA1 ...
... (FOXO1), also known as forkhead in rhabdomyosarcoma (FKHR), is a protein that in humans is encoded by ... "DAF-16 recruits the CREB-binding protein coactivator complex to the insulin-like growth factor binding protein 1 promoter in ... FOXO1A+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH) This article incorporates text ... Guo S, Rena G, Cichy S, He X, Cohen P, Unterman T (June 1999). "Phosphorylation of serine 256 by protein kinase B disrupts ...
... is a protein that in humans is encoded by the FBXO16 gene. This gene encodes a member of the F-box protein ... The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), ... "Entrez Gene: F-box protein 16". Retrieved 2016-09-13. Cheng H, Ma Y, Ni X, Jiang M, Guo L, Jin W, Xu W, Cao G, Ji C, Yin K, Gu ... The F-box proteins are divided into three classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and ...
... and F-box proteins, act as protein-ubiquitin ligases. F-box proteins interact with SKP1 through the F box, and they interact ... F-box protein 15 also known as Fbx15 is a protein that in humans is encoded by the FBXO15 gene. Members of the F-box protein ... Differently from other F-box proteins, Fbx15 recognizes its substrate Kif1-Binding Protein (KBP) in an acetylation dependent ... "Entrez Gene: F-box protein 15". Jin J, Cardozo T, Lovering RC, Elledge SJ, Pagano M, Harper JW (November 2004). "Systematic ...
... and F-box proteins, act as protein-ubiquitin ligases. F-box proteins interact with SKP1 through the F box, and they interact ... F-box protein 40 is a protein that in humans is encoded by the FBXO40 gene. Fbxo40 induces ubiquitination of IRS1, thus ... Members of the F-box protein family, such as FBXO40, are characterized by an approximately 40-amino acid F-box motif. SCF ... "Entrez Gene: F-box protein 40". Retrieved 2017-11-24. Jin J, Cardozo T, Lovering RC, Elledge SJ, Pagano M, Harper JW (November ...
... also known as Y-box transcription factor or nuclease-sensitive element-binding protein 1 is a protein ... Y box binding protein 1 has been shown to interact with: ANKRD2, CTCF, P53, PCNA, RBBP6, and SFRS9. GRCh38: Ensembl release 89 ... "Entrez Gene: YBX1 Y box binding protein 1". Lage H, Surowiak P, Holm PS (November 2008). "[YB-1 as a potential target in cancer ... Safak M, Gallia GL, Ansari SA, Khalili K (1999). "Physical and functional interaction between the Y-box binding protein YB-1 ...
... is a protein that in humans is encoded by the TBPL2 gene. The TBPL2 protein is also known as ... "Entrez Gene: TATA-box binding protein like 2". Retrieved 2018-01-31. Persengiev SP, Zhu X, Dixit BL, Maston GA, Kittler EL, ... a TATA-box-binding protein-related factor, is vertebrate-specific and widely expressed". Proceedings of the National Academy of ... The protein was independently discovered in three laboratories as a vertebrate-specific family member of TATA-binding protein ( ...
... is a protein that in humans is encoded by the FBXL15 gene. GRCh38: Ensembl release 89 ... "Entrez Gene: F-box and leucine rich repeat protein 15". Retrieved 2018-03-21. v t e (Articles with short description, Short ...
Matz KM, Guzman RM, Goodman AG (2019-01-01). Vanpouille-Box C, Galluzzi L (eds.). "The Role of Nucleic Acid Sensing in ... Protein kinase RNA-activated also known as protein kinase R (PKR), interferon-induced, double-stranded RNA-activated protein ... Patel RC, Sen GC (August 1998). "PACT, a protein activator of the interferon-induced protein kinase, PKR". The EMBO Journal. 17 ... PKR also mediates ethanol-induced protein synthesis inhibition and apoptosis which is linked to fetal alcohol syndrome. Protein ...
... "c-Fos-induced activation of a TATA-box-containing promoter involves direct contact with TATA-box-binding protein". Mol. Cell. ... "Pax-6 interactions with TATA-box-binding protein and retinoblastoma protein". Invest. Ophthalmol. Vis. Sci. 40 (7): 1343-50. ... The TATA-box binding protein (TBP) is required for the initiation of transcription by RNA polymerases I, II and III, from ... The TATA-binding protein (TBP) is a general transcription factor that binds specifically to a DNA sequence called the TATA box ...
This gene encodes a protein that is a member of the SCF ubiquitin ligase protein complex. It binds to F-box proteins (proteins ... Yam CH, Ng RW, Siu WY, Lau AW, Poon RY (1999). "Regulation of cyclin A-Cdk2 by SCF component Skp1 and F-box protein Skp2". Mol ... Ng RW, Arooz T, Yam CH, Chan IW, Lau AW, Poon RY (1998). "Characterization of the cullin and F-box protein partner Skp1". FEBS ... Ng RW, Arooz T, Yam CH, Chan IW, Lau AW, Poon RY (November 1998). "Characterization of the cullin and F-box protein partner ...
Most pages in SCOP contain a search box. Entering "trypsin +human" retrieves several proteins, including the protein ... Protein structure, Protein folds, Protein classification, Protein superfamilies, Science and technology in Cambridgeshire). ... For simple proteins, it can be the entire protein. The broadest groups on SCOP version 1.75 are the protein fold classes. These ... The source of protein structures is the Protein Data Bank. The unit of classification of structure in SCOP is the protein ...
FOX (forkhead box) proteins are a family of transcription factors that play important roles in regulating the expression of ... Forkhead proteins are a subgroup of the helix-turn-helix class of proteins. Many genes encoding FOX proteins have been ... The defining feature of FOX proteins is the forkhead box, a sequence of 80 to 100 amino acids forming a motif that binds to DNA ... Forkhead+Box+Proteins at the U.S. National Library of Medicine Medical Subject Headings (MeSH) (Articles with short description ...
The protein encoded by this gene contains a SH2 domain and a SOCS box domain. The protein thus belongs to the cytokine-induced ... Cytokine-inducible SH2-containing protein is a protein that in humans is encoded by the CISH gene. CISH orthologs have been ... "Functional association of cytokine-induced SH2 protein and protein kinase C in activated T cells". International Immunology. 15 ... Kile BT, Schulman BA, Alexander WS, Nicola NA, Martin HM, Hilton DJ (May 2002). "The SOCS box: a tale of destruction and ...
Cdc4 (cell division control protein 4) is a substrate recognition component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ... "F-box" motif)) and 7 WD repeats. Cdc4 is a WD-40 repeat F-box protein. Like all members of this family, it contains a conserved ... Almeida AD, Wise HM, Hindley CJ, Slevin MK, Hartley RS, Philpott A (2010). "The F-box protein Cdc4/Fbxw7 is a novel regulator ... The corresponding gene product is the F-box/WD repeat-containing protein 7.[citation needed] In the nematode C. elegans, the ...
Cyclins are molecules that possess a consensus domain called the 'cyclin box.' In mammalian cells, 9 cyclin species have been ... The other domain is the N terminal kinase domain which is a functional Ser/Thr protein kinase. The N-terminal kinase domain is ... Cyclin G-associated kinase is a two domain cystolic protein. The domain of interest is the C-terminal domain which consists of ... In all eukaryotes, the cell cycle is governed by cyclin-dependent protein kinases (CDKs), whose activities are regulated by ...
Liu F, Putnam A, Jankowsky E (Dec 2008). "ATP hydrolysis is required for DEAD-box protein recycling but not for duplex ... Protein ZGRF1 is a protein encoded in the human by the ZGRF1 gene also known as C4orf21, that has a weight of 236.6 kDa. The ... "Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa". Cell. 125 (2): 287-300. doi:10.1016/j.cell.2006.01 ... A majority of these proteins are in the RNA helicase family. There are no known paralogs to the large N-terminal portion of the ...
The DNA binding domain recognizes and binds a 17-bp sequence (CENP-B box) in the centromeric alpha satellite DNA. This protein ... In humans, centromere protein B is encoded by the CENPB gene. Centromere protein B is a highly conserved protein that ... Centromere protein B also known as major centromere autoantigen B is an autoantigen protein of the cell nucleus. ... Lomonte P, Morency E (February 2007). "Centromeric protein CENP-B proteasomal degradation induced by the viral protein ICP0". ...
U3-box: Site in which Act1 can perform the ubiquitination of other proteins. TRAF domains (residues 35 to 42, and 333 to 337): ... Act 1 adaptor protein (Act 1) is an essential intermediate in the interleukin-17 pathway. The IL-17 protein is a pro- ... They indeed use the adaptor Act1 protein, and TRAF family protein in order to activate the nuclear factor-kappa B (NF-κB), a ... Subsequently, Act1 recruits TRAF6 through its TRAF domain and ubiquitinates this protein. Once this protein is ubiquitinated, ...
... the TAF15 protein encoded by the TAF15 gene (also termed the TATA-box binding protein associated factor 15, Npl3, RBP56, TAF2N ... The FET protein family (also known as the TET protein family) consists of three similarly structured and functioning proteins. ... the EWSR1 protein encoded by the EWSR1 gene (also termed the Ewing sarcoma RNA binding protein, EWS RNA binding protein 1, or ... FET proteins are abundantly expressed in virtually all tissues examined. They are RNA-binding proteins. By binding to their RNA ...
"The HMG-box transcription factor HBP1 is targeted by the pocket proteins and E1A". Oncogene. 14 (22): 2721-8. doi:10.1038/sj. ... Retinoblastoma-like protein 2 is a protein that in humans is encoded by the RBL2 gene. Retinoblastoma-like protein 2 has been ... Li Y, Graham C, Lacy S, Duncan AM, Whyte P (Dec 1993). "The adenovirus E1A-associated 130-kD protein is encoded by a member of ... Li Y, Graham C, Lacy S, Duncan AM, Whyte P (Dec 1993). "The adenovirus E1A-associated 130-kD protein is encoded by a member of ...
The zinc finger protein 226 is also known as the Kruppel-associated box protein. Within humans, the ZNF226 gene is found on the ... This protein contains the Kruppel associated box A (KRAB-A) domain, which functions as a transcriptional repressor. However, ... The FUS protein was another one found with a binding site on a predicted stem loop. The gene encodes for a protein which ... The RBMX protein is a homolog of the RBMY protein involved in sperm production. It is also known to promote transcription of a ...
... proteins. However, in contrast to E-box-binding HLH proteins, an arginine residue is replaced with tyrosine making them capable ... These proteins work with asymmetric sterol regulatory element (StRE). SREBPs have a structure similar to E-box-binding helix- ... SCAP, in turn, can bind reversibly with another ER-resident membrane protein, INSIG. In the presence of sterols, which bind to ... Then, SCAP undergoes a conformational change that exposes a portion of the protein ('MELADL') that signals it to be included as ...
"The HMG-box transcription factor HBP1 is targeted by the pocket proteins and E1A". Oncogene. 14 (22): 2721-8. doi:10.1038/sj. ... The retinoblastoma protein (protein name abbreviated Rb; gene name abbreviated Rb, RB or RB1) is a tumor suppressor protein ... E2F1 to E2F5 are known to associate with proteins in the pRb-family of proteins while E2F6 and E2F7 are independent of pRb. ... RB/E2F-family proteins repress transcription. pRb is a multifunctional protein with many binding and phosphorylation sites. ...
All RGS proteins contain an RGS-box (or RGS domain), which is required for activity. Some small RGS proteins such as RGS1 and ... Thus G proteins and GTPase accelerating proteins appear to have evolved before any known G protein activator. RGS domains can ... Regulators of G protein signaling (RGS) are protein structural domains or the proteins that contain these domains, that ... 1] in PROSITE Portal: Biology (CS1 errors: periodical ignored, G proteins, Protein domains, Peripheral membrane proteins). ...
Diagrams illustrate receptor sequences (using snake-plots and helix box diagrams) and relationships (phylogenetic trees). ... The GPCRdb database is the main repository of curated data for G protein-coupled receptors (GPCRs). It integrates various web ... G protein-coupled receptors Pandy-Szekeres, Gaspar; Munk, Christian; Tsonkov, Tsonko; Mordalski, Stefan; Harpsoe, Kasper; ... The GPCRdb browsing system is structured on most relevant categories which are: GPCRdb Receptors G Proteins B-Arrestins Biased ...
The encoded protein directly interacts with a DEAD box protein and several spliceosome core proteins. Alternatively spliced ... Gem-associated protein 4 is a protein that in humans is encoded by the GEMIN4 gene. The product of this gene is part of the SMN ... protein and a specific subset of spliceosomal Sm proteins". Hum. Mol. Genet. 9 (13): 1977-86. doi:10.1093/hmg/9.13.1977. PMID ... protein and a specific subset of spliceosomal Sm proteins". Hum. Mol. Genet. 9 (13): 1977-86. doi:10.1093/hmg/9.13.1977. PMID ...
TMEM254 can be seen at the thin red band with the box around, placed at q22.3. TMEM254 consists of ten total exons and is ... Transmembrane protein 254 - Homo sapiens (Human) - TMEM254 gene & protein". "I-TASSER server for protein structure and function ... Transmembrane protein 254 is a transmembrane protein that is encoded by the TMEM254 gene, it is predicted to have many ... Protein - NCBI". "PSORT II Prediction". "TMEM254 (human)". "Tissue expression of TMEM254 - Summary - the Human Protein Atlas". ...
SRY is a member of the SOX (SRY-like box) gene family of DNA-binding proteins. When complexed with the (SF-1) protein, SRY acts ... Sex-determining region Y protein (SRY), or testis-determining factor (TDF), is a DNA-binding protein (also known as gene- ... The SF-1 protein, on its own, leads to minimal transcription of the SOX9 gene in both the XX and XY bipotential gonadal cells ... How these proteins regulate SRY transcription is not clear, but FOG2 and GATA4 mutants have significantly lower levels of SRY ...
Gronenborn, AM; Clore GM (1994). "Identification of N-terminal helix capping boxes by means of 13C chemical shifts". Journal of ... Chemical Shift Random Coil Index Chemical shift index Protein NMR RefDB (chemistry) SHIFTCOR Protein structure database NMR ... Protein chemical shift re-referencing is a post-assignment process of adjusting the assigned NMR chemical shifts to match IUPAC ... A key limitation to the SHIFTCOR approach is that requires that the 3D structure for the target protein be available to assess ...
F-box proteins are proteins containing at least one F-box domain. The first identified F-box protein is one of three components ... interacts directly with the SCF protein Skp1. F-box domains commonly exist in proteins in cancer with other protein-protein ... F-box domain is a protein structural motif of about 50 amino acids that mediates protein-protein interactions. It has consensus ... F-box proteins are involved in many plant vegetative and reproduction growth and development. For example, F-box protein-FOA1 ...
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F-box only protein 5. Names. early mitotic inhibitor 1. f-box only protein 31. ... Fbxo5 F-box protein 5 [Mus musculus] Fbxo5 F-box protein 5 [Mus musculus]. Gene ID:67141 ... mRNA and Protein(s) * XM_036155959.1 → XP_036011852.1 F-box only protein 5 isoform X1 ... mRNA and Protein(s) * NM_025995.2 → NP_080271.2 F-box only protein 5 ...
STIP1 homology and U box-containing protein 1, STUB1 ... U-box: *Protein STIP1 homology and U box-containing protein 1, ... More info for Protein STIP1 homology and U box-containing protein 1, STUB1 from g.44.1.2: U-box. Timeline for Protein STIP1 ... Protein STIP1 homology and U box-containing protein 1, STUB1 from g.44.1.2: U-box appears in SCOPe 2.06. *Protein STIP1 ... Lineage for Protein: STIP1 homology and U box-containing protein 1, STUB1. *Root: SCOPe 2.07 *. Class g: Small proteins [56992 ...
Look for a special coupon for a FREE box of Fiber One ... FREE Box of Fiber One Protein Chewy Bars ... Look for a special coupon for a FREE box of Fiber One Protein Chewy Bars! Load this coupon to your card and enjoy! ...
... By Elaine Watson 13-Nov-2020. - Last updated on 13 ... Seven Sundays deploys sunflower protein in new grain-free boxed cereal line Natures Path launches oatmeal, granola, with ... uses sustainable sunflower protein in its new line of grain-free boxed cereals available nationwide at Whole Foods. The cocoa ... How Tech Transforms Pea Protein Production Roquette , Download Case Study * White Paper: Solving for Sugar Reduction ADM: ...
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Purification and characterization of a protein binding to the SP6 κ promoter : A potential role for CArG-box binding factor-A ... box binding factor.A. An antiserum raised against the protein recognized two different forms indicating either that different ... box binding factor.A. An antiserum raised against the protein recognized two different forms indicating either that different ... box binding factor.A. An antiserum raised against the protein recognized two different forms indicating either that different ...
The technical storage or access that is used exclusively for statistical purposes. The technical storage or access that is used exclusively for anonymous statistical purposes. Without a subpoena, voluntary compliance on the part of your Internet Service Provider, or additional records from a third party, information stored or retrieved for this purpose alone cannot usually be used to identify you. ...
... so why isnt it a major player in the plant-based protein arena? ... "Sunflower protein checks all the boxes as an ideal source of ... Could sunflower protein join the plant-based protein major league? It checks all the boxes says Burcon By Elaine Watson 15- ... Related tags sunflower protein plant-based protein plant protein Sunflower is the worlds third largest oilseed crop behind soy ... Consumer-friendly protein​. So whats attractive about sunflower protein isolates?. "High purity sunflower protein isolates ...
Home » Genetics Box » 6. Protein Factory 6. Protein Factory - Background. Teacher Background. The process of turning DNA into ... Protein - the primary building material of cells. Proteins constitute most of the dry mass of a cell and execute nearly all ... Thus, the protein will fold itself up to protect the water-hating parts of the protein from the surrounding cytosol. In ... DNA - the blue print for construction of specific proteins. A section of DNA that codes for a protein is called a gene. More on ...
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... Zanotti, KJ ; ... Thermodynamics of the fragile X mental retardation protein RGG box interactions with G quartet forming RNA. Login ... FMRP is an RNA binding protein that binds to G quartet forming RNA using its RGG box motif. In this study we have performed a ... Our results also indicate that the G quartet RNA recognition is not a general feature of the RGG box motif but rather carries ...
... and TATA-box-binding protein] or HAP (heterogeneous nuclear ribonucleoprotein A1-interacting protein)}. Here, we show that SLTM ... and TATA-box-binding protein] or HAP (heterogeneous nuclear ribonucleoprotein A1-interacting protein)}. Here, we show that SLTM ... and TATA-box-binding protein] or HAP (heterogeneous nuclear ribonucleoprotein A1-interacting protein)}. Here, we show that SLTM ... and TATA-box-binding protein] or HAP (heterogeneous nuclear ribonucleoprotein A1-interacting protein)}. Here, we show that SLTM ...
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Lys-C retains proteolytic activity under protein denaturing conditions such as 8M urea, which is used to improve digestion of ... This protease can be used alone or in combination with other proteases to produce protein digests for peptide mapping ... proteolytically resistant proteins. Lys-C activity is optimal in the pH range of 7.0-9.0. ... applications or protein identification by peptide mass fingerprinting or MS/MS spectral matching. ...
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BOX Chemi XX6 system to analyse nitrated proteins fluorescently stained with Cy2, Cy3 and Cy5 on 2D DIGE (Difference Gel ... This is providing the researchers with accurate information on changes in proteins and may help to identify biomarkers related ... BOX Chemi XX6 multi-application imager is being utilised by scientists at the University of Brescia for analysing nitrated ... University of Brescia uses G:BOX Chemi XX6 to Detect Nitrated Proteins Research is Helping Identify Biomarkers of Alzheimer. ...
... is an allergic disease with expression predominantly in the GI tract. Whats the ... Box 1. Clues in favor of a specific IgE role in food protein-induced enterocolitis syndrome pathogenesis. *. There are some ... Food Protein-Induced Enterocolitis Syndrome. From Practice to Theory. Stefano Miceli Sopo; Monica Greco; Serena Monaco; ... Avoidance of the offending protein from the diet results in resolution of symptoms. Removal of causative food results in ...
Protein moving out of box during npt simulation" *Maybe reply: bharat gupta: "Re: Re: Protein moving out of box during npt ... Protein moving out of box during npt simulation" *Maybe reply: bharat gupta: "Re: Re: Protein moving out of box during npt ... Re: Re: Protein moving out of box during npt simulation. From: bharat gupta (bharat.85.monu_at_gmail.com). Date: Tue Jul 05 ... Reply: Bjoern Olausson: "Re: Re: Protein moving out of box during npt simulation" *Messages sorted by: [ date ] [ thread ] [ ...
... black box) 5′ to the Gad1 translation start site. Thus, the transgene does not encode an EGFP fusion protein product. EGFP ... 3d, box). Figure 3j-l shows the clear overlap in EGFP and SOM expression in SO of area CA1. Note the O-LM cell-like ... derivative of the autofluorescent protein, green fluorescent protein (EGFP) (Morise et al., 1974; Prasher et al., 1992; Cormack ... The portion of theGad1 gene used consisted of ∼1.2 kbp of upstream regulatory sequence (mGad1urs;gray box) 5′ to the major ...
The most enriched proteins released were the nucleosomal histones, which have previously been identified as damage-associated ... We identified 231 proteins released from actomyosin contraction-dependent blebs and apoptotic bodies by adapted SILAC (stable ... Blebbing, apoptotic body formation and protein release during early apoptosis are dependent on ROCK and myosin ATPase activity ... which allows release of proteins that may affect the proximal microenvironment before the catastrophic loss of membrane ...
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New technique opens the door for studies of countless hard-to-crystallize proteins involved in health and disease. ... PO Box 5000. Upton, NY 11973-5000. (631) 344-8000. Contact us ... flexible proteins, and many complex human proteins," said ... Deciphering protein structures. Protein crystallography has been a dominant method for solving protein structures since 1958, ... "The method we developed can handle small protein crystals, but it can also be used for any size protein crystals, any time you ...
Atomic level snapshots show how one key enzyme modifies a protein involved in turning genes on or off inside cells, potentially ... PO Box 5000. Upton, NY 11973-5000. (631) 344-8000. Contact us ... Its a protein chain that spans the cell membrane with ... "We set out to do just that-to find out what features in the Notch protein Rumi is looking for and how it puts a sugar (glucose ... Details of the enzyme-protein interaction. Lis team studied samples of a fruit-fly derived version of Rumi in complex with a ...
  • There are other examples of proteins modified by other simple sugars, but Rumi is the first enzyme known to specifically add glucose. (bnl.gov)
  • Many of these items are usually loaded with saturated fat, added sugars, and many types of preservatives, and they often lack protein, fiber, or other nutrient-dense ingredients. (eatthis.com)
  • This is a game changer in the plant protein arena and should set a new benchmark for sunflower protein ingredients. (foodnavigator-usa.com)
  • With this investment, Burcon and Pristine Gourmet can accelerate the development of value-added premium protein ingredients coming from a by-product normally used as animal feed. (foodnavigator-usa.com)
  • Only premium ingredients are used to deliver a clean whey protein taste without any junk sweeteners. (healthsmartfoods.com)
  • F-box domain is a protein structural motif of about 50 amino acids that mediates protein-protein interactions. (wikipedia.org)
  • Proteins are long single stranded chains constructed of 20 different building blocks called amino acids. (mysciencebox.org)
  • Depending on the sequence of amino acids, some parts of the protein like water and some curl away from it. (mysciencebox.org)
  • We identified 231 proteins released from actomyosin contraction-dependent blebs and apoptotic bodies by adapted SILAC (stable isotope labeling with amino acids in cell culture) combined with mass spectrometry analysis. (nature.com)
  • Many vegetarians supplement their diet with soy protein because it contains all the essential amino acids. (allstarhealth.com)
  • Pea protein provides the same essential amino acids soy protein does, without the side effects! (allstarhealth.com)
  • Either at genomic or at proteomic level, mutations have significant impact on normal gene or protein function, and human diseases could be associated with mutations like nonsynonymous single-nucleotide variations (nsSNVs) on amino acids. (hindawi.com)
  • Our technique really opens the door to dealing with microcrystals that have been previously inaccessible, including difficult-to-crystallize cell-surface receptors and other membrane proteins, flexible proteins, and many complex human proteins," said Brookhaven Lab scientist Qun Liu, the corresponding author on the study, which was published on May 3 in IUCrJ, a journal of the International Union of Crystallography. (bnl.gov)
  • In plants, many F-box proteins are represented in gene networks broadly regulated by microRNA-mediated gene silencing via RNA interference. (wikipedia.org)
  • A section of DNA that codes for a protein is called a gene. (mysciencebox.org)
  • The abnormal hypermethylation of the expanded CGG repeats causes the transcriptional silencing of the FMR1 gene and, consequently, the loss of the fragile X mental retardation protein (FMRP). (auckland.ac.nz)
  • Thus the inhibitory effects of SLTM on gene expression appear to result from generalized down-regulation of mRNA synthesis and initiation of apoptosis consequent upon overexpressing the protein. (bris.ac.uk)
  • The existence of mRNAs retaining both nuclear cap binding protein and EJC in the distal sites of neuronal processes suggests that some localized mRNAs have not yet undergone the "very first translation," which contribute to the spatio-temporal regulation of gene expression. (frontiersin.org)
  • methylation at certain residues of histones can regulate gene expression [ 4 ], and glycosylation is responsible for targeting substrates and changing protein half-life [ 2 ]. (hindawi.com)
  • Yet how gene mutations affect protein activities through posttranslational modification sites have not been widely studied. (hindawi.com)
  • During embryonic development, the PAX2 gene provides instructions for producing a protein that is involved in the formation of the eyes, ears, brain and spinal cord (central nervous system), kidneys, urinary tract, and genital tract. (medlineplus.gov)
  • The effects of CAKUT-associated PAX2 gene variants are not fully understood, but it is likely that they impair the function of the PAX2 protein, disrupting formation of the kidneys and urinary system during embryonic development. (medlineplus.gov)
  • Mutations of this gene introduce a premature stop codon and result in truncated protein versions. (medscape.com)
  • The T-box gene family is a group of related genes that play a critical role in human embryonic development. (medscape.com)
  • id":10972849036,"title":"ProtiDiet Protein Shake - Chocolate - 7\/Box","handle":"protidiet-shake-chocolate-7-box","description":"\u003cp\u003eThis delicious chocolate shake has 15 grams of protein in addition to 4 grams of fiber and 20% of your daily calcium. (nashuanutrition.com)
  • This delicious chocolate shake has 15 grams of protein in addition to 4 grams of fiber and 20% of your daily calcium. (nashuanutrition.com)
  • Raw Organic Protein is smooth, creamy and delicious. (vitaminlife.com)
  • Legendary Protein Sweet Roll is a delicious on-the-go snack that provides you with 20 grams of protein and 5 grams of net carbs. (mysupplementstore.com)
  • Legendary Tasty Pastry Cake Style 12/BOX If you are looking for a delicious snack, check out Legendary Tasty Pastry Cake Style. (mysupplementstore.com)
  • IWON Protein Stix 8/1.5oz Sweet Dijon Iwon Protein Stixs are delicious on-the-go snacks that are made with 10 grams of protein and 5 grams of fiber. (mysupplementstore.com)
  • this delicious brownie snack is also made with Whey Protein to help boost. (mysupplementstore.com)
  • Barebells Bar 12/Box If you are looking for a delicious, protein filled snack, check out Barebells Bar! (mysupplementstore.com)
  • Delicious tasting high protein bars that taste like chocolate ship cookie dough with milk chocolate inclusions throughout the dough. (healthsmartfoods.com)
  • These large 64g protein bars deliver a very clean, delicious taste with only the highest quality Whey Protein and Milk Proteins! (healthsmartfoods.com)
  • One Box of 12 - 64g High Protein Bars Delicious tasting uncoated protein bars made with cookie dough protein dough. (healthsmartfoods.com)
  • Delicious tasting uncoated protein bars made with peanut butter protein dough and variegated with peanut butter and milk chocolate crisp. (healthsmartfoods.com)
  • Delicious tasting high protein bars that taste like yellow cake flavored dough with white chocolate inclusions throughout the dough. (healthsmartfoods.com)
  • Delicious tasting high protein bars with chocolate dough and dark chocolate and white chocolate inclusions throughout. (healthsmartfoods.com)
  • Our USDA organic plant-based protein is delicious, additive-free, and a genuinely energy-packed addition to any lifestyle. (woot.com)
  • Announcing our 5-day vegan cleanse plan with our delicious vegan soups, cold-pressed juices and protein powder. (veginout.com)
  • And if you know what to order or which drive-thru to visit, you can even find some delicious, high-protein fast-food breakfasts to help you meet your protein goals for the day . (eatthis.com)
  • It has 17 grams of protein while only providing 230 calories, and most importantly, it tastes delicious and will keep you satisfied as you go through your day. (eatthis.com)
  • Even though you may be thinking of a hamburger or frosty when you consider heading to Wendy's, you'll also be able to find a handful of delicious breakfast options, too-some of which are higher in protein and not terrible in the nutrition department. (eatthis.com)
  • If you're looking for a breakfast that's both delicious and protein-packed, check out Einstein Bros Bagels Santa Fe Egg White Breakfast Sandwich ," suggests Jessie Hulsey RD, LD . (eatthis.com)
  • With its exceptional nutritional profile and so many delicious flavors, Built Bar is the favorite protein bar of many discerning fitness trainers and fitness enthusiasts alike. (netrition.com)
  • In this study we have performed a thermodynamic analysis of the interactions between the FMRP RGG box domain and Sc1, an RNA molecule which had been previously shown to be bound with high affinity by both the full-length FMRP and by its RGG box domain. (auckland.ac.nz)
  • To determine a protein structure, scientists measure how x-rays like those generated at NSLS-II diffract, or bounce off, the atoms in an ordered crystalline lattice consisting of many copies of the same protein molecule all arrayed the same way. (bnl.gov)
  • Our work describes the structure and function of an important enzyme called Rumi, which adds a glucose molecule to several signaling proteins to modify their activities," said the study's lead author, Huilin Li, a biologist at the U.S. Department of Energy's Brookhaven National Laboratory and Stony Brook University. (bnl.gov)
  • Using mAb 4F10 as a probe, the Zta protein could be detected as a 36-kD molecule in L5 cells and as a 38-kD molecule in B95-8 cells, reflecting the fact reported by other laboratories, using rabbit polyclonal antisera, that the Zta protein was variously modified in different host cells. (karger.com)
  • High Protein - 15 Grams Only 100 Calories Low Carb - 7 Net Carbs. (nashuanutrition.com)
  • Barebells Bar is a great tasting protein bar that is made with a whopping 20 grams of protein. (mysupplementstore.com)
  • A Starbucks Chicken & Hummus Protein Box contains 300 calories, 9 grams of fat and 32 grams of carbohydrates. (fastfoodnutrition.org)
  • Every Diesel Protein Bar packs a punch with 16-17 grams of high-quality protein, fueling your muscles and supporting your fitness aspirations. (supplementsource.ca)
  • While this won't add any protein, it will reduce the amount of carbohydrates by 24 grams-worth it if you're watching your carb intake. (purewow.com)
  • Meatless fast-food meals that still contain a decent amount of protein are few and far between, but this Starbucks option is fully vegetarian and has 20 grams of the good stuff. (purewow.com)
  • Another high-protein item at the popular coffee chain is the turkey, provolone and pesto on ciabatta, which contains 32 grams of protein and only 3 grams of sugar. (purewow.com)
  • It has 320 calories with 18 grams of protein, compared to Wendy's Sausage, Egg & Cheese Sandwich, which has 480 calories and 21 grams of protein," says Lara Clevenger MSH, RDN, CPT . (eatthis.com)
  • Packed with a substantial 31 grams of protein from egg whites and turkey sausage, it's a flavorful powerhouse that fuels your body and keeps you satisfied. (eatthis.com)
  • On average 21.4g Protein, 1.4g Fats, 3.7g Carbs and 125cals per bar. (sportsfuel.co.nz)
  • Further, at only 200 calories, they deliver 20g protein with only 3 net carbs and no maltitol! (healthsmartfoods.com)
  • Luckily, there are plenty of restaurant chains with options that offer a boost of satisfying protein (and not just refined carbs). (purewow.com)
  • Luckily, McDonald's McDouble, (aka two beef patties, American cheese, pickles, ketchup, onion and mustard) is relatively low in calories and carbs considering the amount of protein it offers. (purewow.com)
  • The Center for Molecular Protein Science (CMPS) brings together scientists active within the fields of biochemistry, molecular biophysics, structural biology, and physical and theoretical chemistry. (lu.se)
  • The Center for Molecular Protein Science (CMPS) main research areas are within biochemistry, biophysical chemistry and molecular biophysics. (lu.se)
  • We now show that during early apoptosis limited membrane permeabilization occurs in blebs and apoptotic bodies, which allows release of proteins that may affect the proximal microenvironment before the catastrophic loss of membrane integrity during secondary necrosis. (nature.com)
  • These results indicate that limited membrane permeabilization occurs in blebs and apoptotic bodies before secondary necrosis, leading to acute and localized release of immunomodulatory proteins during the early phase of active apoptotic membrane blebbing. (nature.com)
  • 2 , 3 A key feature of apoptosis has been defined as the maintenance of an intact cellular membrane (detectable as exclusion of impermeable dyes such as propidium iodide, PI) throughout the apoptotic program to prevent intracellular protein release and subsequent immunological activation. (nature.com)
  • It's a protein chain that spans the cell membrane with complicated 3D folding-including 36 repeating "beads on a necklace" folds that can each be modified in different ways to affect the protein's overall function. (bnl.gov)
  • TOCP administration conferred calcium and calmodulin dependence on the phosphorylation of a few brain cytosolic proteins and caused an increase in the phosphorylation of a number of other cytosolic and membrane proteins. (cdc.gov)
  • In human cells, under high-iron conditions, two iron atoms stabilise the F-Box FBXL5 and then the complex mediates the ubiquitination of IRP2. (wikipedia.org)
  • Magenta mesh patterns surrounding sulfur atoms intrinsic to the protein (yellow spheres) indicate the anomalous signals that were extracted using low-energy x-ray diffraction of thousands of crystals measuring less than 10 millionths of a meter, the size of a bacterium. (bnl.gov)
  • Scientists sometimes artificially insert heavy atoms such as selenium or platinum into the protein for this purpose. (bnl.gov)
  • But sulfur atoms, which appear naturally throughout protein molecules, can also produce such signals, albeit weaker. (bnl.gov)
  • Even though these anomalous signals are weak, a big crystal usually has enough copies of the protein with enough sulfur atoms to make them measurable. (bnl.gov)
  • Once you know the sulfur positions, you can calculate the phases for the other protein atoms because the relationship between the sulfur and the other atoms is fixed," said Liu. (bnl.gov)
  • But eventually, using intensely bright beams of x-rays at the National Synchrotron Light Source (NSLS) at Brookhaven and the Advanced Photon Source (APS) at Argonne National Laboratory-both DOE Office of Science User Facilities-they gathered sufficient data on the arrangement of the proteins' atoms. (bnl.gov)
  • For starters, protein is important for helping to maintain a speedy metabolism. (eatthis.com)
  • The process of turning DNA into protein is called the "central dogma of molecular biology" because it is the foundation of all modern genetics, biotech and pharmacology. (mysciencebox.org)
  • A cartoon representing the structure of a well-studied plant protein that served as a test case for the newly developed microcrystallography technique. (bnl.gov)
  • Coconut Milk Drink with Cocoa & Plant Protein 100% Natural. (hotukdeals.com)
  • F-box domains commonly exist in proteins in cancer with other protein-protein interaction motifs such as leucine-rich repeats (illustrated in the Figure) and WD repeats, which are thought to mediate interactions with SCF substrates. (wikipedia.org)
  • Through this interaction, mRNAs and their associative proteins form messenger ribonucleoprotein particles (mRNPs) that are actively transported along the cytoskeleton to intracellular destinations. (frontiersin.org)
  • We use the cleanest proteins, including organic peas grown and processed in the USA, plus 13 organic sprouted grains, seeds and legumes, with probiotics and enzymes added to promote comfortable and efficient digestion. (vitaminlife.com)
  • There are 300 calories in a Chicken & Hummus Protein Box from Starbucks. (fastfoodnutrition.org)
  • To burn the 300 calories in a Chicken & Hummus Protein Box, you would have to run for 26 minutes or walk for 43 minutes. (fastfoodnutrition.org)
  • Subway's Fresh Fit menu includes items with higher amounts of protein, plus 400 calories or fewer and two servings of vegetables. (purewow.com)
  • Eating foods that are highly processed and low in protein (like many fast food items) can contribute to things like weight gain, high cholesterol, gut imbalance, and heart complications-but, if you look for high-protein breakfast orders that are also lower in calories, fat, and sodium, you can give yourself a decently healthy start to your day on even the busiest mornings. (eatthis.com)
  • The Classic Bacon, Egg & Cheese Sandwich is a great high-protein option if you're tracking your calories. (eatthis.com)
  • With an impressive 15g of protein, a mere 8g of sugar, and a lean 160 calories per serving, it's the latest addition to BUILT's lineup of delectable, high-protein, low-sugar snacks. (netrition.com)
  • UPTON, NY-Scientists have captured atomic level snapshots showing how one key enzyme modifies a protein involved in turning genes on or off inside cells. (bnl.gov)
  • 4F10 was against the Epstein-Barr virus (EBV) Zta protein and 311 H specifically recognized EBV DNase enzyme. (karger.com)
  • The standard experiment is to separate the proteins, e.g. by 2D gel electrophoresis, digest the proteins with a highly specific enzyme, measure the masses of the peptide fragments with a mass spectrometer (typically a MALDI-TOF mass spectrometer) and then compare the peptide monoisotopic masses with expected monoisotopic masses from a database (protein or DNA database). (lu.se)
  • This product keeps my stomach in check while getting me the amount of protein I need for my 7 days of workouts, keeping my muscle mass stable or growing pending the season I am in. (allstarhealth.com)
  • Farm2table Protein box will be the perfect amount of protein for you. (farm2table.co.uk)
  • Just mix with water and you've got a terrific high protein shake. (nashuanutrition.com)
  • All-in-one protein shake and complete multivitamin. (woot.com)
  • ProtiDiet High Protein Shakes are great for dieting, weight management, or for your post workout protein fix. (nashuanutrition.com)
  • To illustrate our approach, we provide experimental procedures to detect the interaction between plant DNA and two proteins (the AeCRN13 effector from the oomycete Aphanomyces euteiches and the AtWRKY22 defensive transcription factor from Arabidopsis ). (nature.com)
  • Most variants occur in the region of the protein that attaches to DNA, impairing its function as a transcription factor. (medlineplus.gov)
  • Dying cells have been defined as apoptotic by distinguishing features, including cell contraction, nuclear fragmentation, blebbing, apoptotic body formation and maintenance of intact cellular membranes to prevent massive protein release and consequent inflammation. (nature.com)
  • Consequent abnormal expression of the cardiac and limb-specific T-box transcription factors lead to the malformations described in HOS. (medscape.com)
  • Low Sugar Gummy Bears & More - Smart Sweets Candy 12/Box *Smart Sweets have undergone a formula change, and now have a softer texture than before. (mysupplementstore.com)
  • We set out to do just that-to find out what features in the Notch protein Rumi is looking for and how it puts a sugar (glucose) on it. (bnl.gov)
  • Though their choice of chocolate does contribute a small amount of sugar to the bar, Built Bar has found that the fiber and protein present greatly decrease the rate of sugar absorption, giving no noticeable blood sugar spike in either Type 1 or Type 2 diabetics. (netrition.com)
  • Premium, high quality whey protein powder from a leading sports nutrition brand Provides 22 g of protein per serving and is low in sugar. (hotukdeals.com)
  • 2) Box of nutrition facts in brief according to Clause 1.2 of Attachment No.1 of the Notification of Ministry of Public Health : Format and Provision to present nutrition facts which display only total energy, total fat, protein, total carbohydrate, sugar, sodium and cholesterol in addition if such food contains cholesterol amount more than 2 milligrams per serving. (who.int)
  • Two Ets proteins, PU.1 and elf-1, that have previously been shown to bind to an adjacent DNA element were shown to physically interact with CArG- box binding factor.A. An antiserum raised against the protein recognized two different forms indicating either that different splice-forms of CArG-box binding factor-A are expressed, or that the protein is subject to posttranslational modification. (lu.se)
  • Healthy Snacks - Quest Nutrition Quest Protein Bars 12/ Box Have you looked everywhere but can't find a protein bar that actually tastes good, without an ingredient profile that looks like a candy. (mysupplementstore.com)
  • We have determined that the association between the FMRP RGG box and Sc1 RNA is dominated by hydrophobic and hydrogen bond interactions, with minor contributions from electrostatic interactions, and that the FMRP RGG box binding increases the stability of the G quartet RNA structure significantly. (auckland.ac.nz)
  • Interestingly, we found that the G quartet recognition is necessary but not sufficient for the FMRP RGG box binding to this RNA target, indicating that additional interactions of the peptide, possibly with the stem and/or stem-G quartet junction region, are required. (auckland.ac.nz)
  • Various experimental approaches exist for the study of nucleic acid-protein interactions in vitro and in vivo , but the detection of such interactions at the subcellular level remains challenging. (nature.com)
  • Here we describe how to detect nucleic acid-protein interactions in plant leaves by using a fluorescence resonance energy transfer (FRET) approach coupled to fluorescence lifetime imaging microscopy (FLIM). (nature.com)
  • We want to understand the molecular mechanisms of biological processes by exploring the structure, dynamics, interactions and function of proteins. (lu.se)
  • It is formed from an assembly of several different individual proteins with various roles. (mysciencebox.org)
  • DNA-binding proteins (DNA-BPs) and RNA-binding proteins (RNA-BPs) have critical roles in living cells in all kingdoms of life. (nature.com)
  • Protein posttranslational modifications (PTMs) play key roles in a variety of protein activities and cellular processes. (hindawi.com)
  • To carry out these roles, the PAX genes provide instructions for making proteins that attach to specific areas of DNA and help control the activity (expression) of particular genes. (medlineplus.gov)
  • Illustration from Radboud University Nijmegen There are 2 major steps in the protein synthesis process. (mysciencebox.org)
  • This second step of the protein synthesis process is known as translation. (mysciencebox.org)
  • The hexosamine biosynthetic pathway (HBP) generates uridine diphosphate N-acetylglucosamine ( UDP -GlcNAc) for glycan synthesis and O-linked GlcNAc (O-GlcNAc) protein modifications. (bvsalud.org)
  • CMPS conduct basic research on proteins with a strong focus on their molecular characteristics and function. (lu.se)
  • That's why every batch of our Diesel Protein Bars undergoes rigorous testing through the Informed-Choice program to ensure they're free from substances banned by the World Anti-Doping Agency (WADA). (supplementsource.ca)
  • FMRP is an RNA binding protein that binds to G quartet forming RNA using its RGG box motif. (auckland.ac.nz)
  • RFX binds the X1 box of MHC-II promoters. (lu.se)
  • The vegan soups offer a variety of flavors and textures as well as the cold-pressed juices and protein powder. (veginout.com)
  • Seven Sundays - best-known for its New Zealand-style muesli - uses sustainable sunflower protein in its new line of grain-free boxed cereals available nationwide at Whole Foods. (foodnavigator-usa.com)
  • Could sunflower protein join the plant-based protein major league? (foodnavigator-usa.com)
  • Burcon claims its technology can deliver sunflower protein isolates with a 'neutral color and exceptionally bland flavor. (foodnavigator-usa.com)
  • So what's attractive about sunflower protein isolates? (foodnavigator-usa.com)
  • The unique organoleptic and functional properties of sunflower protein isolates make them the ideal candidate for many potential food and beverage applications and in particular, for formulations which require delicate flavors. (foodnavigator-usa.com)
  • Sunflower protein checks all the boxes as an ideal source of plant-based protein ​," added Peter H. Kappel, interim CEO and chairman of the board at Burcon, which has licensed its technology to produce high-purity pea and canola proteins to Merit Functional Foods. (foodnavigator-usa.com)
  • UPTON, NY-Using x-rays to reveal the atomic-scale 3-D structures of proteins has led to countless advances in understanding how these molecules work in bacteria, viruses, plants, and humans-and has guided the development of precision drugs to combat diseases such as cancer and AIDS. (bnl.gov)
  • Prior to the current study, the scientists already knew that Rumi modifies Notch by adding glucose molecules to the protein. (bnl.gov)
  • A cardiomelic developmental field has also been postulated to relate the genetic heterogeneity of HOS (and other similar syndromes) to a cascade of molecules, including the brachyury, sonic hedgehog, bone morphogenetic protein, retinoic acid receptor, and transforming growth factor beta families. (medscape.com)
  • It was first identified in cyclin F. The F-box motif of Skp2, consisting of three alpha-helices, interacts directly with the SCF protein Skp1. (wikipedia.org)
  • Our results also indicate that the G quartet RNA recognition is not a general feature of the RGG box motif but rather carries some sequence, protein and/or RNA, specificity. (auckland.ac.nz)
  • Many promotor sequences contain the sequence TATAAA, known as a TATA box by biologists. (mysciencebox.org)
  • i have used many different protein supplements, that both tastes bad and never blend. (allstarhealth.com)
  • In fact, without the right protein supplements, it can be tough to sustain muscle growth and reach fitness targets. (hotukdeals.com)
  • Formulated with keto friendly macros, we use plant-based protein and energy-boosting MCT oil to help you stay on your journey towards better health. (hihealth.com)
  • But many proteins can't be grown into crystals large enough for their atomic arrangements to be deciphered. (bnl.gov)
  • Protein crystallography has been a dominant method for solving protein structures since 1958, improving over time as x-ray sources have grown more powerful, allowing more precise structure determinations. (bnl.gov)
  • This is providing the researchers with accurate information on changes in proteins and may help to identify biomarkers related to Alzheimer's disease. (labbulletin.com)
  • Researchers in the Department of Molecular and Translational Medicine (DMMT) at theUniversity of Brescia in Italy are using a G:BOX Chemi XX6 system to analyse nitrated proteins fluorescently stained with Cy2, Cy3 and Cy5 on 2D DIGE (Difference Gel Electrophoresis) gels. (labbulletin.com)
  • Since then many researchers in our department have said the system is easy to use so we are very satisfied with the performance of the G:BOX XX6 in our laboratory. (labbulletin.com)
  • PPS focuses on the production and purification of (mainly) recombinant protein reagents for all Swedish researchers. (gu.se)
  • Researchers can access the PPS infrastructure via a common entry-point and obtain individualized support based on their research needs throughout the whole process of protein production and purification. (gu.se)
  • Although becoming less commonly used, the array production LIMS of previous BASE versions is retained to support researchers with spotting facilities, e.g., protein array production and BAC array printing that may not be commercially available. (lu.se)
  • It is balanced with not only veggies, flavors but also protein intake. (veginout.com)
  • Look for a special coupon for a FREE box of Fiber One Protein Chewy Bars! (yofreesamples.com)
  • The success of a PMF experiment depends on several factors: The noise level in the spectrum, the mass accuracy, the amount and purity of the sample, the number of proteins in the sample, possible post-translational modifications, algorithm accuracy, and (to a considerable extent) operator skill and experience. (lu.se)
  • Heterogeneous population of RNA granules serve as motile units to translocate, store, translate, and degrade mRNAs in the dendrites contain cis -elements and trans -acting factors such as RNA-binding proteins and microRNAs to convey stimulus-, transcript-specific local translation. (frontiersin.org)
  • Can a healthy vegan protein bar taste like cookie dough? (hihealth.com)
  • The lingering chocolate aftertaste - your last impression of the bar - is in sharp contrast to other protein bars which have quite negative aftertastes. (netrition.com)
  • Built Bar is truly a standout among protein bars. (netrition.com)
  • If you encounter product melting issues, place boxes of bars or unopened items in the refrigerator for about an hour. (netrition.com)
  • Li's team studied samples of a fruit-fly derived version of Rumi in complex with a Notch "surrogate"-a human protein with a Notch-like fold-that were provided by Haltiwanger. (bnl.gov)
  • In vivo, large RNAs rely on proteins to fold to their native conformation. (nih.gov)
  • Keep reading to see the full nutrition facts and Weight Watchers points for a Chicken & Hummus Protein Box from Starbucks Coffee. (fastfoodnutrition.org)
  • There are 7 Weight Watchers Freestyle Points, 8 WW SmartPoints and 7 WW PointsPlus in a serving of Chicken & Hummus Protein Box from Starbucks. (fastfoodnutrition.org)
  • According to our website visitors, a Chicken & Hummus Protein Box is a healthy and nutritious option from Starbucks, with 92% of voters finding it to be healthy. (fastfoodnutrition.org)
  • Review the nutrition facts above and then vote on whether you think a Chicken & Hummus Protein Box is healthy or not. (fastfoodnutrition.org)
  • Is the Chicken & Hummus Protein Box healthy? (fastfoodnutrition.org)
  • 92% of voters think the Chicken & Hummus Protein Box is healthy. (fastfoodnutrition.org)
  • Does the Chicken & Hummus Protein Box taste good? (fastfoodnutrition.org)
  • 98% of voters think the Chicken & Hummus Protein Box tastes good. (fastfoodnutrition.org)
  • a Starbucks Chicken & Hummus Protein Box contains gluten, milk and wheat. (fastfoodnutrition.org)
  • Select a second item to compare to the Chicken & Hummus Protein Box from Starbucks. (fastfoodnutrition.org)
  • Another high-protein salad option is Chick-Fil-A's classic Market Salad topped with grilled chicken. (purewow.com)
  • 90%) sunflower proteins, with neutral color and exceptionally bland flavor. (foodnavigator-usa.com)
  • Built Bar's perfectly tempered dark chocolate mixes with their naturally flavored protein base to produce a flavor combination reminiscent of high-quality candy or dessert. (netrition.com)
  • PTMs are involved in many protein activities and cellular processes, such as protein folding, stability, conformation, and some significant regulatory mechanisms [ 1 ]. (hindawi.com)
  • Inactivation of TCF7L2 protein attained by removing the high-mobility group (HMG)-box DNA binding domain in mature adipocytes in vivo leads to whole-body glucose intolerance and hepatic insulin resistance. (medscape.com)
  • A homeodomain protein that interacts with TATA-BOX BINDING PROTEIN. (bvsalud.org)
  • Blebbing, apoptotic body formation and protein release during early apoptosis are dependent on ROCK and myosin ATPase activity to drive actomyosin contraction. (nature.com)
  • This means we have to have sensitive detection with an imager that can visualise nanogram amounts of protein. (labbulletin.com)
  • Find answers in Plant-based protein in focus: From Pongamia to chickepeas ​​​ ​, part of FoodNavigator's global Positive Nutrition ​​​ ​virtual series, now available on demand. (foodnavigator-usa.com)
  • Now Foods Pea Protein Nutrition 2 Pounds Vegan Friendly Unflavored Introducing an incredibly Pure, unflavored Non-GMO, Vegetable Protein from NOW Foods! (mysupplementstore.com)
  • This Starbucks sandwich is a great option for a high-protein breakfast on the go," says Brittany DeLaurentis, MPH, RD, CSO, LD , founder of Brittany Lynn Nutrition . (eatthis.com)
  • In case of food labels according to 3(2) display nutrition claims, utilizing value to promote sale or specify consumer groups in sale promotion shall display with a box of full text of nutrition facts according to Clause 1.1 of Attachment No.1: Format and Provisions of displaying of nutrition facts box of the Notification of Ministry of Public Health, Re: Nutrition Label. (who.int)