Rod Cell Outer Segment
Retinal Rod Photoreceptor Cells
GTP-Binding Protein Regulators
Cyclic Nucleotide Phosphodiesterases, Type 6
Molecular Sequence Data
Tandem Repeat Sequences
G-Protein-Coupled Receptor Kinase 1
Repetitive Sequences, Nucleic Acid
Adenosine Diphosphate Ribose
Amino Acid Sequence
GTP-Binding Protein alpha Subunits
Heterotrimeric GTP-Binding Proteins
Retinal Cone Photoreceptor Cells
Trinucleotide Repeat Expansion
Virulence Factors, Bordetella
Repetitive Sequences, Amino Acid
Receptors, Adrenergic, beta
Photoreceptor Cells, Vertebrate
GTP-Binding Protein beta Subunits
Nucleoside Diphosphate Sugars
Inverted Repeat Sequences
DNA Repeat Expansion
Transforming Growth Factor beta
Retinal Photoreceptor Cell Outer Segment
Sequence Homology, Amino Acid
The human F box protein beta-Trcp associates with the Cul1/Skp1 complex and regulates the stability of beta-catenin. (1/185)Ubiquitin-conjugation targets numerous cellular regulators for proteasome-mediated degradation. Thus, the identification of ubiquitin ligases and their physiological substrates is crucially important, especially for those cases in which aberrant levels of regulatory proteins (e.g., beta-catenin, p27) result from a deregulated ubiquitination pathway. In yeast, the proteolysis of several G1 regulators is controlled by ubiquitin ligases (or SCFs) formed by three subunits: Skp1, Cul A (Cdc53), and one of many F-box proteins. Specific F-box proteins (Fbps) recruit different substrates to the SCF. Although many Fbps have been identified in mammals, their specific substrates and the existence of multiple SCFs have not yet been reported. We have found that one human Fbp, beta-Trcp (beta-Transducin repeat containing protein), does indeed form a novel SCF with human Skp1 and Cul1. Consistent with recent reports indicating that Xenopus and Drosophila beta-Trcp homologs act as negative regulators of the Wnt/beta-catenin signaling pathway, we report here that human beta-Trcp interacts with beta-catenin in vivo. Furthermore, beta-catenin is specifically stabilized in vivo by the expression of a dominant negative beta-Trcp. These results indicate that the Cul1/Skp1/beta-Trcp complex forms a ubiquitin ligase that mediates the degradation of beta-catenin. (+info)
The F-box protein beta-TrCP associates with phosphorylated beta-catenin and regulates its activity in the cell. (2/185)Defects in beta-catenin regulation contribute to the neoplastic transformation of mammalian cells. Dysregulation of beta-catenin can result from missense mutations that affect critical sites of phosphorylation by glycogen synthase kinase 3beta (GSK3beta). Given that phosphorylation can regulate targeted degradation of beta-catenin by the proteasome, beta-catenin might interact with an E3 ubiquitin ligase complex containing an F-box protein, as is the case for certain cell cycle regulators. Accordingly, disruption of the Drosophila F-box protein Slimb upregulates the beta-catenin homolog Armadillo. We reasoned that the human homologs of Slimb - beta-TrCP and its isoform beta-TrCP2 (KIAA0696) - might interact with beta-catenin. We found that the binding of beta-TrCP to beta-catenin was direct and dependent upon the WD40 repeat sequences in beta-TrCP and on phosphorylation of the GSK3beta sites in beta-catenin. Endogenous beta-catenin and beta-TrCP could be coimmunoprecipitated from mammalian cells. Overexpression of wild-type beta-TrCP in mammalian cells promoted the downregulation of beta-catenin, whereas overexpression of a dominant-negative deletion mutant upregulated beta-catenin protein levels and activated signaling dependent on the transcription factor Tcf. In contrast, beta-TrCP2 did not associate with beta-catenin. We conclude that beta-TrCP is a component of an E3 ubiquitin ligase that is responsible for the targeted degradation of phosphorylated beta-catenin. (+info)
Inducible degradation of IkappaBalpha by the proteasome requires interaction with the F-box protein h-betaTrCP. (3/185)Activation of NF-kappaB transcription factors requires phosphorylation and ubiquitin-proteasome-dependent degradation of IkappaB proteins. We provide evidence that a human F-box protein, h-betaTrCP, a component of Skp1-Cullin-F-box protein (SCF) complexes, a new class of E3 ubiquitin ligases, is essential for inducible degradation of IkappaBalpha. betaTrCP associates with Ser32-Ser36 phosphorylated, but not with unmodified IkappaBalpha or Ser32-Ser36 phosphorylation-deficient mutants. Expression of a F-box-deleted betaTrCP inhibits IkappaBalpha degradation, promotes accumulation of phosphorylated Ser32-Ser36 IkappaBalpha, and prevents NF-kappaB-dependent transcription. Our findings indicate that betaTrCP is the adaptor protein required for IkappaBalpha recognition by the SCFbetaTrCP E3 complex that ubiquitinates IkappaBalpha and makes it a substrate for the proteasome. (+info)
Negative regulation of axis formation and Wnt signaling in Xenopus embryos by the F-box/WD40 protein beta TrCP. (4/185)Screening a maternal Xenopus expression library for activities that synergize with low levels of injected beta-catenin, we have isolated a clone encoding the C-terminal end of x-beta TrCP-2, a highly conserved protein belonging to the F-box/WD40 family of ubiquitin-ligase specificity factors. We show that x-beta TrCP-2 expression reduces dorsal axis formation in Xenopus embryos. A dominant negative mutant lacking the F-box triggers the opposite effect, inducing secondary axes and activating the expression of Wnt responsive genes in ectodermal explants. In light of the existence of beta TrCP transcripts associated with the vegetal cortex, we propose that beta TrCP plays a fundamental role in the establishment of the dorsal determinants during cortical rotation in Xenopus. (+info)
An F-box protein, FWD1, mediates ubiquitin-dependent proteolysis of beta-catenin. (5/185)beta-catenin plays an essential role in the Wingless/Wnt signaling cascade and is a component of the cadherin cell adhesion complex. Deregulation of beta-catenin accumulation as a result of mutations in adenomatous polyposis coli (APC) tumor suppressor protein is believed to initiate colorectal neoplasia. beta-catenin levels are regulated by the ubiquitin-dependent proteolysis system and beta-catenin ubiquitination is preceded by phosphorylation of its N-terminal region by the glycogen synthase kinase-3beta (GSK-3beta)/Axin kinase complex. Here we show that FWD1 (the mouse homologue of Slimb/betaTrCP), an F-box/WD40-repeat protein, specifically formed a multi-molecular complex with beta-catenin, Axin, GSK-3beta and APC. Mutations at the signal-induced phosphorylation site of beta-catenin inhibited its association with FWD1. FWD1 facilitated ubiquitination and promoted degradation of beta-catenin, resulting in reduced cytoplasmic beta-catenin levels. In contrast, a dominant-negative mutant form of FWD1 inhibited the ubiquitination process and stabilized beta-catenin. These results suggest that the Skp1/Cullin/F-box protein FWD1 (SCFFWD1)-ubiquitin ligase complex is involved in beta-catenin ubiquitination and that FWD1 serves as an intracellular receptor for phosphorylated beta-catenin. FWD1 also links the phosphorylation machinery to the ubiquitin-proteasome pathway to ensure prompt and efficient proteolysis of beta-catenin in response to external signals. SCFFWD1 may be critical for tumor development and suppression through regulation of beta-catenin protein stability. (+info)
HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IkappaB and beta-catenin. (6/185)SCF E3 ubiquitin ligases mediate ubiquitination and proteasome-dependent degradation of phosphorylated substrates. We identified a human F-box/WD40 repeats protein (HOS), which is homologous to Slimb/h betaTrCP. Being a part of SCF complex with Skp1 and Cullin1, HOS specifically interacted with the phosphorylated IkappaB and beta-catenin, targeting these proteins for proteasome-dependent degradation in vivo. This targeting required Cullin1 as expression of a mutant Cullin1 abrogated the degradation of IkappaB and of beta-catenin. Mutant HOS which lacks the F-box blocked TNF alpha-induced degradation of IkappaB as well as GSK3beta-mediated degradation of beta-catenin. This mutant also inhibited NF-kappaB transactivation and increased the beta-catenin-dependent transcription activity of Tcf. These results demonstrate that SCF(HOS) E3 ubiquitin ligase regulate both NF-kappaB and beta-catenin signaling pathways. (+info)
beta-Trcp couples beta-catenin phosphorylation-degradation and regulates Xenopus axis formation. (7/185)Regulation of beta-catenin stability is essential for Wnt signal transduction during development and tumorigenesis. It is well known that serine-phosphorylation of beta-catenin by the Axin-glycogen synthase kinase (GSK)-3beta complex targets beta-catenin for ubiquitination-degradation, and mutations at critical phosphoserine residues stabilize beta-catenin and cause human cancers. How beta-catenin phosphorylation results in its degradation is undefined. Here we show that phosphorylated beta-catenin is specifically recognized by beta-Trcp, an F-box/WD40-repeat protein that also associates with Skp1, an essential component of the ubiquitination apparatus. beta-catenin harboring mutations at the critical phosphoserine residues escapes recognition by beta-Trcp, thus providing a molecular explanation for why these mutations cause beta-catenin accumulation that leads to cancer. Inhibition of endogenous beta-Trcp function by a dominant negative mutant stabilizes beta-catenin, activates Wnt/beta-catenin signaling, and induces axis formation in Xenopus embryos. Therefore, beta-Trcp plays a central role in recruiting phosphorylated beta-catenin for degradation and in dorsoventral patterning of the Xenopus embryo. (+info)
A complex containing betaTrCP recruits Cdc34 to catalyse ubiquitination of IkappaBalpha. (8/185)Activation of transcription factor NF-kappaB is accomplished by degradation of its inhibitor IkappaBalpha. Signal induced phosphorylation of IkappaBalpha on serine 32 and 36 targets the protein for ubiquitination on lysine 21 and 22. Here we use a phosphorylated peptide substrate representing residues 20-43 of IkappaBalpha to investigate requirements for ubiquitination of IkappaBalpha. Phosphorylation dependent polyubiquitination is carried out by a multiprotein complex containing betaTrCP, Skp1 and Cdc53 (Cull). In the presence of ubiquitin activating enzyme and the protein complex containing betaTrCP, polyubiquitination of IkappaBalpha peptide was dependent on the presence of Cdc34, while Ubc5 only stimulated mono- and di-ubiquitination. (+info)
Transducin is a protein complex that plays a crucial role in the process of vision. It is activated by the binding of light-sensitive molecules called rhodopsin to a photoreceptor cell in the retina of the eye. When rhodopsin is activated, it causes a conformational change in transducin, which in turn activates a second messenger system that ultimately leads to the opening of ion channels in the cell membrane. This allows ions to flow into the cell, which generates an electrical signal that is transmitted to the brain and interpreted as visual information.
Rhodopsin is a protein found in the retina of the eye that is responsible for the process of vision in low light conditions. It is a type of photopigment that is sensitive to light in the short-wavelength region of the visible spectrum, which corresponds to blue and violet light. When light strikes the rhodopsin molecules, it causes a chemical change in the protein that triggers a series of events that ultimately leads to the transmission of visual information to the brain. Rhodopsin is essential for night vision and plays a critical role in the early stages of the visual process.
3',5'-Cyclic-GMP Phosphodiesterases (cGMP-PDEs) are a family of enzymes that play a crucial role in regulating the levels of cyclic guanosine monophosphate (cGMP) in the body. cGMP is a second messenger molecule that is involved in a wide range of cellular processes, including smooth muscle relaxation, neurotransmission, and immune cell function. cGMP-PDEs are responsible for breaking down cGMP into guanosine monophosphate (GMP), thereby terminating the signaling effects of cGMP. There are 11 different subtypes of cGMP-PDEs, each with different tissue distribution and substrate specificity. In the medical field, cGMP-PDEs are of particular interest because they are targeted by a class of drugs called phosphodiesterase inhibitors (PDE inhibitors). PDE inhibitors are used to treat a variety of conditions, including erectile dysfunction, pulmonary hypertension, and glaucoma. By inhibiting cGMP-PDEs, PDE inhibitors increase the levels of cGMP in the body, leading to the desired therapeutic effects.
GTP-binding protein regulators, also known as G protein-coupled receptor (GPCR) regulators, are a class of proteins that modulate the activity of GTP-binding proteins, which are involved in a wide range of cellular signaling pathways. These regulators can either activate or inhibit the activity of GTP-binding proteins, thereby controlling the downstream signaling cascades that they activate. In the medical field, GTP-binding protein regulators are of great interest because they play important roles in many physiological processes, including sensory perception, neurotransmission, and hormone signaling. They are also involved in a number of diseases, including cardiovascular disease, neurological disorders, and cancer. There are several classes of GTP-binding protein regulators, including G protein-coupled receptor kinases (GRKs), arrestins, and G protein-coupled receptor interacting proteins (GIRKs). These regulators can be targeted for therapeutic intervention in the treatment of various diseases, and there is ongoing research to develop drugs that modulate their activity.
Arrestin is a protein that plays a role in regulating the activity of certain receptors in the cell. It is involved in the process of desensitization, which is the decrease in the responsiveness of a receptor to its ligand (the molecule that binds to the receptor and triggers a response). Arrestin helps to internalize and degrade receptors that have been activated by their ligands, which prevents them from continuing to respond to the ligand. This process is important for maintaining the proper functioning of cells and for preventing overstimulation of receptors. Arrestins are found in a variety of cells and are involved in regulating the activity of a number of different receptors, including those for hormones, neurotransmitters, and sensory stimuli.
Cyclic Nucleotide Phosphodiesterases, Type 6 (PDE6) are a family of enzymes that are responsible for breaking down cyclic nucleotides, such as cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP), in the retina of the eye. These enzymes play a crucial role in regulating the transmission of visual signals from the retina to the brain. PDE6 is a heterodimeric enzyme composed of two subunits, alpha and beta, which are encoded by different genes. The alpha subunit contains the catalytic site of the enzyme, while the beta subunit is involved in the regulation of the enzyme's activity. Mutations in the genes encoding PDE6 can cause a group of inherited eye disorders known as cone-rod dystrophies, which affect the photoreceptor cells in the retina responsible for color vision and night vision. These disorders are characterized by progressive vision loss and can lead to blindness in affected individuals.
Guanosine triphosphate (GTP) is a nucleotide that plays a crucial role in various cellular processes, including energy metabolism, signal transduction, and protein synthesis. It is composed of a guanine base, a ribose sugar, and three phosphate groups. In the medical field, GTP is often studied in relation to its role in regulating cellular processes. For example, GTP is a key molecule in the regulation of the actin cytoskeleton, which is responsible for maintaining cell shape and facilitating cell movement. GTP is also involved in the regulation of protein synthesis, as it serves as a substrate for the enzyme guanine nucleotide exchange factor (GEF), which activates the small GTPase protein Rho. In addition, GTP is involved in the regulation of various signaling pathways, including the Ras/MAPK pathway and the PI3K/Akt pathway. These pathways play important roles in regulating cell growth, differentiation, and survival, and are often dysregulated in various diseases, including cancer. Overall, GTP is a critical molecule in cellular metabolism and signaling, and its dysfunction can have significant consequences for cellular function and disease.
GTP phosphohydrolases are a family of enzymes that hydrolyze guanosine triphosphate (GTP) into guanosine diphosphate (GDP) and inorganic phosphate (Pi). These enzymes play a crucial role in regulating various cellular processes, including signal transduction, protein synthesis, and cell division. In the medical field, GTP phosphohydrolases are of particular interest because they are involved in the regulation of many signaling pathways that are implicated in various diseases, including cancer, neurodegenerative disorders, and infectious diseases. For example, the enzyme Rho GTPase activating protein (RhoGAP) is a GTP phosphohydrolase that regulates the activity of Rho GTPases, which are involved in cell migration, cytoskeletal organization, and cell proliferation. Mutations in RhoGAP have been implicated in several human cancers, including breast cancer and glioblastoma. Other examples of GTP phosphohydrolases that are of medical interest include the enzyme GTPase-activating protein (GAP) for heterotrimeric G proteins, which regulates the activity of G protein-coupled receptors (GPCRs), and the enzyme dynamin, which is involved in endocytosis and autophagy. Mutations in these enzymes have been implicated in various diseases, including hypertension, diabetes, and neurodegenerative disorders.
GTP-binding proteins, also known as G proteins, are a family of proteins that play a crucial role in signal transduction in cells. They are involved in a wide range of cellular processes, including cell growth, differentiation, and metabolism. G proteins are composed of three subunits: an alpha subunit, a beta subunit, and a gamma subunit. The alpha subunit is the one that binds to guanosine triphosphate (GTP), a molecule that is involved in regulating the activity of the protein. When GTP binds to the alpha subunit, it causes a conformational change in the protein, which in turn activates or inhibits downstream signaling pathways. G proteins are activated by a variety of extracellular signals, such as hormones, neurotransmitters, and growth factors. Once activated, they can interact with other proteins in the cell, such as enzymes or ion channels, to transmit the signal and initiate a cellular response. G proteins are found in all eukaryotic cells and play a critical role in many physiological processes. They are also involved in a number of diseases, including cancer, neurological disorders, and cardiovascular diseases.
Interleukin-1beta (IL-1β) is a type of cytokine, which is a signaling molecule that plays a crucial role in the immune system. It is produced by various types of immune cells, including macrophages, monocytes, and dendritic cells, in response to infection, injury, or inflammation. IL-1β is involved in the regulation of immune responses, including the activation of T cells, B cells, and natural killer cells. It also promotes the production of other cytokines and chemokines, which help to recruit immune cells to the site of infection or injury. In addition to its role in the immune system, IL-1β has been implicated in a variety of inflammatory and autoimmune diseases, including rheumatoid arthritis, inflammatory bowel disease, and multiple sclerosis. It is also involved in the pathogenesis of certain types of cancer, such as breast cancer and ovarian cancer. Overall, IL-1β is a key mediator of inflammation and immune responses, and its dysregulation has been linked to a range of diseases and conditions.
G-Protein-Coupled Receptor Kinase 1 (GRK1) is a protein that plays a role in regulating the activity of G-protein-coupled receptors (GPCRs) in the human body. GPCRs are a large family of cell surface receptors that are activated by a variety of extracellular signals, such as hormones, neurotransmitters, and sensory stimuli. When a GPCR is activated, it triggers a cascade of intracellular events that ultimately lead to a cellular response. GRK1 is a member of a family of enzymes called G-protein-coupled receptor kinases (GRKs) that phosphorylate activated GPCRs, which in turn leads to the internalization and degradation of the receptor. This process helps to regulate the activity of GPCRs and prevent overstimulation of the cell. GRK1 has been implicated in a number of physiological processes, including vision, hearing, and the regulation of blood pressure. It has also been linked to a number of diseases, including cardiovascular disease, diabetes, and certain types of cancer.
Adenosine diphosphate ribose (ADPR) is a naturally occurring nucleotide that plays a role in various cellular processes, including energy metabolism, signal transduction, and gene expression. It is composed of an adenosine base, a ribose sugar, and two phosphate groups. In the medical field, ADPR is often studied in relation to its role in the regulation of cellular energy metabolism. For example, ADPR is involved in the production of ATP, the primary energy currency of the cell, through a process called substrate-level phosphorylation. ADPR is also involved in the regulation of calcium signaling, which is important for a wide range of cellular processes, including muscle contraction, neurotransmitter release, and gene expression. In addition, ADPR has been implicated in various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. For example, ADPR has been shown to regulate the activity of certain enzymes involved in cell proliferation and survival, which may contribute to the development of cancer. ADPR has also been shown to play a role in the regulation of blood vessel function, which may be important for the prevention and treatment of cardiovascular disease. Finally, ADPR has been implicated in the pathogenesis of neurodegenerative disorders, such as Alzheimer's disease and Parkinson's disease, through its effects on calcium signaling and gene expression.
Eye proteins are proteins that are found in the eye and play important roles in maintaining the structure and function of the eye. These proteins can be found in various parts of the eye, including the cornea, lens, retina, and vitreous humor. Some examples of eye proteins include: 1. Collagen: This is a protein that provides strength and support to the cornea and lens. 2. Alpha-crystallin: This protein is found in the lens and helps to maintain its shape and transparency. 3. Rhodopsin: This protein is found in the retina and is responsible for vision in low light conditions. 4. Vitreous humor proteins: These proteins are found in the vitreous humor, a clear gel-like substance that fills the space between the lens and the retina. They help to maintain the shape of the eye and provide support to the retina. Disruptions in the production or function of these proteins can lead to various eye diseases and conditions, such as cataracts, glaucoma, and age-related macular degeneration. Therefore, understanding the structure and function of eye proteins is important for the development of effective treatments for these conditions.
Guanosine diphosphate (GDP) is a molecule that plays a role in various cellular processes, including metabolism, signal transduction, and gene expression. It is a nucleotide that consists of a guanine base, a ribose sugar, and a phosphate group. In the medical field, GDP is often studied in the context of its role in regulating the activity of enzymes called G-proteins. G-proteins are involved in a wide range of cellular processes, including the transmission of signals from cell surface receptors to intracellular signaling pathways. GDP can bind to G-proteins and inhibit their activity, while guanosine triphosphate (GTP) can activate them. GDP is also involved in the regulation of the activity of enzymes called kinases, which play a key role in cellular signaling and metabolism. GDP can bind to and inhibit the activity of certain kinases, while GTP can activate them. In addition, GDP is a precursor to other important molecules, including guanosine triphosphate (GTP), which is involved in various cellular processes, and guanosine monophosphate (GMP), which is involved in the regulation of blood pressure and the production of nitric oxide. Overall, GDP is an important molecule in the regulation of cellular processes and is the subject of ongoing research in the medical field.
Rod opsins are a type of photopigment found in the retina of the eye. They are responsible for detecting low levels of light and are essential for night vision. Rod opsins are a type of opsin, which is a protein that binds to a molecule called retinal to form a light-sensitive pigment. When light strikes the rod opsin, it causes a chemical reaction that generates an electrical signal, which is then transmitted to the brain via the optic nerve. Rod opsins are found only in the rods, which are specialized cells in the retina that are responsible for detecting low levels of light.
Guanylyl Imidodiphosphate (GMP-ribose-5'-triphosphate, or GTP) is a molecule that plays a crucial role in various cellular processes, including signal transduction, protein synthesis, and cell division. It is a type of nucleotide that is closely related to adenosine triphosphate (ATP), another important energy molecule in the cell. In the medical field, GTP is often studied in the context of its role in regulating the activity of proteins called G-proteins. These proteins are involved in transmitting signals from cell surface receptors to the interior of the cell, and they play a key role in many physiological processes, including the regulation of blood pressure, heart rate, and neurotransmitter release. GTP is also involved in the regulation of protein synthesis, as it is a key component of the initiation complex that forms at the beginning of the translation process. In addition, GTP is involved in the regulation of cell division, as it is required for the proper assembly and function of the mitotic spindle, which is responsible for separating the chromosomes during cell division. Overall, GTP is a critical molecule in many cellular processes, and its dysfunction can lead to a variety of diseases and disorders.
GTP-binding protein alpha subunits, also known as Gα subunits, are a family of proteins that play a crucial role in signal transduction pathways in cells. These proteins are involved in regulating a wide range of cellular processes, including cell growth, differentiation, and metabolism. Gα subunits are part of a larger family of proteins called G-proteins, which are composed of three subunits: an alpha subunit (Gα), a beta subunit (Gβ), and a gamma subunit (Gγ). The Gα subunit is responsible for binding and hydrolyzing guanosine triphosphate (GTP), a molecule that is involved in regulating the activity of many cellular signaling pathways. When a signaling molecule, such as a neurotransmitter or a hormone, binds to a cell surface receptor, it activates a G-protein by causing the Gα subunit to exchange its bound GDP for GTP. This change in the Gα subunit's conformation allows it to interact with and activate downstream effector proteins, such as enzymes or ion channels, which then carry out the specific cellular response to the signaling molecule. Once the signaling event is complete, the Gα subunit hydrolyzes the GTP back to GDP, returning it to its inactive state. This process is tightly regulated to ensure that the signaling pathway is turned off quickly and efficiently. Overall, GTP-binding protein alpha subunits play a critical role in regulating cellular signaling pathways and are involved in many important physiological processes.
In the medical field, macromolecular substances refer to large molecules that are composed of repeating units, such as proteins, carbohydrates, lipids, and nucleic acids. These molecules are essential for many biological processes, including cell signaling, metabolism, and structural support. Macromolecular substances are typically composed of thousands or even millions of atoms, and they can range in size from a few nanometers to several micrometers. They are often found in the form of fibers, sheets, or other complex structures, and they can be found in a variety of biological tissues and fluids. Examples of macromolecular substances in the medical field include: - Proteins: These are large molecules composed of amino acids that are involved in a wide range of biological functions, including enzyme catalysis, structural support, and immune response. - Carbohydrates: These are molecules composed of carbon, hydrogen, and oxygen atoms that are involved in energy storage, cell signaling, and structural support. - Lipids: These are molecules composed of fatty acids and glycerol that are involved in energy storage, cell membrane structure, and signaling. - Nucleic acids: These are molecules composed of nucleotides that are involved in genetic information storage and transfer. Macromolecular substances are important for many medical applications, including drug delivery, tissue engineering, and gene therapy. Understanding the structure and function of these molecules is essential for developing new treatments and therapies for a wide range of diseases and conditions.
Beta 2-Microglobulin (β2M) is a small protein that is produced by most cells in the body, including immune cells such as T cells and B cells. It is a component of the major histocompatibility complex (MHC) class I molecules, which are found on the surface of most cells and are responsible for presenting antigens (foreign substances) to the immune system. In the medical field, β2M is often used as a marker of kidney function. High levels of β2M in the blood can indicate kidney damage or failure, as the kidneys are responsible for removing β2M from the bloodstream. In addition, high levels of β2M have been associated with an increased risk of certain types of cancer, including multiple myeloma and prostate cancer. β2M is also used as a diagnostic tool in the laboratory to help identify and monitor certain diseases and conditions, such as multiple myeloma, autoimmune disorders, and viral infections. It is also used as a component of some types of cancer treatments, such as immunotherapy.
Retinaldehyde is a form of vitamin A that is produced from retinol (vitamin A alcohol) in the body. It is an important molecule in the process of vision, as it is converted into retinal, which is a component of the visual pigment rhodopsin. Retinaldehyde is also involved in the regulation of cell growth and differentiation, and has been shown to have potential therapeutic applications in the treatment of various diseases, including cancer, diabetes, and inflammatory disorders. In the medical field, retinaldehyde is often used as a supplement or in the development of new drugs.
Hydroxylamine is a chemical compound with the formula NH2OH. It is a colorless, highly toxic gas that is used in various industrial applications, including the production of dyes, pharmaceuticals, and explosives. In the medical field, hydroxylamine is not commonly used. However, it has been studied for its potential as an antiviral agent against certain viruses, including HIV and influenza. It is also used as a reagent in analytical chemistry for the determination of certain compounds.
Heterotrimeric GTP-binding proteins, also known as G proteins, are a family of proteins that play a crucial role in signal transduction in cells. They are composed of three subunits: an alpha subunit, a beta subunit, and a gamma subunit. When a signaling molecule, such as a hormone or neurotransmitter, binds to a cell surface receptor, it causes a conformational change in the receptor that leads to the activation of a G protein. The alpha subunit then exchanges GDP (guanosine diphosphate) for GTP (guanosine triphosphate) and dissociates from the beta and gamma subunits. The alpha subunit then binds to and activates an effector protein, such as an enzyme or ion channel, leading to a cellular response. The beta and gamma subunits remain associated and can be recycled to form a new G protein complex. The G protein cycle is tightly regulated and allows cells to respond to a wide range of signaling molecules with precision and specificity. Heterotrimeric G proteins are involved in many physiological processes, including muscle contraction, neurotransmitter release, and the regulation of blood pressure. Mutations in G protein genes can lead to a variety of diseases, including hypertension, diabetes, and neurological disorders.
RGS proteins, also known as regulator of G protein signaling proteins, are a family of proteins that play a crucial role in modulating the activity of G protein-coupled receptors (GPCRs) in the body. GPCRs are a large group of cell surface receptors that respond to a wide range of signals, including hormones, neurotransmitters, and sensory stimuli. RGS proteins bind to the active form of G proteins and accelerate the rate at which the G protein returns to its inactive state, thereby reducing the duration of the signaling response. This process is important for regulating the activity of GPCRs and ensuring that their signaling is tightly controlled. RGS proteins are involved in a wide range of physiological processes, including vision, hearing, smell, taste, and pain sensation. They have also been implicated in a number of diseases, including hypertension, diabetes, and cancer. As such, RGS proteins are an important area of research in the medical field, with potential applications in the development of new drugs and therapies.
Membrane proteins are proteins that are embedded within the lipid bilayer of a cell membrane. They play a crucial role in regulating the movement of substances across the membrane, as well as in cell signaling and communication. There are several types of membrane proteins, including integral membrane proteins, which span the entire membrane, and peripheral membrane proteins, which are only in contact with one or both sides of the membrane. Membrane proteins can be classified based on their function, such as transporters, receptors, channels, and enzymes. They are important for many physiological processes, including nutrient uptake, waste elimination, and cell growth and division.
Pertussis toxin is a protein toxin produced by Bordetella pertussis, the bacterium responsible for whooping cough. It is one of the major virulence factors of B. pertussis and plays a key role in the pathogenesis of the disease. Pertussis toxin is a complex molecule composed of two subunits: the A subunit, which is responsible for its toxic effects, and the B subunit, which is responsible for its binding to host cells. The A subunit of pertussis toxin ADP-ribosylates a specific host cell protein, called the G protein, which is involved in signal transduction pathways. This ADP-ribosylation leads to the inhibition of the G protein, which in turn disrupts normal cellular signaling and causes a variety of toxic effects, including inflammation, cell death, and disruption of the respiratory system. Pertussis toxin is a major contributor to the severity of whooping cough, and it is the target of several vaccines used to prevent the disease. In addition to its role in whooping cough, pertussis toxin has also been studied for its potential use as a therapeutic agent in the treatment of other diseases, such as cancer and autoimmune disorders.
Receptors, Adrenergic, beta (β-adrenergic receptors) are a type of protein found on the surface of cells in the body that bind to and respond to signaling molecules called catecholamines, including adrenaline (epinephrine) and noradrenaline (norepinephrine). These receptors are part of the adrenergic signaling system, which plays a critical role in regulating a wide range of physiological processes, including heart rate, blood pressure, metabolism, and immune function. There are three main types of β-adrenergic receptors: β1, β2, and β3. Each type of receptor is found in different tissues and has different functions. For example, β1 receptors are primarily found in the heart and are responsible for increasing heart rate and contractility. β2 receptors are found in the lungs, blood vessels, and muscles, and are involved in relaxing smooth muscle and increasing blood flow. β3 receptors are found in adipose tissue and are involved in regulating metabolism. Activation of β-adrenergic receptors can have a variety of effects on the body, depending on the specific receptor subtype and the tissue it is found in. For example, activation of β2 receptors in the lungs can cause bronchodilation, which can help to open up airways and improve breathing in people with asthma or other respiratory conditions. Activation of β1 receptors in the heart can increase heart rate and contractility, which can help to improve blood flow and oxygen delivery to the body's tissues. Activation of β3 receptors in adipose tissue can increase metabolism and help to promote weight loss. β-adrenergic receptors are important therapeutic targets for a variety of medical conditions, including heart disease, asthma, and diabetes. Drugs that target these receptors, such as beta blockers and beta agonists, are commonly used to treat these conditions.
Integrin beta3, also known as CD18, is a protein that plays a crucial role in the immune system and blood clotting. It is a subunit of integrin receptors, which are transmembrane proteins that mediate cell-cell and cell-extracellular matrix interactions. In the context of the immune system, integrin beta3 is expressed on the surface of various immune cells, including neutrophils, monocytes, and platelets. It helps these cells to adhere to the endothelium (inner lining of blood vessels) and migrate through the blood vessel walls to sites of inflammation or infection. In the context of blood clotting, integrin beta3 is expressed on the surface of platelets. It plays a critical role in platelet aggregation, which is the process by which platelets stick together to form a plug at the site of a blood vessel injury. Integrin beta3 also helps to activate platelets and promote the formation of a fibrin clot, which stabilizes the platelet plug and prevents further bleeding. Mutations in the gene encoding integrin beta3 can lead to various bleeding disorders, such as Glanzmann thrombasthenia, a rare inherited bleeding disorder characterized by impaired platelet aggregation.
In the medical field, aluminum compounds refer to substances that contain aluminum as a component. Aluminum is a common element found in many minerals and is used in a variety of industrial and medical applications. In the context of medicine, aluminum compounds are often used as antacids to neutralize stomach acid and relieve symptoms of heartburn and indigestion. They may also be used as a component in certain medications, such as antiperspirants and certain types of antacids. However, excessive exposure to aluminum compounds can be harmful to human health. Aluminum has been linked to a number of health problems, including Alzheimer's disease, osteoporosis, and kidney damage. As a result, the use of aluminum compounds in certain medical applications is closely regulated to minimize the risk of adverse effects.
In the medical field, a protein subunit refers to a smaller, functional unit of a larger protein complex. Proteins are made up of chains of amino acids, and these chains can fold into complex three-dimensional structures that perform a wide range of functions in the body. Protein subunits are often formed when two or more protein chains come together to form a larger complex. These subunits can be identical or different, and they can interact with each other in various ways to perform specific functions. For example, the protein hemoglobin, which carries oxygen in red blood cells, is made up of four subunits: two alpha chains and two beta chains. Each of these subunits has a specific structure and function, and they work together to form a functional hemoglobin molecule. In the medical field, understanding the structure and function of protein subunits is important for developing treatments for a wide range of diseases and conditions, including cancer, neurological disorders, and infectious diseases.
GTP-binding protein beta subunits, also known as Gβ subunits, are a type of protein that plays a crucial role in signal transduction pathways in cells. They are a component of heterotrimeric G proteins, which are a family of proteins that are involved in transmitting signals from cell surface receptors to intracellular effector proteins. Gβ subunits are composed of two domains: an amino-terminal domain that interacts with the alpha subunit (Gα) and a carboxy-terminal domain that interacts with the gamma subunit (Gγ). When a signal is received by a cell surface receptor, it causes the exchange of GDP (guanosine diphosphate) for GTP (guanosine triphosphate) on the Gα subunit. This change in the Gα subunit leads to the dissociation of the Gα subunit from the Gβγ dimer, allowing the Gα subunit to activate its downstream effector proteins and the Gβγ dimer to interact with other signaling molecules. Gβ subunits are involved in a wide range of cellular processes, including the regulation of ion channels, the modulation of neurotransmitter release, and the control of cell growth and differentiation. They are also involved in the development and progression of various diseases, including cancer, neurological disorders, and cardiovascular diseases.
Nucleoside diphosphate sugars are a type of sugar molecule that serves as the backbone of nucleic acids, such as DNA and RNA. They are composed of a pentose sugar (ribose or deoxyribose) linked to a nitrogenous base and a phosphate group. The nitrogenous base can be either a purine (adenine or guanine) or a pyrimidine (cytosine, thymine, or uracil). In the medical field, nucleoside diphosphate sugars are important components of nucleic acid metabolism and are involved in various cellular processes, including DNA replication, RNA transcription, and protein synthesis. They are also used as precursors for the synthesis of nucleotides, which are the building blocks of nucleic acids. In addition, nucleoside diphosphate sugars are used in the development of antiviral drugs, as many viruses rely on the host cell's nucleic acid metabolism to replicate. By inhibiting the synthesis of nucleoside diphosphate sugars, these drugs can prevent the replication of the virus and treat viral infections.
Recombinant proteins are proteins that are produced by genetically engineering bacteria, yeast, or other organisms to express a specific gene. These proteins are typically used in medical research and drug development because they can be produced in large quantities and are often more pure and consistent than proteins that are extracted from natural sources. Recombinant proteins can be used for a variety of purposes in medicine, including as diagnostic tools, therapeutic agents, and research tools. For example, recombinant versions of human proteins such as insulin, growth hormones, and clotting factors are used to treat a variety of medical conditions. Recombinant proteins can also be used to study the function of specific genes and proteins, which can help researchers understand the underlying causes of diseases and develop new treatments.
Thionucleotides are a type of nucleotide that contain a sulfur atom in place of the oxygen atom that is typically found in the sugar-phosphate backbone of nucleotides. They are an important component of the genetic material of certain bacteria and archaea, and are also used in the synthesis of certain drugs and other compounds. Thionucleotides are synthesized using a variety of methods, including chemical synthesis and enzymatic synthesis. They have a number of unique properties that make them useful in a variety of applications, including their ability to form stable bonds with other molecules and their ability to undergo a variety of chemical reactions.
Hydroxylamines are a class of organic compounds that contain a hydroxyl group (-OH) bonded to an amine group (-NH2). They are commonly used as oxidizing agents in various chemical reactions, including the synthesis of pharmaceuticals and the treatment of wastewater. In the medical field, hydroxylamines have been studied for their potential therapeutic applications. For example, hydroxylamine hydrochloride has been used as a vasodilator to treat hypertension and angina pectoris. It works by relaxing blood vessels and improving blood flow to the heart. Hydroxylamines have also been investigated as potential antiviral agents against a variety of viruses, including HIV and influenza. They are thought to work by inhibiting viral replication and preventing the virus from infecting host cells. However, hydroxylamines can also be toxic and have been associated with adverse effects, including respiratory distress, nausea, and vomiting. Therefore, their use in the medical field is carefully regulated and monitored to ensure their safety and efficacy.
Transforming Growth Factor beta (TGF-β) is a family of cytokines that play a crucial role in regulating cell growth, differentiation, and migration. TGF-βs are secreted by a variety of cells, including immune cells, fibroblasts, and epithelial cells, and act on neighboring cells to modulate their behavior. TGF-βs have both pro-inflammatory and anti-inflammatory effects, depending on the context in which they are released. They can promote the differentiation of immune cells into effector cells that help to fight infections, but they can also suppress the immune response to prevent excessive inflammation. In addition to their role in immune regulation, TGF-βs are also involved in tissue repair and fibrosis. They can stimulate the production of extracellular matrix proteins, such as collagen, which are essential for tissue repair. However, excessive production of TGF-βs can lead to fibrosis, a condition in which excessive amounts of connective tissue accumulate in the body, leading to organ dysfunction. Overall, TGF-βs are important signaling molecules that play a critical role in regulating a wide range of cellular processes in the body.
Guanine nucleotides are a type of nucleotide that contains the nitrogenous base guanine. They are important components of DNA and RNA, which are the genetic material of all living organisms. In DNA, guanine nucleotides are paired with cytosine nucleotides to form the base pair G-C, which is one of the four possible base pairs in DNA. In RNA, guanine nucleotides are paired with uracil nucleotides to form the base pair G-U. Guanine nucleotides play a crucial role in the structure and function of DNA and RNA, and are involved in many important biological processes, including gene expression, DNA replication, and protein synthesis.
Skatole is a chemical compound that is produced by the breakdown of tryptophan in the human body. It is also known as 3-methylindole or 3-methyl-1H-indole. Skatole is a foul-smelling compound that is often associated with the smell of feces. It is produced by the gut bacteria of some animals, including humans, and is present in small amounts in the urine and feces of these animals. In the medical field, skatole is sometimes used as a diagnostic tool to identify certain types of gastrointestinal disorders, such as inflammatory bowel disease or colon cancer. It is also used as a marker of exposure to certain drugs, such as the anti-inflammatory drug indomethacin.
In the medical field, RNA, Messenger (mRNA) refers to a type of RNA molecule that carries genetic information from DNA in the nucleus of a cell to the ribosomes, where proteins are synthesized. During the process of transcription, the DNA sequence of a gene is copied into a complementary RNA sequence called messenger RNA (mRNA). This mRNA molecule then leaves the nucleus and travels to the cytoplasm of the cell, where it binds to ribosomes and serves as a template for the synthesis of a specific protein. The sequence of nucleotides in the mRNA molecule determines the sequence of amino acids in the protein that is synthesized. Therefore, changes in the sequence of nucleotides in the mRNA molecule can result in changes in the amino acid sequence of the protein, which can affect the function of the protein and potentially lead to disease. mRNA molecules are often used in medical research and therapy as a way to introduce new genetic information into cells. For example, mRNA vaccines work by introducing a small piece of mRNA that encodes for a specific protein, which triggers an immune response in the body.
DNA, or deoxyribonucleic acid, is a molecule that carries genetic information in living organisms. It is composed of four types of nitrogen-containing molecules called nucleotides, which are arranged in a specific sequence to form the genetic code. In the medical field, DNA is often studied as a tool for understanding and diagnosing genetic disorders. Genetic disorders are caused by changes in the DNA sequence that can affect the function of genes, leading to a variety of health problems. By analyzing DNA, doctors and researchers can identify specific genetic mutations that may be responsible for a particular disorder, and develop targeted treatments or therapies to address the underlying cause of the condition. DNA is also used in forensic science to identify individuals based on their unique genetic fingerprint. This is because each person's DNA sequence is unique, and can be used to distinguish one individual from another. DNA analysis is also used in criminal investigations to help solve crimes by linking DNA evidence to suspects or victims.
Phosphoric diester hydrolases are a group of enzymes that catalyze the hydrolysis of phosphoric diesters, which are esters of phosphoric acid. These enzymes are involved in a variety of biological processes, including the breakdown of nucleic acids, the metabolism of lipids, and the regulation of signaling pathways. In the medical field, phosphoric diester hydrolases are important for the proper functioning of the body. For example, they are involved in the breakdown of nucleic acids, which are the building blocks of DNA and RNA. This process is essential for the replication and repair of DNA, as well as the production of proteins from genetic information. Phosphoric diester hydrolases are also involved in the metabolism of lipids, which are a type of fat that is stored in the body. These enzymes help to break down lipids into smaller molecules that can be used for energy or stored for later use. In addition, phosphoric diester hydrolases play a role in the regulation of signaling pathways, which are the communication networks that allow cells to respond to changes in their environment. These enzymes help to control the activity of signaling molecules, which can affect a wide range of cellular processes, including cell growth, differentiation, and death. Overall, phosphoric diester hydrolases are important enzymes that play a variety of roles in the body. They are involved in the breakdown of nucleic acids, the metabolism of lipids, and the regulation of signaling pathways, and are essential for the proper functioning of the body.
Pleckstrin homology domain
Mothers against decapentaplegic homolog 4
G beta-gamma complex
Index of biochemistry articles
Sp4 transcription factor
PWP1 - RPN5 Interaction Summary | BioGRID
SMART: WD40 domain annotation
The miR-15b-Smurf2-HSP27 axis promotes pulmonary fibrosis | Journal of Biomedical Science | Full Text
IGF2BP1 Monoclonal Antibody | Diagenode
Anti-Cheat Bypasser | Triggerbot, Spinbot, Bunny Hop - Alcha Shop
β-TrCP- and Casein Kinase II-Mediated Degradation of Cyclin F Controls Timely Mitotic Progression. - MRC Weatherall Institute...
Búsqueda | Portal Regional de la BVS
Oligomerization of the human immunodeficiency virus type 1 (HIV-1) Vpu protein - a genetic, biochemical and biophysical...
miRNA biomarkers for NPC diagnosis and prognosis - Fijardo - Annals of Nasopharynx Cancer
The human being immunodeficiency virus type 1 (HIV-1) Vpu accessory protein - DNA Ligase Inhibitors with Broad-Spectrum Activity
SCOP 1.73: Domain d2ce9b1: 2ce9 B:434-770
MedlinePlus: Genes: G
AT5G35670 : IQ-domain 33
The canonical WNT-β-catenin pathway is essential for self-renewal growth and survival - Pathways and therapeutic targets in...
Mechanisms of Fetal Membrane Rupture - Jerome Strauss
DeCS 2004 - Novos termos
DeCS 2004 - Nuevos términos
DeCS 2004 - Nuevos términos
DeCS 2004 - Nuevos términos
DeCS 2004 - New terms
DeCS 2004 - Novos termos
DeCS 2004 - Novos termos
DeCS 2004 - New terms
DeCS 2004 - Nuevos términos
DeCS 2004 - New terms
DeCS 2004 - Nuevos términos
DeCS 2004 - New terms
DeCS 2004 - New terms
- WD40 repeats usually assume a 7-8 bladed beta-propeller fold, but proteins have been found with 4 to 16 repeated units, which also form a circularised beta-propeller structure. (embl.de)
- several WD40-containing proteins act as key regulators of plant-specific developmental events. (embl.de)
- There are 1918936 WD40 domains in 345139 proteins in SMART's nrdb database. (embl.de)
- Taxonomic distribution of proteins containing WD40 domain. (embl.de)
- The complete taxonomic breakdown of all proteins with WD40 domain is also avaliable . (embl.de)
- Click on the protein counts, or double click on taxonomic names to display all proteins containing WD40 domain in the selected taxonomic class. (embl.de)
- Folding of proteins with WD-repeats: comparison of six members of the WD-repeat superfamily to the G protein beta subunit. (embl.de)
- Members of this family include the signal-transducing G protein beta subunit, as well as other proteins that regulate signal transduction, transcription, pre-mRNA splicing, cytoskeletal organization, and vesicular fusion. (embl.de)
- Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling. (cusabio.com)
- One question that has remained unanswered is whether the G-protein α-subunit can support signaling without its cognate βγ partner complex. (eneuro.org)
- The visual signal, or photoresponse, is initiated when photoexcited rhodopsin activates the transducin heterotrimer by catalyzing GDP−GTP exchange on its α-subunit (Gα t ). (eneuro.org)
- they are improvement of disease launch from contaminated cells (26 41 47 50 and degradation from the HIV receptor Compact disc4 proteins in the endoplasmic reticulum (ER) (53). (cancer-pictures.org)
- WD-repeat proteins are a large family found in all eukaryotes and are implicated in a variety of functions ranging from signal transduction and transcription regulation to cell cycle control and apoptosis. (embl.de)
- Decreased mRNA expression of SMAD-specific E3 ubiquitin-protein ligase 2 (Smurf2), which is involved in ubiquitin degradation of HSP27, was responsible for the increased expression of pHSP27. (biomedcentral.com)
- SMAD-specific E3 ubiquitin protein ligase 2 (Smurf2), which is a crucial part of the ubiquitin-proteasome pathway, was suggested to be involved in the degradation of HSP27 [ 15 ] without elucidation of a detailed mechanism. (biomedcentral.com)
- Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. (cusabio.com)
- Newer studies claim that Vpu aswell as the Vpu-like activity PHA-848125 of HIV-2 envelope protein works by overcoming a book species-specific host limitation to HIV launch (51). (cancer-pictures.org)
- MiRNA expression is frequently altered during cancer development, associated with dysregulated expression of a plethora of different miRNAs, their biogenesis or processing proteins, such as DROSHA and DICER1 ( 1 ). (amegroups.org)
- The specificity of the proteins is determined by the sequences outside the repeats themselves. (embl.de)
- Besides coding for the normal retroviral Gag Pol and Env protein the HIV-1 genome also encodes the regulatory Tat and Rev protein and the accessories Vif Vpr Vpu and Nef protein (14). (cancer-pictures.org)
- The mammalian genome comprises nuclear DNA (nDNA) derived from both parents and mitochondrial DNA (mtDNA) that is maternally inherited and encodes essential proteins required for oxidative phosphorylation. (regenerativemedicine.net)
- WD-40 repeats (also known as WD or beta-transducin repeats) are short ~40 amino acid motifs, often terminating in a Trp-Asp (W-D) dipeptide. (embl.de)
- Using Vpu proteins from a primary subtype C and the pNL4-3 subtype B isolates of HIV-1, we show oligomerization of the full-length protein as well as its transmembrane (TM) domain by genetic, biochemical and biophysical methods. (biomedcentral.com)
- The human being immunodeficiency virus type 1 (HIV-1) Vpu accessory protein is a transmembrane protein that down regulates CD4 expression and promotes the discharge of new virions. (cancer-pictures.org)
- However, the only studied example of a WD-repeat protein, G beta, synthesized in vitro in a rabbit reticulocyte lysate, is unable to fold into a native structure without its partner protein G gamma. (embl.de)
- The non-WD-repeat amino terminal alpha helix of G beta does not inhibit folding because G beta does not fold even when this region is removed. (embl.de)
- It is not known whether all WD-repeat proteins are unable to fold when synthesized in an in vitro system. (embl.de)
- We show that unlike G beta, several proteins with WD-repeats are able to fold into globular proteins in a rabbit reticulocyte lysate. (embl.de)
- The HIV-1 Vpu protein is an oligomeric integral membrane protein essential for particle release, viral load and CD4 degradation. (biomedcentral.com)
- One such protein is viral protein U (Vpu) that is encoded by HIV-1 but not HIV-2 or the simian immunodeficiency virus (SIV) [ 2 ]. (biomedcentral.com)
- Whether Vpu is a viral pathogenesis factor remains to be established, but compared to HIV-1, closely related retroviruses such as HIV-2 and SIV that lack expression of a fully functional Vpu protein also cause less severe disease outcomes. (biomedcentral.com)
- Therefore the Vpu proteins also plays a part in viral persistence by attenuating immune system reactions during HIV disease. (cancer-pictures.org)
- its steady association with Vpu impacts the Wnt and nuclear element kappa B (NF-κB) signaling pathways (1 5 In HIV-infected cells Vpu can be synthesized from a bicistronic mRNA that also rules for the viral envelope (Env) proteins gp160. (cancer-pictures.org)
Less severe disease1
- Whether Vpu can be a virulence element remains to become established but in comparison to HIV-1 carefully related retroviruses such as for example PHA-848125 HIV-2 and SIV that absence expression of a completely functional Vpu proteins also cause much less severe disease results. (cancer-pictures.org)
- Even though transcriptional regulation of hsp27 is well recognized [ 14 ], few papers focus on degradation mechanisms of HSP27 protein. (biomedcentral.com)
- The family of WD-repeat proteins comprises over 30 different proteins that share a highly conserved repeating motif [Neer, E. J., Schmidt, C. J., Nambudripad, R., & Smith, T. F. (1994) Nature 371, 297-300]. (embl.de)
- The precise regulation of the levels of cyclin proteins is fundamental to coordinate cell division with checkpoints, avoiding genome instability. (ox.ac.uk)
- Our working definition of folding was that the proteins from globular, trypsin-resistant structures because, except for G beta gamma, their functions are not known or cannot be assayed in reticulocyte lysates. (embl.de)
- Keywords: acute myeloid leukemia Beta Catenin Intro β-catenin functions as a co-activator for the T-cell Citalopram Hydrobromide element (TCF) 4/lymphoid enhancer element (LEF) 1 bipartite transcription element in the promoters of the WNT-β-catenin target genes and is implicated in malignancy transformation1. (researchassistantresume.com)
- Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request. (cusabio.com)