MONOMERIC GTP-BINDING PROTEINS that were initially recognized as allosteric activators of the MONO(ADP-RIBOSE) TRANSFERASE of the CHOLERA TOXIN catalytic subunit. They are involved in vesicle trafficking and activation of PHOSPHOLIPASE D. This enzyme was formerly listed as EC 3.6.1.47
ADP-RIBOSYLATION FACTOR 1 is involved in regulating intracellular transport by modulating the interaction of coat proteins with organelle membranes in the early secretory pathway. It is a component of COAT PROTEIN COMPLEX I. This enzyme was formerly listed as EC 3.6.1.47.
A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.
Vesicles formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles are covered with a lattice-like network of coat proteins, such as CLATHRIN, coat protein complex proteins, or CAVEOLINS.
A 700-kDa cytosolic protein complex consisting of seven equimolar subunits (alpha, beta, beta', gamma, delta, epsilon and zeta). COATOMER PROTEIN and ADP-RIBOSYLATION FACTOR 1 are principle components of COAT PROTEIN COMPLEX I and are involved in vesicle transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.
Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.
Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.
A protein complex comprised of COATOMER PROTEIN and ADP RIBOSYLATION FACTOR 1. It is involved in transport of vesicles between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.
A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)
Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.
An ester formed between the aldehydic carbon of RIBOSE and the terminal phosphate of ADENOSINE DIPHOSPHATE. It is produced by the hydrolysis of nicotinamide-adenine dinucleotide (NAD) by a variety of enzymes, some of which transfer an ADP-ribosyl group to target proteins.
An enzyme found mostly in plant tissue. It hydrolyzes glycerophosphatidates with the formation of a phosphatidic acid and a nitrogenous base such as choline. This enzyme also catalyzes transphosphatidylation reactions. EC 3.1.4.4.
Guanosine 5'-(trihydrogen diphosphate), monoanhydride with phosphorothioic acid. A stable GTP analog which enjoys a variety of physiological actions such as stimulation of guanine nucleotide-binding proteins, phosphoinositide hydrolysis, cyclic AMP accumulation, and activation of specific proto-oncogenes.
Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.
Nucleoside Diphosphate Sugars (NDPs) are biomolecules consisting of a nucleoside monophosphate sugar molecule, which is formed from the condensation of a nucleotide and a sugar molecule through a pyrophosphate bond.
Esters formed between the aldehydic carbon of sugars and the terminal phosphate of adenosine diphosphate.
Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
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 pentose active in biological systems usually in its D-form.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
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.
Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.
Transport proteins that carry specific substances in the blood or across cell membranes.
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.
An ENTEROTOXIN from VIBRIO CHOLERAE. It consists of two major protomers, the heavy (H) or A subunit and the B protomer which consists of 5 light (L) or B subunits. The catalytic A subunit is proteolytically cleaved into fragments A1 and A2. The A1 fragment is a MONO(ADP-RIBOSE) TRANSFERASE. The B protomer binds cholera toxin to intestinal epithelial cells, and facilitates the uptake of the A1 fragment. The A1 catalyzed transfer of ADP-RIBOSE to the alpha subunits of heterotrimeric G PROTEINS activates the production of CYCLIC AMP. Increased levels of cyclic AMP are thought to modulate release of fluid and electrolytes from intestinal crypt cells.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
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.
One of the virulence factors produced by BORDETELLA PERTUSSIS. It is a multimeric protein composed of five subunits S1 - S5. S1 contains mono ADPribose transferase activity.
A set of BACTERIAL ADHESINS and TOXINS, BIOLOGICAL produced by BORDETELLA organisms that determine the pathogenesis of BORDETELLA INFECTIONS, such as WHOOPING COUGH. They include filamentous hemagglutinin; FIMBRIAE PROTEINS; pertactin; PERTUSSIS TOXIN; ADENYLATE CYCLASE TOXIN; dermonecrotic toxin; tracheal cytotoxin; Bordetella LIPOPOLYSACCHARIDES; and tracheal colonization factor.
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.
Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
Enzymes that catalyze the transfer of multiple ADP-RIBOSE groups from nicotinamide-adenine dinucleotide (NAD) onto protein targets, thus building up a linear or branched homopolymer of repeating ADP-ribose units i.e., POLY ADENOSINE DIPHOSPHATE RIBOSE.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Toxic proteins produced from the species CLOSTRIDIUM BOTULINUM. The toxins are synthesized as a single peptide chain which is processed into a mature protein consisting of a heavy chain and light chain joined via a disulfide bond. The botulinum toxin light chain is a zinc-dependent protease which is released from the heavy chain upon ENDOCYTOSIS into PRESYNAPTIC NERVE ENDINGS. Once inside the cell the botulinum toxin light chain cleaves specific SNARE proteins which are essential for secretion of ACETYLCHOLINE by SYNAPTIC VESICLES. This inhibition of acetylcholine release results in muscular PARALYSIS.
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
An enzyme of the lyase class that catalyzes the formation of CYCLIC AMP and pyrophosphate from ATP. EC 4.6.1.1.
One of the virulence factors produced by virulent BORDETELLA organisms. It is a bifunctional protein with both ADENYLYL CYCLASES and hemolysin components.
A polynucleotide formed from the ADP-RIBOSE moiety of nicotinamide-adenine dinucleotide (NAD) by POLY(ADP-RIBOSE) POLYMERASES.
A phosphoinositide present in all eukaryotic cells, particularly in the plasma membrane. It is the major substrate for receptor-stimulated phosphoinositidase C, with the consequent formation of inositol 1,4,5-triphosphate and diacylglycerol, and probably also for receptor-stimulated inositol phospholipid 3-kinase. (Kendrew, The Encyclopedia of Molecular Biology, 1994)
Toxic substances formed in or elaborated by bacteria; they are usually proteins with high molecular weight and antigenicity; some are used as antibiotics and some to skin test for the presence of or susceptibility to certain diseases.
The rate dynamics in chemical or physical systems.
A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. They perform functions such as binding to the cell membrane, capturing cargo molecules and promoting the assembly of CLATHRIN. The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found.
A RHO GTP-BINDING PROTEIN involved in regulating signal transduction pathways that control assembly of focal adhesions and actin stress fibers. This enzyme was formerly listed as EC 3.6.1.47.
Proteins prepared by recombinant DNA technology.
One of the early purine analogs showing antineoplastic activity. It functions as an antimetabolite and is easily incorporated into ribonucleic acids.
Thin structures that encapsulate subcellular structures or ORGANELLES in EUKARYOTIC CELLS. They include a variety of membranes associated with the CELL NUCLEUS; the MITOCHONDRIA; the GOLGI APPARATUS; the ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
Established cell cultures that have the potential to propagate indefinitely.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
NAD+ Nucleosidase is an enzyme that catalyzes the breakdown of NAD+ (nicotinamide adenine dinucleotide) into nicotinamide and ADP-ribose, which plays a role in regulating NAD+ levels and modulating cellular signaling pathways.
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.
A group of telomere associated proteins that interact with TRF1 PROTEIN, contain ANKYRIN REPEATS and have poly(ADP-ribose) polymerase activity.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.
A class of nucleotide translocases found abundantly in mitochondria that function as integral components of the inner mitochondrial membrane. They facilitate the exchange of ADP and ATP between the cytosol and the mitochondria, thereby linking the subcellular compartments of ATP production to those of ATP utilization.
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.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

Identification of a new Pyk2 target protein with Arf-GAP activity. (1/429)

Protein tyrosine kinase Pyk2 is activated by a variety of G-protein-coupled receptors and by extracellular signals that elevate intracellular Ca2+ concentration. We have identified a new Pyk2 binding protein designated Pap. Pap is a multidomain protein composed of an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal SH3 domain. We demonstrate that Pap forms a stable complex with Pyk2 and that activation of Pyk2 leads to tyrosine phosphorylation of Pap in living cells. Immunofluorescence experiments demonstrate that Pap is localized in the Golgi apparatus and at the plasma membrane, where it is colocalized with Pyk2. In addition, in vitro recombinant Pap exhibits strong GTPase-activating protein (GAP) activity towards the small GTPases Arf1 and Arf5 and weak activity towards Arf6. Addition of recombinant Pap protein to Golgi preparations prevented Arf-dependent generation of post-Golgi vesicles in vitro. Moreover, overexpression of Pap in cultured cells reduced the constitutive secretion of a marker protein. We propose that Pap functions as a GAP for Arf and that Pyk2 may be involved in regulation of vesicular transport through its interaction with Pap.  (+info)

GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro. (2/429)

Recent cloning of a rat brain phosphatidylinositol 3,4, 5-trisphosphate binding protein, centaurin alpha, identified a novel gene family based on homology to an amino-terminal zinc-binding domain. In Saccharomyces cerevisiae, the protein with the highest homology to centaurin alpha is Gcs1p, the product of the GCS1 gene. GCS1 was originally identified as a gene conditionally required for the reentry of cells into the cell cycle after stationary phase growth. Gcs1p was previously characterized as a guanosine triphosphatase-activating protein for the small guanosine triphosphatase Arf1, and gcs1 mutants displayed vesicle-trafficking defects. Here, we have shown that similar to centaurin alpha, recombinant Gcs1p bound phosphoinositide-based affinity resins with high affinity and specificity. A novel GCS1 disruption strain (gcs1Delta) exhibited morphological defects, as well as mislocalization of cortical actin patches. gcs1Delta was hypersensitive to the actin monomer-sequestering drug, latrunculin-B. Synthetic lethality was observed between null alleles of GCS1 and SLA2, the gene encoding a protein involved in stabilization of the actin cytoskeleton. In addition, synthetic growth defects were observed between null alleles of GCS1 and SAC6, the gene encoding the yeast fimbrin homologue. Recombinant Gcs1p bound to actin filaments, stimulated actin polymerization, and inhibited actin depolymerization in vitro. These data provide in vivo and in vitro evidence that Gcs1p interacts directly with the actin cytoskeleton in S. cerevisiae.  (+info)

EFA6, a sec7 domain-containing exchange factor for ARF6, coordinates membrane recycling and actin cytoskeleton organization. (3/429)

We have identified a human cDNA encoding a novel protein, exchange factor for ARF6 (EFA6), which contains Sec7 and pleckstrin homology domains. EFA6 promotes efficient guanine nucleotide exchange on ARF6 and is distinct from the ARNO family of ARF1 exchange factors. The protein localizes to a dense matrix on the cytoplasmic face of plasma membrane invaginations, induced on its expression. We show that EFA6 regulates endosomal membrane recycling and promotes the redistribution of transferrin receptors to the cell surface. Furthermore, expression of EFA6 induces actin-based membrane ruffles that are inhibited by co-expression of dominant-inhibitory mutant forms of ARF6 or Rac1. Our results demonstrate that by catalyzing nucleotide exchange on ARF6 at the plasma membrane and by regulating Rac1 activation, EFA6 coordinates endocytosis with cytoskeletal rearrangements.  (+info)

Characterization of the regulation of phospholipase D activity in the detergent-insoluble fraction of HL60 cells by protein kinase C and small G-proteins. (4/429)

Phospholipase D (PLD) activity has been shown to be GTP-dependent both in vivo and in vitro. One protein that confers GTP sensitivity to PLD activity in vitro is the low-molecular-mass G-protein ADP-ribosylation factor (Arf). However, members of the Rho family and protein kinase C (PKC) have also been reported to activate PLD in various cell systems. We have characterized the stimulation of PLD in HL60 cell membranes by these proteins. The results demonstrate that a considerable proportion of HL60 PLD activity is located in a detergent-insoluble fraction of the cell membrane that is unlikely to be a caveolae-like domain, but is probably cytoskeletal. This PLD activity required the presence of Arf1, a Rho-family member and PKC for efficient catalysis of the lipid substrate, suggesting that the activity represents PLD1. We show that recombinant human PLD1b is regulated in a similar manner to HL60-membrane PLD, and that PKCalpha and PKCdelta are equally effective PLD activators. Therefore maximum PLD activity requires Arf, a Rho-family member and PKC, emphasizing the high degree of regulation of this enzyme.  (+info)

Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. (5/429)

The crystal structure of the complex of ARF1 GTPase bound to GDP and the catalytic domain of ARF GTPase-activating protein (ARFGAP) has been determined at 1.95 A resolution. The ARFGAP molecule binds to switch 2 and helix alpha3 to orient ARF1 residues for catalysis, but it supplies neither arginine nor other amino acid side chains to the GTPase active site. In the complex, the effector-binding region appears to be unobstructed, suggesting that ARFGAP could stimulate GTP hydrolysis while ARF1 maintains an interaction with its effector, the coatomer complex of COPI-coated vesicles. Biochemical experiments show that coatomer directly participates in the GTPase reaction, accelerating GTP hydrolysis a further 1000-fold in an ARFGAP-dependent manner. Thus, a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.  (+info)

Expression and distribution of adenosine diphosphate-ribosylation factors in the rat kidney. (6/429)

BACKGROUND: Adenosine diphosphate (ADP)-ribosylation factors (ARFs) are small guanosine triphosphatases involved in membrane traffic regulation. Aiming to explore the possible involvement of ARF1 and ARF6 in the reabsorptive properties of the nephron, we evaluated their distribution along the different renal epithelial segments. METHODS: ARFs were detected by immunofluorescence and immunogold cytochemistry on renal sections, using specific anti-ARF antibodies. RESULTS: ARF1 was detected in proximal and distal tubules, thick ascending limbs of Henle's loops, and cortical and medullary collecting ducts. By immunofluorescence, labeling was mostly localized to the cell cytoplasm, particularly in Golgi areas. By electron microscopy, the Golgi apparatus and the endosomal compartment of proximal and distal tubular cells were labeled. ARF6 immunofluorescence was observed in brush border membranes and the cytoplasm of proximal convoluted tubular cells, whereas it was restricted to the apical border of proximal straight tubules. ARF6 immunogold labeling was detected over microvilli and endocytic compartments of proximal tubular cells. CONCLUSIONS: This study demonstrates the following: (a) the heterogeneous distributions of ARF1 and ARF6 along the nephron, (b) the existence of cytosolic and membrane-bound forms for both ARFs, and (c) their association with microvilli and endocytic compartments, suggesting an active participation in renal reabsorption.  (+info)

Purification and cloning of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors. (7/429)

Activation of ADP-ribosylation factors (ARFs), approximately 20-kDa guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking, depends on guanine nucleotide-exchange proteins (GEPs), which accelerate replacement of bound GDP with GTP. Two major families of ARF GEPs are known: approximately 200-kDa molecules that are inhibited by brefeldin A (BFA), a fungal metabolite that blocks protein secretion and causes apparent disintegration of Golgi structure, and approximately 50-kDa GEPs that are insensitive to BFA. We describe here two human brain cDNAs that encode BFA-inhibited GEPs. One is a approximately 209-kDa protein 99.5% identical in deduced amino acid sequence (1, 849 residues) to a BFA-inhibited ARF GEP (p200) from bovine brain. The other smaller protein, which is approximately 74% identical (1, 785 amino acids), represents a previously unknown gene. We propose that the former, p200, be named BIG1 for (brefeldin A-inhibited GEP1) and the second, which encodes a approximately 202-kDa protein, BIG2. A protein containing sequences found in BIG2 had been purified earlier from bovine brain. Human tissues contained a 7.5-kilobase BIG1 mRNA and a 9.4-kilobase BIG2 transcript. The BIG1 and BIG2 genes were localized, respectively, to chromosomes 8 and 20. BIG2, synthesized as a His6 fusion protein in Sf9 cells, accelerated guanosine 5'-3-O-(thio)triphosphate binding by recombinant ARF1, ARF5, and ARF6. It activated native ARF (mixture of ARF1 and ARF3) more effectively than it did any of the nonmyristoylated recombinant ARFs. BIG2 activity was inhibited by BFA in a concentration-dependent manner but not by B17, a structural analog without effects on Golgi function. Although several clones for approximately 50-kDa BFA-insensitive ARF GEPs are known, these new clones for the approximately 200-kDa BIG1 and BIG2 should facilitate characterization of this rather different family of proteins as well as the elucidation of mechanisms of regulation of BFA-sensitive ARF function in Golgi transport.  (+info)

Structural elements of ADP-ribosylation factor 1 required for functional interaction with cytohesin-1. (8/429)

ADP-ribosylation factor 1 (ARF1) is a 20-kDa guanine nucleotide-binding protein involved in vesicular trafficking. Conversion of inactive ARF-GDP to active ARF-GTP is catalyzed by guanine nucleotide exchange proteins such as cytohesin-1. Cytohesin-1 and its Sec7 domain (C-1Sec7) exhibit guanine nucleotide exchange protein activity with ARF1 but not ARF-like protein 1 (ARL1), which is 57% identical in amino acid sequence. With chimeric proteins composed of ARF1 (F) and ARL1 (L) sequences we identified three structural elements responsible for this specificity. Cytohesin-1 increased [35S]guanosine 5'-(gamma-thio)triphosphate binding to L28/F (first 28 residues of L, remainder F) and to a much lesser extent F139/L, and mut13F139/L (F139/L with random sequence in the first 13 positions) but not Delta13ARF1 that lacks the first 13 amino acids; therefore, a nonspecific ARF N terminus was required for cytohesin-1 action. The N terminus was not, however, required for that of C-1Sec7. Both C-1Sec7 and cytohesin-1 effectively released guanosine 5'-(gamma-thio)triphosphate from ARF1, but only C-1Sec7 displaced the nonhydrolyzable GTP analog bound to mut13F139/L, again indicating that structure in addition to the Sec7 domain is involved in cytohesin-1 interaction. Some element(s) of the C-terminal region is also involved, because replacement of the last 42 amino acids with ARL sequence in F139L decreased markedly the interaction with cytohesin-1. Participation of both termini is consistent with the crystallographic structure of ARF in which the two terminal alpha-helices are in close proximity. ARF1 residues 28-50 are also important in the interaction with cytohesin-1; replacement of Lys-38 with Gln, the corresponding residue in ARL1, abolished the ability to serve as substrate for cytohesin-1 or C-1Sec7. These studies have defined multiple structural elements in ARF1, including switch 1 and the N and C termini, that participate in functional interactions with cytohesin-1 (or its catalytic domain C-1Sec7), which were not apparent from crystallographic analysis.  (+info)

ADP-ribosylation factors (ARFs) are a family of small GTP-binding proteins that play a crucial role in intracellular membrane traffic, actin dynamics, and signal transduction. They function as molecular switches, cycling between an active GTP-bound state and an inactive GDP-bound state.

ARFs are involved in the regulation of vesicle formation, budding, and transport, primarily through their ability to activate phospholipase D and recruit coat proteins to membranes. There are six isoforms of ARFs (ARF1-6) that share a high degree of sequence similarity but have distinct cellular functions and subcellular localizations.

ADP-ribosylation factors get their name from the fact that they were originally identified as proteins that become ADP-ribosylated by cholera toxin, an enzyme produced by Vibrio cholerae bacteria. However, this post-translational modification is not required for their cellular functions.

Defects in ARF function have been implicated in various human diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, understanding the regulation and function of ARFs is an important area of research in biology and medicine.

ADP-Ribosylation Factor 1 (ARF1) is a small GTP-binding protein that belongs to the ADP-ribosylation factor family. It plays a crucial role in intracellular membrane traffic, actin dynamics, and signal transduction pathways. ARF1 functions as a molecular switch by cycling between an active GTP-bound state and an inactive GDP-bound state.

In the active state, ARF1 regulates the recruitment of coat proteins to membranes, which facilitates vesicle formation and transport. It also activates phospholipase D, which generates second messengers that regulate various cellular processes. In contrast, in the inactive state, ARF1 is bound to GDP and cannot participate in these functions.

Mutations or dysregulation of ARF1 have been implicated in several human diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, understanding the structure, function, and regulation of ARF1 is essential for developing new therapeutic strategies to treat these conditions.

Brefeldin A is a fungal metabolite that inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus. It disrupts the organization of the Golgi complex and causes the redistribution of its proteins to the endoplasmic reticulum. Brefeldin A is used in research to study various cellular processes, including vesicular transport, protein trafficking, and signal transduction pathways. In medicine, it has been studied as a potential anticancer agent due to its ability to induce apoptosis (programmed cell death) in certain types of cancer cells. However, its clinical use is not yet approved.

Coated vesicles are membrane-bound compartments found within cells that are characterized by a coat of proteins on their cytoplasmic surface. These vesicles play a crucial role in intracellular transport and membrane trafficking, particularly in the process of endocytosis and exocytosis.

Endocytosis is the process by which cells engulf extracellular material, such as nutrients or molecules like receptors, into vesicles that are formed from the plasma membrane. During this process, coated vesicles called clathrin-coated vesicles form around the region of the plasma membrane where endocytosis is taking place. Clathrin, a protein involved in the formation of these vesicles, polymerizes to form a lattice-like structure that curves the membrane into a spherical shape and pinches it off from the plasma membrane.

Exocytosis, on the other hand, is the process by which cells release molecules or vesicles containing molecules to the extracellular space. In this case, coated vesicles called COP-coated vesicles are involved. These vesicles have a different protein coat, composed of coatomer proteins (COP), and they mediate the transport of proteins and lipids between the endoplasmic reticulum, Golgi apparatus, and the plasma membrane.

Coated vesicles are essential for maintaining cellular homeostasis by controlling the movement of molecules in and out of the cell, as well as the proper sorting and targeting of proteins within the cell. Dysfunctions in coated vesicle formation or trafficking have been implicated in various diseases, including neurodegenerative disorders and cancer.

Coatomer is a protein complex that plays a role in the formation of transport vesicles within cells. These vesicles are responsible for carrying proteins and other cargo between different cellular compartments. Coatomer gets its name from the coat-like structure it forms on the surface of budding vesicles. It is composed of several individual protein subunits, known as α-COP, β-COP, γ-COP, δ-COP, ε-COP, ζ-COP, and η-COP. These subunits work together to help recognize and bind to specific proteins, curvature the membrane, and ultimately pinch off the vesicle from the donor compartment.

Coatomer protein is primarily involved in transport between the endoplasmic reticulum (ER) and the Golgi apparatus, but it also plays a role in other intracellular transport processes. Mutations or dysfunction in coatomer proteins have been linked to various diseases, including neurological disorders and cancer.

Guanine Nucleotide Exchange Factors (GEFs) are a group of regulatory proteins that play a crucial role in the activation of GTPases, which are enzymes that regulate various cellular processes such as signal transduction, cytoskeleton reorganization, and vesicle trafficking.

GEFs function by promoting the exchange of guanosine diphosphate (GDP) for guanosine triphosphate (GTP) on GTPases. GTP is the active form of the GTPase, and its binding to the GTPase leads to a conformational change that activates the enzyme's function.

In the absence of GEFs, GTPases remain in their inactive GDP-bound state, and cellular signaling pathways are not activated. Therefore, GEFs play a critical role in regulating the activity of GTPases and ensuring proper signal transduction in cells.

There are many different GEFs that are specific to various GTPase families, including Ras, Rho, and Arf families. Dysregulation of GEFs has been implicated in various diseases, including cancer and neurological disorders.

GTP-binding proteins, also known as G proteins, are a family of molecular switches present in many organisms, including humans. They play a crucial role in signal transduction pathways, particularly those involved in cellular responses to external stimuli such as hormones, neurotransmitters, and sensory signals like light and odorants.

G proteins are composed of three subunits: α, β, and γ. The α-subunit binds GTP (guanosine triphosphate) and acts as the active component of the complex. When a G protein-coupled receptor (GPCR) is activated by an external signal, it triggers a conformational change in the associated G protein, allowing the α-subunit to exchange GDP (guanosine diphosphate) for GTP. This activation leads to dissociation of the G protein complex into the GTP-bound α-subunit and the βγ-subunit pair. Both the α-GTP and βγ subunits can then interact with downstream effectors, such as enzymes or ion channels, to propagate and amplify the signal within the cell.

The intrinsic GTPase activity of the α-subunit eventually hydrolyzes the bound GTP to GDP, which leads to re-association of the α and βγ subunits and termination of the signal. This cycle of activation and inactivation makes G proteins versatile signaling elements that can respond quickly and precisely to changing environmental conditions.

Defects in G protein-mediated signaling pathways have been implicated in various diseases, including cancer, neurological disorders, and cardiovascular diseases. Therefore, understanding the function and regulation of GTP-binding proteins is essential for developing targeted therapeutic strategies.

Coat Protein Complex I (CPCI or COPI) is a protein complex involved in the intracellular transport of proteins within eukaryotic cells. It functions primarily in the retrograde transport of proteins from the Golgi apparatus to the endoplasmic reticulum (ER). The complex is composed of seven subunits, known as alpha, beta, gamma, delta, epsilon, zeta, and eta COPs (coat proteins), which form a cage-like structure around transport vesicles. This coat assists in the selection of cargo proteins, vesicle budding, and subsequent fusion with target membranes during the recycling of ER-derived proteins.

The Golgi apparatus, also known as the Golgi complex or simply the Golgi, is a membrane-bound organelle found in the cytoplasm of most eukaryotic cells. It plays a crucial role in the processing, sorting, and packaging of proteins and lipids for transport to their final destinations within the cell or for secretion outside the cell.

The Golgi apparatus consists of a series of flattened, disc-shaped sacs called cisternae, which are stacked together in a parallel arrangement. These stacks are often interconnected by tubular structures called tubules or vesicles. The Golgi apparatus has two main faces: the cis face, which is closest to the endoplasmic reticulum (ER) and receives proteins and lipids directly from the ER; and the trans face, which is responsible for sorting and dispatching these molecules to their final destinations.

The Golgi apparatus performs several essential functions in the cell:

1. Protein processing: After proteins are synthesized in the ER, they are transported to the cis face of the Golgi apparatus, where they undergo various post-translational modifications, such as glycosylation (the addition of sugar molecules) and sulfation. These modifications help determine the protein's final structure, function, and targeting.
2. Lipid modification: The Golgi apparatus also modifies lipids by adding or removing different functional groups, which can influence their properties and localization within the cell.
3. Protein sorting and packaging: Once proteins and lipids have been processed, they are sorted and packaged into vesicles at the trans face of the Golgi apparatus. These vesicles then transport their cargo to various destinations, such as lysosomes, plasma membrane, or extracellular space.
4. Intracellular transport: The Golgi apparatus serves as a central hub for intracellular trafficking, coordinating the movement of vesicles and other transport carriers between different organelles and cellular compartments.
5. Cell-cell communication: Some proteins that are processed and packaged in the Golgi apparatus are destined for secretion, playing crucial roles in cell-cell communication and maintaining tissue homeostasis.

In summary, the Golgi apparatus is a vital organelle involved in various cellular processes, including post-translational modification, sorting, packaging, and intracellular transport of proteins and lipids. Its proper functioning is essential for maintaining cellular homeostasis and overall organismal health.

GTPase-activating proteins (GAPs) are a group of regulatory proteins that play a crucial role in the regulation of intracellular signaling pathways, particularly those involving GTP-binding proteins. GTPases are enzymes that can bind and hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP). This biochemical reaction is essential for the regulation of various cellular processes, such as signal transduction, vesicle trafficking, and cytoskeleton organization.

GAPs function as negative regulators of GTPases by accelerating the rate of GTP hydrolysis, thereby promoting the inactive GDP-bound state of the GTPase. By doing so, GAPs help terminate GTPase-mediated signaling events and ensure proper control of downstream cellular responses.

There are various families of GAPs, each with specificity towards particular GTPases. Some well-known GAP families include:

1. p50/RhoGAP: Regulates Rho GTPases involved in cytoskeleton organization and cell migration.
2. GIT (G protein-coupled receptor kinase interactor 1) family: Regulates Arf GTPases involved in vesicle trafficking and actin remodeling.
3. IQGAPs (IQ motif-containing GTPase-activating proteins): Regulate Rac and Cdc42 GTPases, which are involved in cell adhesion, migration, and cytoskeleton organization.

In summary, GTPase-activating proteins (GAPs) are regulatory proteins that accelerate the GTP hydrolysis of GTPases, thereby acting as negative regulators of various intracellular signaling pathways and ensuring proper control of downstream cellular responses.

Adenosine diphosphate ribose (ADPR) is a molecule that plays a role in various cellular processes, including the modification of proteins and the regulation of enzyme activity. It is formed by the attachment of a diphosphate group and a ribose sugar to the adenine base of a nucleotide. ADPR is involved in the transfer of chemical energy within cells and is also a precursor in the synthesis of other important molecules, such as NAD+ (nicotinamide adenine dinucleotide). It should be noted that ADPR is not a medication or a drug, but rather a naturally occurring biomolecule.

Phospholipase D is an enzyme that catalyzes the hydrolysis of phosphatidylcholine and other glycerophospholipids to produce phosphatidic acid and a corresponding alcohol. This reaction plays a crucial role in various cellular processes, including signal transduction, membrane trafficking, and lipid metabolism. There are several isoforms of Phospholipase D identified in different tissues and organisms, each with distinct regulatory mechanisms and functions. The enzyme's activity can be modulated by various factors such as calcium ions, protein kinases, and G proteins, making it a critical component in the regulation of cellular homeostasis.

Guanosine triphosphate (GTP) is a nucleotide that plays a crucial role in various cellular processes, such as protein synthesis, signal transduction, and regulation of enzymatic activities. It serves as an energy currency, similar to adenosine triphosphate (ATP), and undergoes hydrolysis to guanosine diphosphate (GDP) or guanosine monophosphate (GMP) to release energy required for these processes. GTP is also a precursor for the synthesis of other essential molecules, including RNA and certain signaling proteins. Additionally, it acts as a molecular switch in many intracellular signaling pathways by binding and activating specific GTPase proteins.

Nucleoside diphosphate sugars (NDP-sugars) are essential activated sugars that play a crucial role in the biosynthesis of complex carbohydrates, such as glycoproteins and glycolipids. They consist of a sugar molecule linked to a nucleoside diphosphate, which is formed from a nucleotide by removal of one phosphate group.

NDP-sugars are created through the action of enzymes called nucleoside diphosphate sugars synthases or transferases, which transfer a sugar molecule from a donor to a nucleoside diphosphate, forming an NDP-sugar. The resulting NDP-sugar can then be used as a substrate for various glycosyltransferases that catalyze the addition of sugars to other molecules, such as proteins or lipids.

NDP-sugars are involved in many important biological processes, including cell signaling, protein targeting, and immune response. They also play a critical role in maintaining the structural integrity of cells and tissues.

Adenosine diphosphate (ADP) sugars, also known as sugar nucleotides, are molecules that play a crucial role in the biosynthesis of complex carbohydrates, such as glycoproteins and glycolipids. These molecules consist of a sugar molecule, usually glucose or galactose, linked to a molecule of adenosine diphosphate (ADP).

The ADP portion of the molecule provides the energy needed for the transfer of the sugar moiety to other molecules during the process of glycosylation. The reaction is catalyzed by enzymes called glycosyltransferases, which transfer the sugar from the ADP-sugar donor to an acceptor molecule, such as a protein or lipid.

ADP-sugars are important in various biological processes, including cell recognition, signal transduction, and protein folding. Abnormalities in the metabolism of ADP-sugars have been implicated in several diseases, including cancer, inflammation, and neurodegenerative disorders.

Endocytosis is the process by which cells absorb substances from their external environment by engulfing them in membrane-bound structures, resulting in the formation of intracellular vesicles. This mechanism allows cells to take up large molecules, such as proteins and lipids, as well as small particles, like bacteria and viruses. There are two main types of endocytosis: phagocytosis (cell eating) and pinocytosis (cell drinking). Phagocytosis involves the engulfment of solid particles, while pinocytosis deals with the uptake of fluids and dissolved substances. Other specialized forms of endocytosis include receptor-mediated endocytosis and caveolae-mediated endocytosis, which allow for the specific internalization of molecules through the interaction with cell surface receptors.

Protein transport, in the context of cellular biology, refers to the process by which proteins are actively moved from one location to another within or between cells. This is a crucial mechanism for maintaining proper cell function and regulation.

Intracellular protein transport involves the movement of proteins within a single cell. Proteins can be transported across membranes (such as the nuclear envelope, endoplasmic reticulum, Golgi apparatus, or plasma membrane) via specialized transport systems like vesicles and transport channels.

Intercellular protein transport refers to the movement of proteins from one cell to another, often facilitated by exocytosis (release of proteins in vesicles) and endocytosis (uptake of extracellular substances via membrane-bound vesicles). This is essential for communication between cells, immune response, and other physiological processes.

It's important to note that any disruption in protein transport can lead to various diseases, including neurological disorders, cancer, and metabolic conditions.

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.

Ribose is a simple carbohydrate, specifically a monosaccharide, which means it is a single sugar unit. It is a type of sugar known as a pentose, containing five carbon atoms. Ribose is a vital component of ribonucleic acid (RNA), one of the essential molecules in all living cells, involved in the process of transcribing and translating genetic information from DNA to proteins. The term "ribose" can also refer to any sugar alcohol derived from it, such as D-ribose or Ribitol.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

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.

ADP Ribose Transferases are a group of enzymes that catalyze the transfer of ADP-ribose groups from donor molecules, such as NAD+ (nicotinamide adenine dinucleotide), to specific acceptor molecules. This transfer process plays a crucial role in various cellular processes, including DNA repair, gene expression regulation, and modulation of protein function.

The reaction catalyzed by ADP Ribose Transferases can be represented as follows:

Donor (NAD+ or NADP+) + Acceptor → Product (NR + ADP-ribosylated acceptor)

There are two main types of ADP Ribose Transferases based on their function and the type of modification they perform:

1. Poly(ADP-ribose) polymerases (PARPs): These enzymes add multiple ADP-ribose units to a single acceptor protein, forming long, linear, or branched chains known as poly(ADP-ribose) (PAR). PARylation is involved in DNA repair, genomic stability, and cell death pathways.
2. Monomeric ADP-ribosyltransferases: These enzymes transfer a single ADP-ribose unit to an acceptor protein, which is called mono(ADP-ribosyl)ation. This modification can regulate protein function, localization, and stability in various cellular processes, such as signal transduction, inflammation, and stress response.

Dysregulation of ADP Ribose Transferases has been implicated in several diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Therefore, understanding the function and regulation of these enzymes is essential for developing novel therapeutic strategies to target these conditions.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

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.

Cholera toxin is a protein toxin produced by the bacterium Vibrio cholerae, which causes the infectious disease cholera. The toxin is composed of two subunits, A and B, and its primary mechanism of action is to alter the normal function of cells in the small intestine.

The B subunit of the toxin binds to ganglioside receptors on the surface of intestinal epithelial cells, allowing the A subunit to enter the cell. Once inside, the A subunit activates a signaling pathway that results in the excessive secretion of chloride ions and water into the intestinal lumen, leading to profuse, watery diarrhea, dehydration, and other symptoms associated with cholera.

Cholera toxin is also used as a research tool in molecular biology and immunology due to its ability to modulate cell signaling pathways. It has been used to study the mechanisms of signal transduction, protein trafficking, and immune responses.

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

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.

Pertussis toxin is an exotoxin produced by the bacterium Bordetella pertussis, which is responsible for causing whooping cough in humans. This toxin has several effects on the host organism, including:

1. Adenylyl cyclase activation: Pertussis toxin enters the host cell and modifies a specific G protein (Gαi), leading to the continuous activation of adenylyl cyclase. This results in increased levels of intracellular cAMP, which disrupts various cellular processes.
2. Inhibition of immune response: Pertussis toxin impairs the host's immune response by inhibiting the migration and function of immune cells like neutrophils and macrophages. It also interferes with antigen presentation and T-cell activation, making it difficult for the body to clear the infection.
3. Increased inflammation: The continuous activation of adenylyl cyclase by pertussis toxin leads to increased production of proinflammatory cytokines, contributing to the severe coughing fits and other symptoms associated with whooping cough.

Pertussis toxin is an essential virulence factor for Bordetella pertussis, and its effects contribute significantly to the pathogenesis of whooping cough. Vaccination against pertussis includes inactivated or genetically detoxified forms of pertussis toxin, which provide immunity without causing disease symptoms.

Virulence factors in Bordetella pertussis, the bacterium that causes whooping cough, refer to the characteristics or components of the organism that contribute to its ability to cause disease. These virulence factors include:

1. Pertussis Toxin (PT): A protein exotoxin that inhibits the immune response and affects the nervous system, leading to the characteristic paroxysmal cough of whooping cough.
2. Adenylate Cyclase Toxin (ACT): A toxin that increases the levels of cAMP in host cells, disrupting their function and contributing to the pathogenesis of the disease.
3. Filamentous Hemagglutinin (FHA): A surface protein that allows the bacterium to adhere to host cells and evade the immune response.
4. Fimbriae: Hair-like appendages on the surface of the bacterium that facilitate adherence to host cells.
5. Pertactin (PRN): A surface protein that also contributes to adherence and is a common component of acellular pertussis vaccines.
6. Dermonecrotic Toxin: A toxin that causes localized tissue damage and necrosis, contributing to the inflammation and symptoms of whooping cough.
7. Tracheal Cytotoxin: A toxin that damages ciliated epithelial cells in the respiratory tract, impairing mucociliary clearance and increasing susceptibility to infection.

These virulence factors work together to enable Bordetella pertussis to colonize the respiratory tract, evade the host immune response, and cause the symptoms of whooping cough.

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.

Adenosine diphosphate (ADP) is a chemical compound that plays a crucial role in energy transfer within cells. It is a nucleotide, which consists of a adenosine molecule (a sugar molecule called ribose attached to a nitrogenous base called adenine) and two phosphate groups.

In the cell, ADP functions as an intermediate in the conversion of energy from one form to another. When a high-energy phosphate bond in ADP is broken, energy is released and ADP is converted to adenosine triphosphate (ATP), which serves as the main energy currency of the cell. Conversely, when ATP donates a phosphate group to another molecule, it is converted back to ADP, releasing energy for the cell to use.

ADP also plays a role in blood clotting and other physiological processes. In the coagulation cascade, ADP released from damaged red blood cells can help activate platelets and initiate the formation of a blood clot.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

Botulinum toxins are neurotoxic proteins produced by the bacterium Clostridium botulinum and related species. They are the most potent naturally occurring toxins, and are responsible for the paralytic illness known as botulism. There are seven distinct botulinum toxin serotypes (A-G), each of which targets specific proteins in the nervous system, leading to inhibition of neurotransmitter release and subsequent muscle paralysis.

In clinical settings, botulinum toxins have been used for therapeutic purposes due to their ability to cause temporary muscle relaxation. Botulinum toxin type A (Botox) is the most commonly used serotype in medical treatments, including management of dystonias, spasticity, migraines, and certain neurological disorders. Additionally, botulinum toxins are widely employed in aesthetic medicine for reducing wrinkles and fine lines by temporarily paralyzing facial muscles.

It is important to note that while botulinum toxins have therapeutic benefits when used appropriately, they can also pose significant health risks if misused or improperly handled. Proper medical training and supervision are essential for safe and effective utilization of these powerful toxins.

NAD (Nicotinamide Adenine Dinucleotide) is a coenzyme found in all living cells. It plays an essential role in cellular metabolism, particularly in redox reactions, where it acts as an electron carrier. NAD exists in two forms: NAD+, which accepts electrons and becomes reduced to NADH. This pairing of NAD+/NADH is involved in many fundamental biological processes such as generating energy in the form of ATP during cellular respiration, and serving as a critical cofactor for various enzymes that regulate cellular functions like DNA repair, gene expression, and cell death.

Maintaining optimal levels of NAD+/NADH is crucial for overall health and longevity, as it declines with age and in certain disease states. Therefore, strategies to boost NAD+ levels are being actively researched for their potential therapeutic benefits in various conditions such as aging, neurodegenerative disorders, and metabolic diseases.

Adenylate cyclase is an enzyme that catalyzes the conversion of adenosine triphosphate (ATP) to cyclic adenosine monophosphate (cAMP). It plays a crucial role in various cellular processes, including signal transduction and metabolism. Adenylate cyclase is activated by hormones and neurotransmitters that bind to G-protein-coupled receptors on the cell membrane, leading to the production of cAMP, which then acts as a second messenger to regulate various intracellular responses. There are several isoforms of adenylate cyclase, each with distinct regulatory properties and subcellular localization.

Adenylate cyclase toxin is a type of exotoxin produced by certain bacteria, including Bordetella pertussis (the causative agent of whooping cough) and Vibrio cholerae. This toxin functions by entering host cells and catalyzing the conversion of adenosine triphosphate (ATP) to cyclic adenosine monophosphate (cAMP), leading to increased intracellular cAMP levels.

The elevated cAMP levels can disrupt various cellular processes, such as signal transduction and ion transport, resulting in a range of physiological effects that contribute to the pathogenesis of the bacterial infection. For example, in the case of Bordetella pertussis, adenylate cyclase toxin impairs the function of immune cells, allowing the bacteria to evade host defenses and establish a successful infection.

In summary, adenylate cyclase toxin is a virulence factor produced by certain pathogenic bacteria that increases intracellular cAMP levels in host cells, leading to disrupted cellular processes and contributing to bacterial pathogenesis.

Poly(ADP-ribose) (PAR) is not strictly referred to as "Poly Adenosine Diphosphate Ribose" in the medical or biochemical context, although the term ADP-ribose is a component of it. Poly(ADP-ribose) is a polymer of ADP-ribose units that are synthesized by enzymes called poly(ADP-ribose) polymerases (PARPs).

Poly(ADP-ribosyl)ation, the process of adding PAR polymers to target proteins, plays a crucial role in various cellular processes such as DNA repair, genomic stability, and cell death. In medical research, alterations in PAR metabolism have been implicated in several diseases, including cancer and neurodegenerative disorders. Therefore, understanding the function and regulation of poly(ADP-ribose) is of significant interest in biomedical sciences.

Phosphatidylinositol 4,5-Diphosphate (PIP2) is a phospholipid molecule that plays a crucial role as a secondary messenger in various cell signaling pathways. It is a constituent of the inner leaflet of the plasma membrane and is formed by the phosphorylation of Phosphatidylinositol 4-Phosphate (PIP) at the 5th position of the inositol ring by enzyme Phosphoinositide kinase.

PIP2 is involved in several cellular processes, including regulation of ion channels, cytoskeleton dynamics, and membrane trafficking. It also acts as a substrate for the generation of two important secondary messengers, Inositol 1,4,5-Trisphosphate (IP3) and Diacylglycerol (DAG), which are produced by the action of Phospholipase C enzyme in response to various extracellular signals. These second messengers then mediate a variety of cellular responses such as calcium mobilization, gene expression, and cell proliferation.

Bacterial toxins are poisonous substances produced and released by bacteria. They can cause damage to the host organism's cells and tissues, leading to illness or disease. Bacterial toxins can be classified into two main types: exotoxins and endotoxins.

Exotoxins are proteins secreted by bacterial cells that can cause harm to the host. They often target specific cellular components or pathways, leading to tissue damage and inflammation. Some examples of exotoxins include botulinum toxin produced by Clostridium botulinum, which causes botulism; diphtheria toxin produced by Corynebacterium diphtheriae, which causes diphtheria; and tetanus toxin produced by Clostridium tetani, which causes tetanus.

Endotoxins, on the other hand, are components of the bacterial cell wall that are released when the bacteria die or divide. They consist of lipopolysaccharides (LPS) and can cause a generalized inflammatory response in the host. Endotoxins can be found in gram-negative bacteria such as Escherichia coli and Pseudomonas aeruginosa.

Bacterial toxins can cause a wide range of symptoms depending on the type of toxin, the dose, and the site of infection. They can lead to serious illnesses or even death if left untreated. Vaccines and antibiotics are often used to prevent or treat bacterial infections and reduce the risk of severe complications from bacterial toxins.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Adaptor proteins play a crucial role in vesicular transport, which is the process by which materials are transported within cells in membrane-bound sacs called vesicles. These adaptor proteins serve as a bridge between vesicle membranes and cytoskeletal elements or other cellular structures, facilitating the movement of vesicles throughout the cell.

There are several different types of adaptor proteins involved in vesicular transport, each with specific functions and localizations within the cell. Some examples include:

1. Clathrin Adaptor Protein Complex (AP-1, AP-2, AP-3, AP-4): These complexes are responsible for recruiting clathrin to membranes during vesicle formation, which helps to shape and stabilize the vesicle. They also play a role in sorting cargo into specific vesicles.

2. Coat Protein Complex I (COPI): This complex is involved in the transport of proteins between the endoplasmic reticulum (ER) and the Golgi apparatus, as well as within the Golgi itself. COPI-coated vesicles are formed by the assembly of coatomer proteins around the membrane, which helps to deform the membrane into a vesicle shape.

3. Coat Protein Complex II (COPII): This complex is involved in the transport of proteins from the ER to the Golgi apparatus. COPII-coated vesicles are formed by the assembly of Sar1, Sec23/24, and Sec13/31 proteins around the membrane, which helps to select cargo and form a vesicle.

4. BAR (Bin/Amphiphysin/Rvs) Domain Proteins: These proteins are involved in shaping and stabilizing membranes during vesicle formation. They can sense and curve membranes, recruiting other proteins to help form the vesicle.

5. SNARE Proteins: While not strictly adaptor proteins, SNAREs play a critical role in vesicle fusion by forming complexes that bring the vesicle and target membrane together. These complexes provide the energy required for membrane fusion, allowing for the release of cargo into the target compartment.

Overall, adaptor proteins are essential components of the cellular machinery that regulates intracellular trafficking. They help to select cargo, deform membranes, and facilitate vesicle formation, ensuring that proteins and lipids reach their correct destinations within the cell.

RhoA (Ras Homolog Family Member A) is a small GTPase protein that acts as a molecular switch, cycling between an inactive GDP-bound state and an active GTP-bound state. It plays a crucial role in regulating various cellular processes such as actin cytoskeleton organization, gene expression, cell cycle progression, and cell migration.

RhoA GTP-binding protein becomes activated when it binds to GTP, and this activation leads to the recruitment of downstream effectors that mediate its functions. The activity of RhoA is tightly regulated by several proteins, including guanine nucleotide exchange factors (GEFs) that promote the exchange of GDP for GTP, GTPase-activating proteins (GAPs) that stimulate the intrinsic GTPase activity of RhoA to hydrolyze GTP to GDP and return it to an inactive state, and guanine nucleotide dissociation inhibitors (GDIs) that sequester RhoA in the cytoplasm and prevent its association with the membrane.

Mutations or dysregulation of RhoA GTP-binding protein have been implicated in various human diseases, including cancer, neurological disorders, and cardiovascular diseases.

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.

Azaguanine is a type of antimetabolite drug that is used in medical research and treatment. It is a purine analogue, which means it has a similar chemical structure to the natural purine bases adenine and guanine, which are building blocks of DNA and RNA. Azaguanine can be incorporated into the genetic material of cells, interfering with their normal function and replication. It is used in research to study the effects of such interference on cell growth and development.

In clinical medicine, azaguanine has been used as an anticancer drug, although it is not widely used today due to its toxicity and the availability of more effective treatments. It may also have some activity against certain types of parasitic infections, such as leishmaniasis and malaria.

It's important to note that azaguanine is not a commonly used medication and its use should be under the supervision of a medical professional with experience in its administration and management of potential side effects.

Intracellular membranes refer to the membrane structures that exist within a eukaryotic cell (excluding bacteria and archaea, which are prokaryotic and do not have intracellular membranes). These membranes compartmentalize the cell, creating distinct organelles or functional regions with specific roles in various cellular processes.

Major types of intracellular membranes include:

1. Nuclear membrane (nuclear envelope): A double-membraned structure that surrounds and protects the genetic material within the nucleus. It consists of an outer and inner membrane, perforated by nuclear pores that regulate the transport of molecules between the nucleus and cytoplasm.
2. Endoplasmic reticulum (ER): An extensive network of interconnected tubules and sacs that serve as a major site for protein folding, modification, and lipid synthesis. The ER has two types: rough ER (with ribosomes on its surface) and smooth ER (without ribosomes).
3. Golgi apparatus/Golgi complex: A series of stacked membrane-bound compartments that process, sort, and modify proteins and lipids before they are transported to their final destinations within the cell or secreted out of the cell.
4. Lysosomes: Membrane-bound organelles containing hydrolytic enzymes for breaking down various biomolecules (proteins, carbohydrates, lipids, and nucleic acids) in the process called autophagy or from outside the cell via endocytosis.
5. Peroxisomes: Single-membrane organelles involved in various metabolic processes, such as fatty acid oxidation and detoxification of harmful substances like hydrogen peroxide.
6. Vacuoles: Membrane-bound compartments that store and transport various molecules, including nutrients, waste products, and enzymes. Plant cells have a large central vacuole for maintaining turgor pressure and storing metabolites.
7. Mitochondria: Double-membraned organelles responsible for generating energy (ATP) through oxidative phosphorylation and other metabolic processes, such as the citric acid cycle and fatty acid synthesis.
8. Chloroplasts: Double-membraned organelles found in plant cells that convert light energy into chemical energy during photosynthesis, producing oxygen and organic compounds (glucose) from carbon dioxide and water.
9. Endoplasmic reticulum (ER): A network of interconnected membrane-bound tubules involved in protein folding, modification, and transport; it is divided into two types: rough ER (with ribosomes on the surface) and smooth ER (without ribosomes).
10. Nucleus: Double-membraned organelle containing genetic material (DNA) and associated proteins involved in replication, transcription, RNA processing, and DNA repair. The nuclear membrane separates the nucleoplasm from the cytoplasm and contains nuclear pores for transporting molecules between the two compartments.

Enzyme activation refers to the process by which an enzyme becomes biologically active and capable of carrying out its specific chemical or biological reaction. This is often achieved through various post-translational modifications, such as proteolytic cleavage, phosphorylation, or addition of cofactors or prosthetic groups to the enzyme molecule. These modifications can change the conformation or structure of the enzyme, exposing or creating a binding site for the substrate and allowing the enzymatic reaction to occur.

For example, in the case of proteolytic cleavage, an inactive precursor enzyme, known as a zymogen, is cleaved into its active form by a specific protease. This is seen in enzymes such as trypsin and chymotrypsin, which are initially produced in the pancreas as inactive precursors called trypsinogen and chymotrypsinogen, respectively. Once they reach the small intestine, they are activated by enteropeptidase, a protease that cleaves a specific peptide bond, releasing the active enzyme.

Phosphorylation is another common mechanism of enzyme activation, where a phosphate group is added to a specific serine, threonine, or tyrosine residue on the enzyme by a protein kinase. This modification can alter the conformation of the enzyme and create a binding site for the substrate, allowing the enzymatic reaction to occur.

Enzyme activation is a crucial process in many biological pathways, as it allows for precise control over when and where specific reactions take place. It also provides a mechanism for regulating enzyme activity in response to various signals and stimuli, such as hormones, neurotransmitters, or changes in the intracellular environment.

Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.

Passive transport does not require the input of energy and includes:

1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.

Active transport requires the input of energy (in the form of ATP) and includes:

1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.

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.

Proteins are complex, large molecules that play critical roles in the body's functions. They are made up of amino acids, which are organic compounds that are the building blocks of proteins. Proteins are required for the structure, function, and regulation of the body's tissues and organs. They are essential for the growth, repair, and maintenance of body tissues, and they play a crucial role in many biological processes, including metabolism, immune response, and cellular signaling. Proteins can be classified into different types based on their structure and function, such as enzymes, hormones, antibodies, and structural proteins. They are found in various foods, especially animal-derived products like meat, dairy, and eggs, as well as plant-based sources like beans, nuts, and grains.

NAD+ nucleosidase, also known as NMN hydrolase or nicotinamide mononucleotide hydrolase, is an enzyme that catalyzes the hydrolysis of nicotinamide mononucleotide (NMN) to produce nicotinamide and 5-phosphoribosyl-1-pyrophosphate (PRPP). NAD+ (nicotinamide adenine dinucleotide) is a crucial coenzyme involved in various redox reactions in the body, and its biosynthesis involves several steps, one of which is the conversion of nicotinamide to NMN by the enzyme nicotinamide phosphoribosyltransferase (NAMPT).

The hydrolysis of NMN to nicotinamide and PRPP by NAD+ nucleosidase is a rate-limiting step in the salvage pathway of NAD+ biosynthesis, which recycles nicotinamide back to NMN and then to NAD+. Therefore, NAD+ nucleosidase plays an essential role in maintaining NAD+ homeostasis in the body.

Deficiencies or mutations in NAD+ nucleosidase can lead to various metabolic disorders, including neurological and cardiovascular diseases, as well as aging-related conditions associated with decreased NAD+ levels.

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.

Tankyrases are a group of proteins that belong to the poly (ADP-ribose) polymerase (PARP) family, specifically PARP5a and PARP5b. They play roles in various cellular processes such as telomere maintenance, Wnt signaling pathway regulation, and protein trafficking. Tankyrases add poly(ADP-ribose) chains to their target proteins, leading to changes in their function, localization, or stability. Dysregulation of tankyrases has been implicated in several diseases, including cancer.

Cricetinae is a subfamily of rodents that includes hamsters, gerbils, and relatives. These small mammals are characterized by having short limbs, compact bodies, and cheek pouches for storing food. They are native to various parts of the world, particularly in Europe, Asia, and Africa. Some species are popular pets due to their small size, easy care, and friendly nature. In a medical context, understanding the biology and behavior of Cricetinae species can be important for individuals who keep them as pets or for researchers studying their physiology.

CHO cells, or Chinese Hamster Ovary cells, are a type of immortalized cell line that are commonly used in scientific research and biotechnology. They were originally derived from the ovaries of a female Chinese hamster (Cricetulus griseus) in the 1950s.

CHO cells have several characteristics that make them useful for laboratory experiments. They can grow and divide indefinitely under appropriate conditions, which allows researchers to culture large quantities of them for study. Additionally, CHO cells are capable of expressing high levels of recombinant proteins, making them a popular choice for the production of therapeutic drugs, vaccines, and other biologics.

In particular, CHO cells have become a workhorse in the field of biotherapeutics, with many approved monoclonal antibody-based therapies being produced using these cells. The ability to genetically modify CHO cells through various methods has further expanded their utility in research and industrial applications.

It is important to note that while CHO cells are widely used in scientific research, they may not always accurately represent human cell behavior or respond to drugs and other compounds in the same way as human cells do. Therefore, results obtained using CHO cells should be validated in more relevant systems when possible.

Mitochondrial ADP/ATP translocases, also known as adenine nucleotide translocators (ANT), are a group of proteins located in the inner mitochondrial membrane that play a crucial role in cellular energy production. These translocases facilitate the exchange of adenosine diphosphate (ADP) and adenosine triphosphate (ATP) across the mitochondrial membrane, which is essential for oxidative phosphorylation and thus, energy homeostasis in the cell.

In more detail, during oxidative phosphorylation, ATP is produced within the mitochondria as a result of the electron transport chain's activity. This ATP must be exported to the cytosol for use by the cell's various processes. Simultaneously, the mitochondria need a continuous supply of ADP to sustain the production of ATP. The mitochondrial ADP/ATP translocases facilitate this exchange, allowing for the import of ADP into the mitochondria and the export of ATP to the cytosol.

There are multiple isoforms of the ADP/ATP translocase in humans (ANT1, ANT2, ANT3, and ANT4), encoded by different genes, with varying tissue distributions and functions. Dysfunction of these translocases has been implicated in several pathological conditions, including neurodegenerative diseases, ischemia-reperfusion injury, and cancer.

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.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

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ADP-ribosylation factor-like) family of proteins, which are structurally related to ADP-ribosylation factors (ARFs). ARFs, ... ADP-ribosylation factor-like protein 1 is a protein that in humans is encoded by the ARL1 gene. The protein encoded by this ... "Entrez Gene: ARL1 ADP-ribosylation factor-like 1". Lu L, Hong W (September 2003). "Interaction of Arl1-GTP with GRIP domains ... Van Valkenburgh H, Shern JF, Sharer JD, Zhu X, Kahn RA (June 2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have ...
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ADP-ribosylation factor-like protein 6-interacting protein 1 is a protein that in humans is encoded by the ARL6IP1 gene. GRCh38 ... "Entrez Gene: ARL6IP1 ADP-ribosylation factor-like 6 interacting protein 1". Human ARL6IP1 genome location and ARL6IP1 gene ... "A novel ADP-ribosylation like factor (ARL-6), interacts with the protein-conducting channel SEC61beta subunit". FEBS Lett. 459 ... ADP-ribosylation-like factor-6 interacting protein (ARL6)". Genomics. 68 (3): 351-4. doi:10.1006/geno.2000.6278. PMID 10995579 ...
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... an ADP-ribosylation factor 6 GTPase activating protein, inhibits beta 2-adrenoceptor internalization". Molecular Pharmacology. ... 5-trisphosphate-binding protein that is functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-activating ... membrane trafficking induced by epidermal growth factor is inhibited by stimulation of phospholipase C-coupled thrombin ... 128 (1): 9-13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. S2CID 18872015. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, ...
... binds to 2 molecules of ADP-ribosylation factor 1 (Arf1) as shown in this figure. A hinge region of exomer is thought to ...
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ADP-ribosylation factor GTPase-activating protein 1 is an enzyme that in humans is encoded by the ARFGAP1 gene. Two transcript ... which associates with the Golgi apparatus and which interacts with ADP-ribosylation factor 1 (ARF1). The encoded protein ...
ADP-ribosylation factor-like protein 3 is a protein that in humans is encoded by the ARL3 gene. ADP-ribosylation factor-like 3 ... "Entrez Gene: ARL3 ADP-ribosylation factor-like 3". Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M ... Van Valkenburgh H, Shern JF, Sharer JD, Zhu X, Kahn RA (June 2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have ... Kim HS (1998). "Assignment of the human ADP-ribosylation factor-like 3 (ARL3) gene to chromosome 10 band q23.3 by radiation ...
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... guanine nucleotide-exchange proteins for ADP-ribosylation factors". J. Biol. Chem. 275 (5): 3221-30. doi:10.1074/jbc.275.5.3221 ... 2008). "GEP100 links epidermal growth factor receptor signalling to Arf6 activation to induce breast cancer invasion". Nat. ... Venkateswarlu K (2003). "Interaction protein for cytohesin exchange factors 1 (IPCEF1) binds cytohesin 2 and modifies its ... 10 (1): 85-92. doi:10.1038/ncb1672. PMID 18084281. S2CID 6148446. Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status ...
April 2005). "Exocytosis of CTLA-4 is dependent on phospholipase D and ADP ribosylation factor-1 and stimulated during ... July 2020). "Blood factors transfer beneficial effects of exercise on neurogenesis and cognition to the aged brain". Science. ... Lugli EB, Pouliot M, Portela M, Loomis MR, Raper J (November 2004). "Characterization of primate trypanosome lytic factors". ... 53 (1): 21-38. PMID 11939716. Jaworek J, Bonio J, Leja-Szpa A, Nawrot K, Tomaszewska MR, Stachura J, et al. (March 2002). " ...
"Entrez Gene: ARFGEF1 ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited)". Padilla PI, Chang MJ ... ADP-ribosylation factors (ARFs) play an important role in intracellular vesicular trafficking. The protein encoded by this gene ... "Isolation of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP ribosylation factor (ARF) 1 and ARF3 that ... "Purification and cloning of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors". The ...
... "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". The Journal of ... "beta-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled ... Arrestin, beta 1, also known as ARRB1, is a protein which in humans is encoded by the ARRB1 gene. Members of arrestin/beta- ... Arrestin beta 1 has been shown to interact with Arf6, PTHLH, DVL2 Mdm2, OPRD1, PSCD2, and RALGDS. GRCh38: Ensembl release 89: ...
... and 3 ADP-ribosylation factors with adaptor protein complexes 1 and 3". Biochemistry. 41 (14): 4669-77. doi:10.1021/bi016064j. ... 271 (1): 9-17. doi:10.1006/viro.2000.0277. PMID 10814565. Crump CM, Xiang Y, Thomas L, Gu F, Austin C, Tooze SA, Thomas G (May ... AP-3 complex subunit delta-1 is a protein that in humans is encoded by the AP3D1 gene. AP3D1 is a subunit of the AP3 adaptor- ... 21 (1): 111-22. doi:10.1016/S0896-6273(00)80519-X. PMID 9697856. S2CID 17237941. Rehling P, Darsow T, Katzmann DJ, Emr SD (2000 ...
... and 3 ADP-ribosylation factors with adaptor protein complexes 1 and 3". Biochemistry. 41 (14): 4669-77. doi:10.1021/bi016064j. ... Eiraku M, Hirata Y, Takeshima H, Hirano T, Kengaku M (Jul 2002). "Delta/notch-like epidermal growth factor (EGF)-related ... AP-1 complex subunit gamma-1 is a protein that in humans is encoded by the AP1G1 gene. Adaptins are important components of ... 22 (1): 78-88. doi:10.1093/emboj/cdg015. PMC 140067. PMID 12505986. Horikawa HP, Kneussel M, El Far O, Betz H (Nov 2002). " ...
ADP ribosylation factors (ARFs) are members of the ARF family of GTP-binding proteins of the Ras superfamily. ARF family ... The small ADP ribosylation factor (Arf) GTP-binding proteins are major regulators of vesicle biogenesis in intracellular ... Kahn RA, Kern FG, Clark J, Gelmann EP, Rulka C (1991). "Human ADP-ribosylation factors. A functionally conserved family of GTP- ... Amor JC, Harrison DH, Kahn RA, Ringe D (1994). "Structure of the human ADP-ribosylation factor 1 complexed with GDP". Nature. ...
"ADP-Ribosylation Factor 1" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... ADP-RIBOSYLATION FACTOR 1 is involved in regulating intracellular transport by modulating the interaction of coat proteins with ... This graph shows the total number of publications written about "ADP-Ribosylation Factor 1" by people in this website by year, ... Below are the most recent publications written about "ADP-Ribosylation Factor 1" by people in Profiles. ...
In the present study, we identified ADP-ribosylation factor 1 (ARF1) contributed to the inhibitory effect of GBV-C E2 on HIV-1 ... Chenliang Wang1,2, Christine L. Timmons1, Qiujia Shao1, Ballington L. Kinlock1, Tiffany M. Turner1, Aikichi Iwamoto3, Hui Zhang ... As of January 1, 2022, Oncotarget has shifted to a continuous publishing model. Papers will now be published continuously ... 1 Center for AIDS Health Disparities Research, Department of Microbiology and Immunology, Meharry Medical College, Nashville, ...
Role for ADP ribosylation factor 1 in the regulation of hepatitis C virus replication. Journal of Virology. 2011 Jan;85(2):946- ... Role for ADP ribosylation factor 1 in the regulation of hepatitis C virus replication. In: Journal of Virology. 2011 ; Vol. 85 ... Role for ADP ribosylation factor 1 in the regulation of hepatitis C virus replication. / Matto, Meirav; Sklan, Ella H.; David, ... Matto, M, Sklan, EH, David, N, Melamed-Book, N, Casanova, JE, Glenn, JS & Aroeti, B 2011, Role for ADP ribosylation factor 1 ...
Compound: ADP-ribosylation factor 1. Species: Homo sapiens [TaxId:9606]. Gene: ARF1. Database cross-references and differences ... Description: Delta-17 Human ADP Ribosylation Factor 1 Complexed with GDP. Class: protein transport. Keywords: Delta17Arf1, ... R-factor: N/A. AEROSPACI score: 0.03 (click here for full SPACI score report) Chains and heterogens:. *Chain A:. ...
PDB Compounds: (A:) ADP-ribosylation factor binding protein GGA1. SCOPe Domain Sequences for d1ujka_:. Sequence; same for both ... Protein ADP-ribosylation factor binding protein Gga1 [74782] (1 species). *. Species Human (Homo sapiens) [TaxId:9606] [74783 ... d1ujka_ a.118.9.2 (A:) ADP-ribosylation factor binding protein Gga1 {Human (Homo sapiens) [TaxId: 9606]} ...
ADP-ribosylation factors (ARFs) are approximately 20-kDa guanine nucleotide-binding proteins recognized as critical components ... A target of phosphatidylinositol 3,4,5-trisphosphate with a zinc finger motif similar to that of the ADP-ribosylation-factor ... Crystal structure of putative GTPase activating protein for ADP ribosylation factor from Cryptosporidium parvum (cgd5_1040). ... Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1). ...
Dissection of Arabidopsis ADP-RIBOSYLATION FACTOR 1 function in epidermal cell polarity ... NAC transcription factors, NST1 and NST3, are key regulators of the formation of secondary walls in woody tissues of ... 5A,B) (Péret et al., 2012; Swarup et al., 2001). Therefore, the regulatory cis-element and transcriptional factors controlling ... collectively called haustorium-inducing factors (HIFs), a group that includes quinones and phenolic acids (Goyet et al., 2019 ...
Dual interaction of ADP ribosylation factor 1 with Sec7 domain and with lipid membranes during catalysis of guanine nucleotide ... Dual interaction of ADP ribosylation factor 1 with Sec7 domain and with lipid membranes during catalysis of guanine nucleotide ... ADP ribosylation factor 1 mutants identify a phospholipase D effector region and reveal that phospholipase D participates in ... ADP ribosylation factor 1 mutants identify a phospholipase D effector region and reveal that phospholipase D participates in ...
The cytohesins are a class of BFA-resistant small GEFs for ADP-ribosylation factors (ARFs), which regulate cytoskeletal ... They are activated by guanine nucleotide exchange factors (GEFs), which facilitate the exchange of GDP for GTP1,2. This ... is a major risk factor for the development of type 2 diabetes. For the majority of affected individuals, the underlying ... The cytohesins are a class of BFA-resistant small GEFs for ADP-ribosylation factors (ARFs), which regulate cytoskeletal ...
1]. Innate immunity in gastrointestinal system includes epithelial cell layers that express tight cell-cell contact, secreted ... Recent data demonstrate that IBD arises from the complex interplay of genetic and environmental factor caused by a change in ... Importantly, ADP ribosylation factor guanine nucleotide exchange factor 1 (BIG1) expression was decreased in IEC from DSS ... transcription factors, and nuclear factor-κB (NF-κB) in the maintenance and remission of IBD progression (5). ...
Multiple and stepwise interactions between coatomer and ADP-ribosylation factor-1 (Arf1)-GTP. Traffic, 8, 582-593. ...
ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Brown, H.A., Gutowski, ... Unexpectedly, we find that the GTPgammaS-dependent activator of PI(4)P5Kalpha is the small G protein ADP-ribosylation factor ( ... Involvement of a phospholipase D in the mechanism of action of granulocyte-macrophage colony-stimulating factor (GM-CSF): ... Involvement of the phospholipase D pathway in tumor necrosis factor alpha synthesis. Balboa, M.A., Balsinde, J., Aramburu, J., ...
Polyclonal Antibody ADP-Ribosylation factor 1 (ARF 1) Immunogen: Peptide (18mer) Host: Rabbit. 200ul. 390.34 €. -. FGen. ... Polyclonal Antibody ADP-Ribosylation factor 4 (ARF 4) Immunogen: peptide (21mer) Host: Rabbit. 200ul. 391.36 €. -. FGen. ... Polyclonal Antibody Post GPI attachment to Protein Factor (N-epitoope) Immunogen: peptide Host: Rabbit. 200ul. 391.36 €. -. ... Polyclonal Antibody Post GPI attachment to Protein Factor (Mid-region) Immunogen: peptide Host: Rabbit. 200ul. 391.36 €. -. ...
The ADP-ribosylation factor 1 (Arf1) is involved in regulating copper uptake. Southon, A., Greenough, M., Hung, Y., Norgate, M. ... Fear-of-intimacy-mediated zinc transport controls the function of zinc-finger transcription factors involved in myogenesis. ... Forbes-Beadle, L., Crossman, T., Johnson, T. K., Burke, R., Warr, C. G. & Whisstock, J. C., 1 Oct 2016, In: Genetics. 204, 2, p ... Zilian, O., Frei, E., Burke, R., Brentrup, D., Gutjahr, T., Bryant, P. J. & Noll, M., 1 Dec 1999, In: Development. 126, 23, p. ...
ADP-ribosylation factor-like 1. Molecular. skeletal muscle. Mouse. Arl1. 6.0% Increase Gene Expression Level. Add. ... AT hook containing transcription factor 1. Molecular. skeletal muscle. Human. AHCTF1. 4.0% Increase Gene Expression Level. Add ... actin, alpha 1, skeletal muscle. Molecular. skeletal muscle. Mouse. Acta1. 55.0% Increase Gene Expression Level. Add. ... adenylosuccinate synthetase like 1. Molecular. skeletal muscle. Mouse. Adssl1. 13.0% Decrease Gene Expression Level. Add. ...
similar to ADP-ribosylation factor. -. 2e-117. At1g10630. ATARFA1F (ARABIDOPSIS THALIANA ADP-RIBOSYLATION FACTOR A1F). C.G.. S. ... ATARF1 (ADP-RIBOSYLATION FACTOR 1). C.G.. S.X.. Please select. 0.45. 1e-132. 474. Gma.6298.1.S1_s_at. BM309168. -. -. 9e-123. ... ATARF1 (ADP-RIBOSYLATION FACTOR 1). C.G.. S.X.. Please select. 0.43. 2e-131. 470. Gma.6298.2.S1_s_at. BU080611. -. -. 5e-118. ... ATARF1 (ADP-RIBOSYLATION FACTOR 1). C.G.. S.X.. Please select. 0.42. 2e-106. 387. Gma.1630.1.S1_x_at. BF596536. -. -. 4e-122. ...
ARF1-208, Transcript of ADP ribosylation factor 1, human. TSL 2. Gene ARF1, Length 930 nt, Biotype processed transcript, ...
ADP ribosylation factor like GTPase 8B .... ARPC1A. 10552. ARPC1A. actin related protein 2/3 complex subun.... ... ADP ribosylation factor like GTPase 1 [.... ARL8B. 55207. ARL8B. ... insulin like growth factor 2 mRNA bindi.... IMP3. 55272. IMP3. ... TFT: Transcription Factor Targets TFT:GTRD: GTRD TFT:TFT_LEGACY: TFT_Legacy C4: Computational CGN: Cancer Gene Neighborhoods CM ... insulin like growth factor 1 [Source:HG.... IGF2BP1. 10642. IGF2BP1. ...
ADP-ribosyl)ation and activation of CCCTC-binding factor (CTCF), leading to de-repression of downstream tumour-suppressive ... Similarly, the transcription factors that mediate the expression of these microRNAs/lncRNAs have not been studied or analysed ... Also, Cctn2, a cell cycle factor that is necessary for proliferation of myelocytic progenitor cells, is a common target of both ... Repression of Id2 by both microRNAs leads to cell proliferation blockage and to Vfg upregulation, a transcription factor that ...
Expression, purification, and properties of ADP-ribosylation factor (ARF) GTPase activating protein- 1. Huber, I., Rotman, M., ... Arazy, J., 23 Dec 1991, Function Spaces. Jarov, K. (ed.). 1 ed. CRC Press, p. 9-23 15 p. (Lecture Notes in Pure and Applied ... Nevo, E., 1991, Evolutionary Biology. Hecht, M. K., Wallace, B. & MacIntyre, R. J. (eds.). 1 ed. New York: Springer New York, ... p. 1-125 125 p.. Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review ...
Active ADP-ribosylation factor-1 (ARF1) is required for mitotic Golgi fragmentation. Xiang, Y., Seemann, J., Bisel, B., ... Evidence that mono-ADP-ribosylation of CtBP1/BARS regulates lipid storage. Bartz, R., Seemann, J., Zehmer, J. K., Serrero, G., ... A direct role for GRASP65 as a mitotically regulated Golgi stacking factor. Wang, Y., Seemann, J., Pypaert, M., Shorter, J. & ... Sec13 Regulates Expression of Specific Immune Factors Involved in Inflammation In Vivo. Moreira, T. G., Zhang, L., Shaulov, L. ...
ADP-ribosylation factor GTPase-activating protein AGD2 OS=Arabidopsis thaliana GN=AGD2 PE=2 SV=1 PSP ... ADP-ribosylation factor GTPase-activating protein AGD7 OS=Arabidopsis thaliana GN=AGD7 PE=1 SV=1 PSP ... Probable ADP-ribosylation factor GTPase-activating protein AGD5 OS=Arabidopsis thaliana GN=AGD5 PE=1... PSP ... Probable ADP-ribosylation factor GTPase-activating protein AGD6 OS=Arabidopsis thaliana GN=AGD6 PE=1... PSP ...
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ADP-ribosylation factor 1. Image. Gene Ontology Annotations. Cellular Component. *Nucleus. *Cytosol ... adp bulk close coated coatomer consumed contact copi dynamics endoplasmic exchange explored fission golgi governed gtpase ... adp bulk close coated coatomer consumed contact copi dynamics endoplasmic exchange explored fission golgi governed gtpase ... interconnected maintain maintenance mitochondria mitochondrial powerhouse presumably produce proximity reticulum ribosylation ...
ADP-RIBOSYLATION FACTORS FACTORES DE RIBOSILACION-ADP FATORES DE RIBOSILAÇÃO DO ADP ... ADP-RIBOSYLATION FACTOR 1 FACTOR 1 DE RIBOSILACION-ADP FATOR 1 DE RIBOSILAÇÃO DO ADP ... FACTOR 2 DE ELONGACION PEPTIDA FATOR 2 DE ELONGAÇÃO DE PEPTÍDIOS PEPTIDE ELONGATION FACTOR G FACTOR G DE ELONGACION PEPTIDA ... RECEPTOR, NERVE GROWTH FACTOR RECEPTOR DE FACTOR DE CRECIMIENTO DEL NERVIO RECEPTOR DO FATOR DE CRESCIMENTO NEURAL ...
ADP-RIBOSYLATION FACTORS FACTORES DE RIBOSILACION-ADP FATORES DE RIBOSILAÇÃO DO ADP ... ADP-RIBOSYLATION FACTOR 1 FACTOR 1 DE RIBOSILACION-ADP FATOR 1 DE RIBOSILAÇÃO DO ADP ... FACTOR 2 DE ELONGACION PEPTIDA FATOR 2 DE ELONGAÇÃO DE PEPTÍDIOS PEPTIDE ELONGATION FACTOR G FACTOR G DE ELONGACION PEPTIDA ... RECEPTOR, NERVE GROWTH FACTOR RECEPTOR DE FACTOR DE CRECIMIENTO DEL NERVIO RECEPTOR DO FATOR DE CRESCIMENTO NEURAL ...
ADP-RIBOSYLATION FACTORS FACTORES DE RIBOSILACION-ADP FATORES DE RIBOSILAÇÃO DO ADP ... ADP-RIBOSYLATION FACTOR 1 FACTOR 1 DE RIBOSILACION-ADP FATOR 1 DE RIBOSILAÇÃO DO ADP ... FACTOR 2 DE ELONGACION PEPTIDA FATOR 2 DE ELONGAÇÃO DE PEPTÍDIOS PEPTIDE ELONGATION FACTOR G FACTOR G DE ELONGACION PEPTIDA ... RECEPTOR, NERVE GROWTH FACTOR RECEPTOR DE FACTOR DE CRECIMIENTO DEL NERVIO RECEPTOR DO FATOR DE CRESCIMENTO NEURAL ...
ADP-RIBOSYLATION FACTORS FACTORES DE RIBOSILACION-ADP FATORES DE RIBOSILAÇÃO DO ADP ... ADP-RIBOSYLATION FACTOR 1 FACTOR 1 DE RIBOSILACION-ADP FATOR 1 DE RIBOSILAÇÃO DO ADP ... FACTOR 2 DE ELONGACION PEPTIDA FATOR 2 DE ELONGAÇÃO DE PEPTÍDIOS PEPTIDE ELONGATION FACTOR G FACTOR G DE ELONGACION PEPTIDA ... RECEPTOR, NERVE GROWTH FACTOR RECEPTOR DE FACTOR DE CRECIMIENTO DEL NERVIO RECEPTOR DO FATOR DE CRESCIMENTO NEURAL ...
ADP-RIBOSYLATION FACTORS FACTORES DE RIBOSILACION-ADP FATORES DE RIBOSILAÇÃO DO ADP ... ADP-RIBOSYLATION FACTOR 1 FACTOR 1 DE RIBOSILACION-ADP FATOR 1 DE RIBOSILAÇÃO DO ADP ... FACTOR 2 DE ELONGACION PEPTIDA FATOR 2 DE ELONGAÇÃO DE PEPTÍDIOS PEPTIDE ELONGATION FACTOR G FACTOR G DE ELONGACION PEPTIDA ... RECEPTOR, NERVE GROWTH FACTOR RECEPTOR DE FACTOR DE CRECIMIENTO DEL NERVIO RECEPTOR DO FATOR DE CRESCIMENTO NEURAL ...
  • Structural studies of Arf1 and Arf6 have revealed that although these proteins feature the switch 1 and 2 conformational changes, they depart from other small GTP-binding proteins in that they use an additional, unique switch to propagate structural information from one side of the protein to the other. (wikipedia.org)
  • The GDP/GTP structural cycles of human Arf1 and Arf6 feature a unique conformational change that affects the beta2beta3 strands connecting switch 1 and switch 2 (interswitch) and also the amphipathic helical N-terminus. (wikipedia.org)
  • There are currently 6 known mammalian ARF proteins, which are divided into three classes of ARFs: class 1: ARF1, ARF2, ARF3 class 2: ARF4, ARF5 class 3: ARF6. (wikipedia.org)
  • In the present study, we identified ADP-ribosylation factor 1 (ARF1) contributed to the inhibitory effect of GBV-C E2 on HIV-1 Gag membrane targeting. (oncotarget.com)
  • The restoration of ARF1 expression rescued the HIV-1 Gag processing and membrane targeting defect imposed by GBV-C E2. (oncotarget.com)
  • Thus, our results indicate that GBV-C E2 inhibits HIV-1 assembly and release by decreasing ARF1, and may provide insights regarding GBV-C E2's potential for a new therapeutic approach for treating HIV-1. (oncotarget.com)
  • We hypothesized that ADP-ribosylation factor 1 (Arf1) plays an important role in the biogenesis and maintenance of infectious hepatitis C virus (HCV). (huji.ac.il)
  • GTPase activating proteins (GAPs) force ARF to hydrolyze bound GTP to GDP, and Guanine nucleotide exchange factors force ARF to adopt a new GTP molecule in place of a bound GDP. (wikipedia.org)
  • Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1). (embl.de)
  • Probable ADP-ribosylation factor GTPase-activating protein AGD5 OS=Arabidopsis thaliana GN=AGD5 PE=1. (yeastrc.org)
  • Probable ADP-ribosylation factor GTPase-activating protein AGD6 OS=Arabidopsis thaliana GN=AGD6 PE=1. (yeastrc.org)
  • Its carboxy terminus contains an ADP-ribosylation factor domain and a guanine nucleotide binding site, while the amino terminus contains a GTPase activating protein domain which acts on the guanine nucleotide binding site. (sfari.org)
  • Wang C, Timmons CL, Shao Q, Kinlock BL, Turner TM, Iwamoto A, Zhang H, Liu H, Liu B. GB virus type C E2 protein inhibits human immunodeficiency virus type 1 Gag assembly by downregulating human ADP-ribosylation factor 1. (ucdenver.edu)
  • GB virus type C (GBV-C) glycoprotein E2 protein disrupts HIV-1 assembly and release by inhibiting Gag plasma membrane targeting, however the mechanism by which the GBV-C E2 inhibits Gag trafficking remains unclear. (oncotarget.com)
  • Morinaga, N., Tsai, S.-C., Moss, J. & Vaughan, M. Isolation of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP ribosylation factor (ARF) 1 and ARF3 that contains a Sec7-like domain. (nature.com)
  • Studies in the past decade have demonstrated the essential roles of several AJC protein, including underlying actinomyosin components, actin isoforms, and intracellular signal transducer and activator of transcription (STAT) transcription factors, and nuclear factor-κB (NF-κB) in the maintenance and remission of IBD progression ( 5 ). (frontiersin.org)
  • adaptor related protein complex 1 assoc. (gsea-msigdb.org)
  • GA binding protein transcription factor. (gsea-msigdb.org)
  • dystrobrevin binding protein 1 [So. (gsea-msigdb.org)
  • huntingtin interacting protein 1 r. (gsea-msigdb.org)
  • They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 1. (lookformedical.com)
  • It is the catalytic subunit of two distinct large protein complexes, mTOR complex 1 (mTORC1) and mTORC2. (bvsalud.org)
  • ADP-ribosylation factor-like protein 13B (ARL13B), also known as ADP-ribosylation factor-like protein 2-like 1 (ARL2L1), is a protein that in humans is encoded by the ARL13B gene. (nsjbio.com)
  • Hypoxia maintains HIFα protein expression through inhibition of prolyl hydroxylases and IL-1 is suggested to effect subunit expression at the level of transcription and in a similarly post-translational fashion [ 26 ]. (biomedcentral.com)
  • This protein is also a member of the ADP ribosylation factor family of guanine nucleotide-binding family of proteins. (sfari.org)
  • ADP ribosylation factors (ARFs) are members of the ARF family of GTP-binding proteins of the Ras superfamily. (wikipedia.org)
  • ADP-ribosylation factors (ARFs) are approximately 20-kDa guanine nucleotide-binding proteins recognized as critical components in intracellular vesicular transport and phospholipase D activation. (embl.de)
  • Gene encoding ADP-ribosylation factor and similar to other ARFs and ARF-like proteins. (or.jp)
  • The small ADP ribosylation factor (Arf) GTP-binding proteins are major regulators of vesicle biogenesis in intracellular traffic. (wikipedia.org)
  • In the GTP-bound form of these proteins, the interswitch undergoes a two-residue register shift that pulls switch 1 and switch 2 up, restoring an active conformation that can bind GTP. (wikipedia.org)
  • ADP-RIBOSYLATION FACTOR 1 is involved in regulating intracellular transport by modulating the interaction of coat proteins with organelle membranes in the early secretory pathway. (ucdenver.edu)
  • The family members encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking as activators of phospholipase D. The gene products, including 6 ARF proteins and 11 ARF-like proteins, constitute a family of the RAS superfamily. (thermofisher.com)
  • Two important pathways were examined in the current study: (1) a basic pathway of exocytosis that brings new proteins to the cell surface and permits the cell to grow, and (2) synaptic transmission, a specialized form of exocytosis, regulated by Ca 2+ entry, in which vesicles already present at synapses fuse with the membrane and recycle locally (Murthy, 2003). (sdbonline.org)
  • Liang, JO & Kornfeld, S 1998, ' Erratum: Comparative activity of ADP-ribosylation factor family members in the early steps of coated vesicle formation on rat liver Golgi membranes (Journal of Biological Chemistry (1997) 272 (4141-4148)) ', Journal of Biological Chemistry , vol. 273, no. 4, pp. 2488. (umn.edu)
  • We report here the identification of the ARF exchange factor GBF1 as a Golgi phosphoprotein. (aston.ac.uk)
  • Here we show, in articular chondrocytes, that IL-1β-induces primary cilia elongation with alterations to cilia trafficking of arl13b. (biomedcentral.com)
  • As of January 1, 2022, Oncotarget has shifted to a continuous publishing model. (oncotarget.com)
  • This reaction activates an ADP-ribosylation factor, a molecule that is involved in vesicle trafficking. (medlineplus.gov)
  • mTOR activity is subjected to tight regulation in response to external nutrition and growth factor stimulation. (bvsalud.org)
  • In this review, we will summarize the earlier work establishing the ability of cAMP to dampen mTORC1 activation in response to insulin and growth factors and then discuss our recent findings demonstrating the regulation of mTOR signaling by the PKA- and PKG-dependent signaling pathways. (bvsalud.org)
  • Western blot testing of 1) human 293T, 2) rat brain and 3) mouse brain tissue lysate with ARL13B antibody. (nsjbio.com)
  • Approximately 70 years ago, several DNA viruses such as adenovirus, human Epstein-Barr virus, polyoma and SV40 were found to be able to cause tumors in humans and rodents [ 1 ] . (encyclopedia.pub)
  • ADP-ribosylation factor 1 is a member of the human ARF gene family. (thermofisher.com)
  • In the past biennium, working groups have concluded that there is sufficient evidence to classify infection with human immunodeficiency virus (HIV-1), human T-cell lymphotropic virus (HTLV-1), Epstein-Barr virus (EBV) and the Kaposi sarcoma-associated herpesvirus 8 as carcinogenic to humans (IARC 0RQRJUDSKV, Vol. 67 and 70). (who.int)
  • p53 supports tumor suppression through its roles as transcription factor and mitochondrial membrane permeabilization (to trigger apoptosis) and, indeed, the most investigated biological activity of p53 is its transcriptional activator role [ 17 ] . (encyclopedia.pub)
  • Shin HW, Morinaga N, Noda M, Nakayama K. BIG2, a guanine nucleotide exchange factor for ADP-ribosylation factors: its localization to recycling endosomes and implication in the endosome integrity. (medlineplus.gov)
  • The classical structural GDP/GTP switch is characterised by conformational changes at the so-called switch 1 and switch 2 regions, which bind tightly to the gamma-phosphate of GTP but poorly or not at all to the GDP nucleotide. (wikipedia.org)
  • Lysates were probed with an ARF4 polyclonal antibody (Product # PA5-37841) at a dilution of 0.5 µg/mL and incubated for 1 hour, followed by chemiluminescent detection. (thermofisher.com)
  • Jackson, C. L. & Casanova, J. E. Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors. (nature.com)
  • This gene encodes a member of the ADP-ribosylation factor-like family. (nsjbio.com)
  • Alzheimer disease (AD) is the most common dementia type and may account for 60-70% of dementia cases [ 1 ]. (biomedcentral.com)
  • The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. (sfari.org)
  • Both anabolic phenotype and inflammatory pathology are proposed to be dependent on hypoxia-inducible factor 2 alpha (HIF-2α). (biomedcentral.com)
  • The following product was used in this experiment: ARL1 Polyclonal Antibody from Thermo Fisher Scientific, catalog # 16012-1-AP. (thermofisher.com)
  • Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors. (nih.gov)
  • ARNO is a soluble guanine nucleotide exchange factor (GEF) for the Arf family of GTPases. (omicsdi.org)
  • We report in the present paper the identification of the ARF (ADP-ribosylation factor) exchange factor GBF1 (Golgi-specific brefeldin A-resistant guanine nucleotide-exchange factor 1) as a Golgi phosphoprotein. (bris.ac.uk)
  • 1. TRPV4 Regulates Breast Cancer Cell Extravasation, Stiffness and Actin Cortex. (nih.gov)
  • 17. CRP2, a new invadopodia actin bundling factor critically promotes breast cancer cell invasion and metastasis. (nih.gov)
  • actin filament associated protein 1 [S. (gsea-msigdb.org)
  • The name ADP-ribosylation factor derives from the discovery, in 1984, of the factor that confers sensitivity of the stimulator of adenylate cyclase (Gs) to cholera toxin, an ADP-ribosyltransferase (4). (nih.gov)
  • SPG61 is due to a mutation in the ARL6IP1 gene (16p12-p11.2) encoding the ADP-ribosylation factor-like protein 6-interacting protein 1. (cdc.gov)
  • The encoded protein is localized to the Golgi apparatus and plays a role in vesicular trafficking by activating ADP ribosylation factor 1. (utsouthwestern.edu)
  • Mus musculus ADP-ribosylation factor-like 3 (Arl3), transcript variant 2, mRNA. (genscript.com)
  • We have show that Arl4 and Arl13b but not Arl3 are interact with polycystin-1 in HEK 293 cells by co-immunoprecipitation. (nih.gov)
  • Co-expression of Sar1-H79G (His79-->Gly) and recombinant, epitope-tagged CS, CSHA1 (where HA1 stands for nine-amino-acid epitope of the viral haemagglutinin 1), barred segregation of CSHA1 to TC. (unipd.it)
  • Fig. 1: Cis elements in FGF2 required for unconventional secretion from tumor cells. (db-engine.de)
  • Finally, the molecular mechanism of FGF2 secretion is used in the lab to develop inhibitors of this process with great potential for the development of drugs for cancer therapy that block the function of FGF2 as a tumor cell survival factor. (db-engine.de)
  • The polycystin-1, lipoxygenase, alpha-toxin (PLAT) domain is found in the first intracellular loop of polycystin-1 and its family members. (nih.gov)
  • chloride intracellular channel 1 [Sour. (gsea-msigdb.org)
  • X-Ray Crystal Structure of the Anthrax Lethal Factor Bound to a Small Molecule Inhibitor, BI-MFM3, 3-{5-[5-(4-Chloro-phenyl)-furan-2-ylmethylene]-4-oxo-2-thioxo-thiazolidin-3-yl}-propionic acid. (berkeley.edu)
  • Allergic rhinitis (AR) is a chronic inflammatory disease of the nasal mucosa mediated by immunoglobulin E (IgE) ( 1 ). (spandidos-publications.com)
  • Previously, treatment of a disease with biological factors and products which are treed in D24, required coordination of the disease with /therapy rather than /drug therapy. (nih.gov)
  • Decreased Expression of Cilia Genes in Pancreatic Islets as a Risk Factor for Type 2 Diabetes in Mice and Humans. (sfb958.de)
  • Moreover, knockdown of TMF-1 by small interfering RNA decreased nuclear translocation of PDGFRβ and caused significant up-regulation of the Brg-1/p53-regulated cell cycle inhibitor CDKN1A (encoding p21) without affecting PDGFRβ-inducible immediate-early genes. (silverchair.com)
  • Clinically, lobomycosis manifests as slow-growing, nodular lesions that can lead to disfigurement and functional impairment if left untreated ( 1 ). (cdc.gov)
  • The Golgi apparatus is a highly reactive organelle that exhibits functional and morphological perturbations in response to molecular-level and contextual factors. (molcells.org)
  • In the nucleus, PDGFRβ formed ligand-inducible complexes with the tyrosine kinase Fer and its substrate, TATA element-modifying factor 1 (TMF-1). (silverchair.com)
  • GBF1 is phosphorylated by CDK1 (cyclin-dependent kinase 1)-cyclin B in mitosis, which results in its dissociation from Golgi membranes. (bris.ac.uk)
  • ARFRP1 function is required for (1) the protein composition of LD coats to regulate lipolysis and lipidation of chylomicrons in the intestine, (2) correct sorting and recycling of the insulin receptor in adipose tissue, and (3) hormone secretion from adipocytes (adiponectin) and pancreatic beta-cells (insulin). (sfb958.de)
  • Association between epidermal growth factor receptor amplification and ADP-ribosylation factor 1 methylation in human glioblastoma. (cancerindex.org)
  • In addition, it has been found that the epidermal growth factor receptor gene (EGFR) is frequently over-expressed and amplified in primary GBs. (cancerindex.org)
  • In this paper, we show that a fraction of full-length cell surface platelet-derived growth factor (PDGF) receptor β (PDGFRβ) accumulates in the nucleus at the chromatin and the nuclear matrix after ligand stimulation. (silverchair.com)
  • Analysis of the resultant clones result in tour target protein as ADP ribosylation factor like 4 (Arl4). (nih.gov)
  • tRNA wybutosine-synthesizing protein 1 homolog,Rad. (wfleabase.org)
  • Collectively, our results suggest that the mechanism of activation of a mammalian non-voltage-activated Na(+)-selective current requires an Arf small G-protein, most probably Arf-1. (ox.ac.uk)
  • NSF, SNAPs, and synaptobrevins) that appear to serve a common role in membrane traffic, synaptic transmission, and organelle remodeling (1). (nih.gov)
  • We learned this from in vitro assays of membrane traffic, including those for intra-Golgi transport and nuclear vesicle and endosome fusion, which are inhibited by GTPgS and require the addition of cytosol or a cytosolic factor (7,8). (nih.gov)
  • Dendritic cells (DCs), which are a major subtype of antigen-presenting cells (APCs), serve a key role in the immunopathogenesis of AR ( 1 , 2 ). (spandidos-publications.com)
  • Mast cells are best known for their role in immunoglobulin E (IgE)-dependent allergic responses as one of the most powerful reactions of the immune system [ 1 ]. (biomedcentral.com)
  • Recent studies suggest that mast cells may also be involved in innate and adaptive immunity by producing high levels of chemokines and cytokines [ 1 - 3 ]. (biomedcentral.com)
  • 15. Role of the focal adhesion protein kindlin-1 in breast cancer growth and lung metastasis. (nih.gov)