ADP-Ribosylation Factors: 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 3.6.1.47ADP-Ribosylation Factor 1: 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.Brefeldin A: A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.Coated Vesicles: 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.Coatomer Protein: 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.Guanine Nucleotide Exchange Factors: Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.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.-.Coat Protein Complex I: 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.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)GTPase-Activating Proteins: Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.Adenosine Diphosphate Ribose: 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.Phospholipase D: 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'-O-(3-Thiotriphosphate): 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 Triphosphate: Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.Nucleoside Diphosphate SugarsAdenosine Diphosphate Sugars: Esters formed between the aldehydic carbon of sugars and the terminal phosphate of adenosine diphosphate.Endocytosis: Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.Protein Transport: 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.Protein Binding: 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.Ribose: A pentose active in biological systems usually in its D-form.Membrane Proteins: 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.HeLa Cells: 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.ADP Ribose Transferases: 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.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Molecular Sequence Data: 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.Cholera Toxin: 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 Fusion Proteins: 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.Amino Acid Sequence: 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.Pertussis Toxin: 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.Virulence Factors, Bordetella: 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.Mutation: 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 Diphosphate: Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.Poly(ADP-ribose) Polymerases: 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.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Botulinum Toxins: 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.NAD: 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)Adenylate Cyclase: An enzyme of the lyase class that catalyzes the formation of CYCLIC AMP and pyrophosphate from ATP. EC 4.6.1.1.Adenylate Cyclase Toxin: One of the virulence factors produced by virulent BORDETELLA organisms. It is a bifunctional protein with both ADENYLYL CYCLASES and hemolysin components.Poly Adenosine Diphosphate Ribose: A polynucleotide formed from the ADP-RIBOSE moiety of nicotinamide-adenine dinucleotide (NAD) by POLY(ADP-RIBOSE) POLYMERASES.Phosphatidylinositol 4,5-Diphosphate: 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)Bacterial Toxins: 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.Kinetics: The rate dynamics in chemical or physical systems.Adaptor Proteins, Vesicular Transport: 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.rhoA GTP-Binding Protein: 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.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Azaguanine: One of the early purine analogs showing antineoplastic activity. It functions as an antimetabolite and is easily incorporated into ribonucleic acids.Intracellular Membranes: 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.Enzyme Activation: 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.Biological Transport: 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.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Proteins: 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+ NucleosidaseCloning, Molecular: 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.Tankyrases: A group of telomere associated proteins that interact with TRF1 PROTEIN, contain ANKYRIN REPEATS and have poly(ADP-ribose) polymerase activity.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.CHO Cells: 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.Mitochondrial ADP, ATP Translocases: 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.Signal Transduction: 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, Cultured: 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)

Promotes guanine-nucleotide exchange on ARF1 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. Play a role in the epithelial polarization (By similarity).
Ver más] The small GTP-binding protein ADP-ribosylation factor 1 (ARF1) is an essential component of the molecular machinery that catalyzes the formation of membranebound transport intermediates. By using an in vitro assay that reproduces recruitment of cytosolic proteins onto purified, high salt-washed Golgi membranes, we have analyzed the role of cAMP-dependent protein kinase A (PKA) on ARF1 incorporation. Addition to this assay of either pure catalytic subunits of PKA (C-PKA) or cAMP increased ARF1 binding. By contrast, ARF1 association was inhibited following C-PKA inactivation with either PKA inhibitory peptide or RIIa as well as after cytosol depletion of C-PKA. C-PKA also stimulated recruitment and activation of a recombinant form of human ARF1 in the absence of additional cytosolic components. The binding step could be dissociated from the activation reaction and found to be independent of guanine nucleotides and saturable. This step was stimulated by C-PKA in an ATP-dependent manner. ...
TY - JOUR. T1 - ADP ribosylation factor 6 regulates neuronal migration in the developing cerebral cortex through FIP3/arfophilin-1-dependent endosomal trafficking of N-cadherin. AU - Hara, Yoshinobu. AU - Fukaya, Masahiro. AU - Hayashi, Kanehiro. AU - Kawauchi, Takeshi. AU - Nakajima, Kazunori. AU - Sakagami, Hiroyuki. PY - 2016. Y1 - 2016. N2 - During neural development, endosomal trafficking controls cell shape and motility through the polarized transport of membrane proteins related to cellcell and cellextracellular matrix interactions. ADP ribosylation factor 6 (Arf6) is a critical small GTPase that regulates membrane trafficking between the plasma membrane and endosomes. We herein demonstrated that the knockdown of endogenous Arf6 in mouse cerebral cortices led to impaired neuronal migration in the intermediate zone and cytoplasmic retention of N-cadherin and syntaxin12 in migrating neurons. Rescue experiments with separation-of-function Arf6 mutants identified Rab11 familyinteracting ...
D. Jones, B. Bax, S. Cockcroft; ADP-ribosylation factor GTPases in signal transduction and membrane traffic: independent functions?. Biochem Soc Trans 1 August 1999; 27 (4): 642-647. doi: https://doi.org/10.1042/bst0270642. Download citation file:. ...
Top performende anti-Ratte (Rattus) ADP-Ribosylation Factor 1 Antikörper für Immunofluorescence (Paraffin-embedded Sections) (IF (p)) vergleichen & kaufen.
Cell migration is an orchestrated and highly coordinated multi-step process that is central to the development and maintenance of multicellular organisms. Dysregulated migration however, is associated with pathological states such as tumor formation and metastasis; thus a clear understanding of the molecular mechanisms that drive this process is critical to the development of counteracting therapeutics. Cell migration and adhesion-dependent cell spreading share a number of features. For example, both processes rely on the activation of mechanisms for the coordinated spatial and temporal assembly/disassembly of focal adhesions, as well as mechanisms controlling actin rearrangements and directed vesicular trafficking. Actin remodeling and vesicular trafficking events are in turn, implicated functions of a variety of small GTPases of the Ras superfamily, which include the Rho and Arf subfamilies. Thus towards efforts of further characterizing the molecular pathways that drive cell spreading, I pursued aims
COPⅠ囊泡:最初研究者利用三磷酸鳥苷(GTP)衍生物GTPγS(一種富含高爾基體膜的細胞質與抗水解的GTP衍生物)共培養時,發現高爾基體池之間存在一種囊泡轉運結構[9](後來在真核細胞中也證實此結構的存在[10])。除了脂質成分外,參與此囊泡形成的成份還有7種外被體蛋白(即外被體α、β、β′、γ、δ、ε、ζ)。這些外被體蛋白相互作用形成的復合物就是COPⅠ囊泡[11][12]。亞單位α、β′、ε在結構上與網格蛋白及COPⅡ囊泡的外層組分具有較高的一致性,形成復合物的內層組分稱為B亞復合物(主要負責與靶蛋白結合),而亞單位β、γ、δ、ζ 與網格蛋白及COPⅡ囊泡的內層組分相似,形成復合物的內層組分稱為F亞復合物,該亞復合物主要負責與靶蛋白結合,並且直接與COPⅠ囊泡形成的招募者ADP核糖基化因子(英语:ADP ribosylation factor)(ADP ribosylation ...
Angiogenesis: Growth of new blood vessels by sprouting from existing ones. Anoxia: a condition characterized by an absence of oxygen supply to an organ or a tissue Apoptosis: Form of cell death, also known as programmed cell death, in which a suicide program is activated within the cell, leading to fragmentation of the DNA, shrinkage of the cytoplasm, membrane changes and cell death without lysis or damage to neighboring cells. It is a normal phenomenon, occurring frequently in a multicellular organism. ARF: ADP Ribosylation Factor (ARF) is a member of the GTP-binding proteins responsible for regulating both COPI coat assembly and clathrin coat assembly at Golgi membranes. ATM: a protein that regulates several cellular responses to DNA breaks. C. elegans: Caenorhabditis elegans is a nematode (unsegmented) worm with very simple anatomy. Chaperone (molecular chaperone): Protein that helps other proteins avoid misfolding pathways that produce inactive or aggregated polypeptides. Drosophila: ...
The protein encoded by this gene catalyzes the hydrolysis of phosphatidylcholine to phosphatidic acid and choline. The activity of the encoded enzyme is enhanced by phosphatidylinositol 4,5-bisphosphate and ADP-ribosylation factor-1. This protein localizes to the peripheral membrane and may be involved in cytoskeletal organization, cell cycle control, transcriptional regulation, and/or regulated secretion. Two transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Jul 2011 ...
Lyophilized antibodies can be kept at 4ºC for up to 3 months and should be kept at -20ºC for long-term storage (2 years). To avoid freeze-thaw cycles, reconstituted antibodies should be aliquoted before freezing for long-term (1 year) storage (-80ºC) or kept at 4ºC for short-term usage (2 months). For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made with the assay buffer. After the maximum long-term storage period (2 years lyophilized or 1 year reconstituted) antibodies should be tested in your assay with a standard sample to verify if you have noticed any decrease in their efficacy ...
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Complete information for ARF6 gene (Protein Coding), ADP Ribosylation Factor 6, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
ARF1 - ARF1 (untagged)-Human ADP-ribosylation factor 1 (ARF1), transcript variant 4 available for purchase from OriGene - Your Gene Company.
Complete information for ARL6IP6 gene (Protein Coding), ADP Ribosylation Factor Like GTPase 6 Interacting Protein 6, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
ARFGAP3 antibody, C-term (ADP-ribosylation factor GTPase activating protein 3) for WB. Anti-ARFGAP3 pAb (GTX89988) is tested in Mouse samples. 100% Ab-Assurance.
ADP-ribosylation factor, GTPase of the Ras superfamily involved in regulation of coated formation vesicles in intracellular trafficking within the ...
ARFIP2 antibody [N1C2] (ADP-ribosylation factor interacting protein 2) for IHC-P, WB. Anti-ARFIP2 pAb (GTX104241) is tested in Human samples. 100% Ab-Assurance.
Brefeldin A-inhibited guanine nucleotide-exchange protein 3 (BIG3) has been identified recently as a novel regulator of estrogen signalling in breast cancer cells. Despite being a potential target for new breast cancer treatment, its amino acid sequence suggests no association with any well-characterized protein family and provides little clues as to its molecular function. In this paper, we predicted the structure, function and interactions of BIG3 using a range of bioinformatic tools. Homology search results showed that BIG3 had distinct features from its paralogues, BIG1 and BIG2, with a unique region between the two shared domains, Sec7 and DUF1981. Although BIG3 contains Sec7 domain, the lack of the conserved motif and the critical glutamate residue suggested no potential guaninyl-exchange factor (GEF) activity. Fold recognition tools predicted BIG3 to adopt an α-helical repeat structure similar to that of the armadillo (ARM) family. Using state-of-the-art methods, we predicted interaction sites
This gene encodes a member of the GIT protein family, which interact with G protein-coupled receptor kinases and possess ADP-ribosylation factor (ARF) GTPase-activating protein (GAP) activity. GIT proteins traffic between cytoplasmic complexes, focal adhesions, and the cell periphery, and interact with Pak interacting exchange factor beta (PIX) to form large oligomeric complexes that transiently recruit other proteins. GIT proteins regulate cytoskeletal dynamics and participate in receptor internalization and membrane trafficking. This gene has been shown to repress lamellipodial extension and focal adhesion turnover, and is thought to regulate cell motility. This gene undergoes extensive alternative splicing to generate multiple isoforms, but the full-length nature of some of these variants has not been determined. The various isoforms have functional differences, with respect to ARF GAP activity and to G protein-coupled receptor kinase 2 binding. [provided by RefSeq, Sep 2008 ...
Coat protein complex I (COPI) vesicles are involved in transport processes within the early secretory pathway (Bethune et al., 2006). For their biogenesis, the small GTPase ADP ribosylation factor 1 (Arf1) in its GDP-bound form is recruited to the Golgi membrane by dimeric transmembrane proteins of the p24 family (Gommel et al., 2001) or by interaction with membrin (Honda et al., 2005). The membrane-associated Arf guanine nucleotide exchange factor GBF1 catalyzes exchange of the bound GDP to GTP (Zhao et al., 2006). Arf1-GTP dissociates from the p24 proteins and is inserted into the Golgi membrane (Franco et al., 1996; Antonny et al., 1997) as a dimer (Beck et al., 2008) to recruit the heptameric protein complex coatomer (Palmer et al., 1993). Coatomer polymerization leads to the formation of a COPI-coated vesicle (Bremser et al., 1999; Reinhard et al., 1999). Arf GTPase-activating proteins (GAPs) catalyze hydrolysis of the GTP bound to Arf1 followed by dissociation of the coat (Tanigawa et al., ...
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Arl1 (ARF like protein1) is a poorly understood member of ARF family small GTPases. This thesis presents an original characterization of Arl1 and its effectors. Arl1 was localized to the tans Golgi under EM. Over expression of guanine nucleotide mutants of Arl1 dramatically affects the structure and function of Golgi apparatus. Arl1-GTP was found to interact with GRIP domain of Golgins (Golgin-97, Golgin-245, GCC1 and KIAA0336). The interaction was dependent on the conserved amino acids on both switch II region of Arl1 and the GRIP domain. Collectively, the research presented in this thesis reveals Arl1 is a new regulator of Golgi structure and function and one mechanism of Arl1a??s function is that it recruits and regulates its effectors a?? GRIP domain Golgins to Golgi ...
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a member of the GIT protein family, which interact with G protein-coupled receptor kinases and possess ADP-ribosylation factor (ARF) GTPase-activating protein (GAP) activity. GIT proteins traffic between cytoplasmic complexes, focal adhesions, and the cell periphery, and interact with Pak interacting exchange factor beta (PIX) to form large oligomeric complexes that transiently recruit other proteins. GIT proteins regulate cytoskeletal dynamics and participate in receptor internalization and membrane trafficking. This gene has been shown to repress lamellipodial extension and focal adhesion turnover, and is thought to regulate cell motility. This gene undergoes extensive alternative splicing to generate multiple isoforms, but the full-length nature of some of these variants has not been determined. The various isoforms have functional differences, with respect to ARF GAP activity ...
Two widely expressed mammalian phosphatidylcholine (PC)-specific phospholipases D (PLD), PLD1 and PLD2, have been identified. Recombinantly expressed PLD2 has high basal activity and is insensitive to GTP-binding protein activators of PLD1 [Colley, W. C., et al. (1997) Curr. Biol. 7, 191-201]. To investigate the regulation of PLD2 we isolated PLD2, from mouse brain by immunoaffinity chromatography. The native and recombinant proteins have indistinguishable properties: PLD2 is potently activated by phosphoinositides with a vicinal 4,5-phosphate pair but is not stimulated by guanosine 5-O-(3-thio triphosphate)-activated ADP-ribosylation factor-1, Rho family GTP-binding proteins, or protein kinases C-alpha, or -beta1 ...
Other than a role for Ca2+ store depletion, the molecular mechanisms that regulate antigen-stimulated Ca2+ influx into mast cells are not well-understood. The observation that CT dramatically enhances 45Ca2+ influx into RBL-2H3 cells suggests that this reagent might be a useful tool to study the Ca2+ entry pathway (Narasimhan et al., 1988). That CT amplifies both antigen-evoked ICRAC and 45Ca2+ influx to a similar extent bolsters the idea that CRAC channels are a major pathway for FcεRI-mediated Ca2+ uptake into RBL-2H3 mast cells (Zhang and McCloskey, 1995).. Two hypotheses to explain the effect of CT on 45Ca2+ influx are immediately testable by patch clamping. First, it is possible that CT activates Cl− or K+ channels, and thereby increases the electrical force propelling Ca2+ entry. This indirect mechanism cannot explain the enhancement of Ca2+ influx currents that we observed, because voltage-clamp measurements eliminate any difference in membrane potential between control and CT-treated ...
GTP-binding protein involved in protein trafficking that regulates endocytic recycling and cytoskeleton remodeling. Required for normal completion of mitotic cytokinesis. May also modulate vesicle budding and uncoating within the Golgi apparatus. Involved in the regulation of dendritic spine development, contributing to the regulation of dendritic branching and filopodia extension (PubMed:16672654). Involved in epithelial polarization (By similarity).
ADP ribosylation factor 1 (Arf1). Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi complex, where it is believed to recruit effector proteins to the trans-Golgi network. Like most members of the Arf family, Arl1 is myristoylated at its N-terminal helix and mutation of the myristoylation site disrupts Golgi targeting. In humans, the Golgi-localized proteins golgin-97 and golgin-245 have been identified as Arl1 effectors. Golgins are large coiled-coil proteins found in the Golgi, and these golgins contain a C-terminal GRIP domain, which is the site of Arl1 binding. Additional Arl1 effectors include the GARP (Golgi-associated retrograde protein)/VFT (Vps53) vesicle-tethering complex and Arfaptin 2. Arl1 is not required for exocytosis, but appears necessary for trafficking from the endosomes to the Golgi. In Drosophila zygotes, mutation of Arl1 is lethal, and in the host-bloodstream form of Trypanosoma brucei, Arl1 is essential for viability. ...
BFA induces the ADP-ribosylation of BARS-50 and GAPDH in permeabilized cells. (A) RBL cells were permeabilized with 3 U/ml SLO and exposed to 10 μg/ml BFA
Stimulates the exchange of guanyl nucleotides associated with the GTPase ARF. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase ...
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Arfgef1 (untagged) - Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited) (Arfgef1), (10ug), 10 µg.
We recently reported that brefeldin A-inhibited guanine nucleotide-exchange proteins 3 (BIG3) binds Prohibitin 2 (PHB2) in cytoplasm, thereby leading to a reduction of function of the PHB2 growth suppressor in the nuclei of breasts tumor cells. PHB2 nuclear transfer may offer restorative strategies for managing Elizabeth2/Emergency room signs in breasts tumor cells. Introduction Prohibitin 1 and 2 (PHB and buy 808118-40-3 PHB2) proteins are highly conserved in eukaryotic cells and exhibit diverse subcellular localization with different functions [1C3]. These molecules are primarily observed in inner mitochondrial membranes via their buy 808118-40-3 N-terminal transmembrane domain but are also present in several other localizations such as the cytosol, endoplasmic reticulum, nucleus, and plasma membrane [1]. Both proteins form hetero-oligomeric ring structures in the inner mitochondrial membrane and function as chaperones buy 808118-40-3 that maintain mitochondrial integrity and stabilize ...
FUNCTION: Guanine nucleotide-exchange factor (GEF) required for the formation or budding of transport vesicles from the ER. This function involves the cytoplasmic domain of the protein, which is thought to interact with the small GTP-binding protein SAR1. Required for autophagy. MISCELLANEOUS: In the process of transport, SEC12 itself may migrate to the Golgi apparatus and function in subsequent transport events. MISCELLANEOUS: Present with 6160 molecules/cell in log phase SD medium ...
The small GTP-binding proteins of the ARF family play a central role in membrane dynamics and protein transport in eukaryotic cells. The GEFs that catalyze GDP/GTP exchange on ARF are of critical importance to ARF function, as they determine when and where ARF proteins will be activated within the cell (reviewed by Jackson and Casanova, 2000). We present here an in vivo characterization of the Gea1p and Gea2p ARF GEFs in the secretory pathway of S. cerevisiae. The Gea1p and Gea2p proteins are members of a subfamily of ARF GEFs with members in plants and animals, as well as in yeast ( Claude et al., 1999; Steinmann et al., 1999). This subfamily is distinct from that of Sec7p and its mammalian orthologues BIG1 and BIG2 ( Mansour et al., 1999; Morinaga et al., 1997; Togawa et al., 1999).. The Gea1p and Gea2p proteins are functionally redundant, but at least one is necessary for viability in yeast. We have generated three temperature-sensitive gea mutants and have examined their phenotypes. The ...
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Arginine adenosine-5′-diphosphoribosylation (ADP-ribosylation) is an enzyme-catalyzed potentially reversible posttranslational changes where the ADP-ribose moiety is transferred from NAD+ towards the guanidino CHR2797 moiety of arginine. proteins with binding companions e.g. toxin-catalyzed ADP-ribosylation of actin at R177 blocks actin polymerization sterically. In case there is the nucleotide-gated P2X7 ion route ADP-ribosylation at R125 near the ligand-binding site causes route Rabbit Polyclonal to SF3B3. gating. Arginine-specific ADP-ribosyltransferases (ARTs) bring a quality R-S-EXE theme that distinguishes these enzymes from structurally related enzymes which catalyze ADP-ribosylation of additional amino acid part chains DNA or little substances. Arginine-specific ADP-ribosylation could be inhibited by little molecule arginine analogues such as for example CHR2797 agmatine or meta-iodobenzylguanidine (MIBG) which themselves can serve as focuses on for arginine-specific ARTs. ...
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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 ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
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Microinjection of the slowly hydrolyzable GTP analogue GTP(gamma)S or the ectopic expression of a GTP restricted mutant of the small GTPase arf1 (arf1[Q71L]) leads to the rapid accumulation of COPI coated vesicles and buds in living cells. This effect is blocked at 15 degrees C and by microinjection of antibodies against (beta)-COP. Anterograde and retrograde membrane protein transport markers, which have been previously shown to be incorporated into COPI vesicles between the endoplasmic reticulum and Golgi complex, are depleted from the GTP(gamma)S or arf1[Q71L] induced COPI coated vesicles and buds. In contrast, in control cells 30 to 60% of the COPI carriers co-localize with these markers. These in vivo data corroborate recent in vitro work, suggesting that GTP(gamma)S and arf1[Q71L] interfere with the sorting of membrane proteins into Golgi derived COPI vesicles, and provide the first in vivo evidence for a role of GTP hydrolysis by arf1 in the sorting of cargo into COPI coated vesicles and ...
CIN85 is a multidomain adaptor protein involved in Cbl-mediated down-regulation of epidermal growth factor (EGF) receptors. CIN85 src homology 3 domains specifically bind to a proline-arginine (PxxxPR) motif in Cbl, and this association seems to be important for EGF receptor endocytosis. Here, we report identification of novel CIN85 effectors, all containing one or more PxxxPR motifs, that are indispensable for their mutual interactions. These effectors include phosphatidyl-inositol phosphatases SHIP-1 and synaptojanin 2B1, Arf GTPase-activating proteins ASAP1 and ARAP3, adaptor proteins Hip1R and STAP1, and a Rho exchange factor, p115Rho GEF. Acting as a molecular scaffold, CIN85 clusters its effectors and recruits them to high-molecular-weight complexes in cytosolic extracts of cells. Further characterization of CIN85 binding to ASAP1 revealed that formation of the complex is independent on cell stimulation. Overexpression of ASAP1 increased EGF receptor recycling, whereas ASAP1 containing ...
Small GTPases largely control membrane traffic, which is essential for the survival of all eukaryotes. Among the small GTP-binding proteins, ARF1 (ADP-ribosylation factor 1) and SAR1 (Secretion-Associated RAS super family 1) are commonly conserved among all eukaryotes with respect to both their functional and sequential characteristics. The ARF1 and SAR1 GTP-binding proteins are involved in the formation and budding of vesicles throughout plant endomembrane systems. ARF1 has been shown to play a critical role in COPI (Coat Protein Complex I)-mediated retrograde trafficking in eukaryotic systems, whereas SAR1 GTPases are involved in intracellular COPII-mediated protein trafficking from the ER to the Golgi apparatus. This review offers a summary of vesicular trafficking with an emphasis on the ARF1 and SAR1 expression patterns at early growth stages and in the de-etiolation process.
Hong Xu wrote: , , Dear Colleagues: , , Our group is using the Clontech s HeLa cDNA library in a yeast , two-hybrid screening with the bait fused to the GAL4AD and the yeast , strain CG 1945. Many of the clones sequenced show one of the following , sequences, including ITBA2 (whatever it is, since almost no references , can be found in Medline), ribosomal s20, transketolase, Ring12 (probably , a proteasome subunit), ADP ribosylation factor, etc., with those listed , above showing up most frequently. We would like to know whether or not , these factors have also been found in somebody else two-hybrid , screenings using the same Clontech HeLa library. , , You are welcome to post your answer to our question in this newsgroup. , Or you can call me at 973-781-7987. , , Thank you very much. , , Richard Dear Richard, try this URL and you find an overview of the most common trash found in two hybrid screens: http://www.fccc.edu/research/labs/golemis/main_false.html Hope this helps, Ricky ...
The KOMP Repository is located at the University of California Davis and Childrens Hospital Oakland Research Institute. Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International +1-530-752-KOMP, or for vectors [email protected] or +1-510-450-7917 ...
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CONTACT: [email protected] GENBANK UPDATE: 22 July 1997 28 unique yeast ORFs ORF NAME LOCUS PRODUCT/DESCRIPTION -------- ----- ---------------------------------------- YFL039C ACT1 Actin YDL192W ARF1 ADP-ribosylation factor YDL137W ARF2 ADP-ribosylation factor 2 YJR121W ATP2 F(1)F(0)-ATPase complex beta subunit, mitochondrial YER177W BMH1 Homolog of mammalian 14-3-3 proteins YLR229C CDC42 member of the Rho subfamily of Ras-like proteins YER133W GLC7 protein phosphatase type I YLR293C GSP1 GTP-binding protein YOR185C GSP2 GTP-binding protein YBR009C HHF1 Histone H4 (HHF1 and HHF2 code for identical proteins) YNL030W HHF2 Histone H4 (HHF1 and HHF2 code for identical proteins) YBR010W HHT1 Histone H3 (HHT1 and HHT2 code for identical proteins) YNL031C HHT2 Histone H3 (HHT1 and HHT2 code for identical proteins) YDR224C HTB1 Histone H2B (HTB1 and HTB2 code for nearly identical proteins) YBL002W HTB2 Histone H2B (HTB1 and HTB2 code for nearly identical proteins) YBL087C RPL17A Ribosomal protein ...
ARF GAP Lis a kind of important regulator of introcellular transport. Recently, a novel human gene has been found from a cDNA library of second trimester human fetal liver. The amino acid sequence encoded by the novel gene has 32% similarity to rat ARF1 GAP, was thus termed as ARFGAP3. Functional studies of the new gene were performed. The full-length cDNA of ARFGAP3 was amplified from the human total placenta RNA by RT-PCR technique, then subcloned into pGEM-T vector and sequenced. The RNA Master blot and multiple tissue Northern blot analysis were used to define the expression profile and the transcript size of ARFGAP3 in human tissues. It was shown that ARFGAP3 was strongly expressed in glands and testis and that ARFGAP3 mRNA existed as only one kind of transcript of 2.7 kb in various human tissues. Then, the expression and purification of the recombinant human ARFGAP3 (rhARFGAP3) were performed. It was demonstrated that rhARFGAP3 exhibited strong GTPase-activating protein ( GAP) activity ...
TY - JOUR. T1 - Active Arf6 recruits ARNO/cytohesin GEFs to the PM by binding their PH domains. AU - Cohen, Lee Ann. AU - Honda, Akira. AU - Várnai, P.. AU - Brown, Fraser D.. AU - Balla, Tamas. AU - Donaldson, Julie G.. PY - 2007/6. Y1 - 2007/6. N2 - ARNO is a soluble guanine nucleotide exchange factor (GEF) for the Arf family of GTPases. Although in biochemical assays ARNO prefers Arf1 over Arf6 as a substrate, its localization in cells at the plasma membrane (PM) suggests an interaction with Arf6. In this study, we found that ARNO activated Arf1 in HeLa and COS-7 cells resulting in the recruitment of Arf1 on to dynamic PM ruffles. By contrast, Arf6 was activated less by ARNO than EFA6, a canonical Arf6 GEF. Remarkably, Arf6 in its GTP-bound form recruited ARNO to the PM and the two proteins could be immunoprecipitated. ARNO binding to Arf6 was not mediated through the catalytic Sec7 domain, but via the pleckstrin homology (PH) domain. Active Arf6 also bound the PH domain of Grp1, another ...
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The KOMP Repository is located at the University of California Davis and Childrens Hospital Oakland Research Institute. Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International +1-530-752-KOMP, or for vectors [email protected] or +1-510-450-7917 ...

Wst p.

Zwi zek nowotworowego rozrostu r dnab onkowego wysokiego stopnia (HG-PIN) i atypowego rozrostu drobnozrazikowego (ASAP) z rozwojem raka stercza nadal nie jest jasny, zw aszcza w przypadku ASAP.

Cel pracy.

Celem pracy by o okre lenie cz sto ci rozpoznania raka oraz zmian przednowotworowych w r d pacjent w poddanych pierwszej i kolejnej biopsji transrektalnej stercza pod kontrol USG (TRUS) oraz analiza wynik w kolejnych biopsji w grupie pacjent w z ASAP i HG-PIN, uzyskanych w pierwszej biopsji.

Materia i metoda.

Ocenie poddano 928 pacjent w, u kt rych wykonano od 6- do 12-skrawkow biopsj stercza pod kontrol TRUS. U pacjent w, u kt rych stwierdzono ASAP b d PIN w pierwszej biopsji, b d podejrzewano rozw j raka, po 4-6 miesi cach wykonano kolejn biopsj (rozszerzon do 10-16 skrawk w).

Wyniki.

Raka stwierdzono u 300 (32,3%) pacjent w poddanych biopsji, za stany przedrakowe (ASAP, HG-PIN) u 135 (14,54%), z czego ASAP u 50 (5,38%), HG
No. You are not. But, were odd like that. We also yell, No one expects the Spanish Inquisition! whenever anybody says that they didnt expect something. Im not sure these are things to brag about.. ...
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BACKGROUND INFORMATION: ARAP1 is an Arf (ADP-ribosylation factor)-directed GAP (GTPase-activating protein) that inhibits the trafficking of EGFR (epidermal growth factor receptor) to the early endosome. To further understand the function of ARAP1, we sought to identify proteins that interact with ARAP1. RESULTS: Here we report that ARAP1 associates with the CIN85 (Cbl-interacting protein of 85 kDa). Arg86 and Arg90 of ARAP1 and the SH3 (Src homology 3) domains of CIN85 are necessary for the interaction. We found that a mutant of ARAP1 with reduced affinity for CIN85 does not efficiently rescue the effect of reduced ARAP1 expression on EGFR trafficking to the early endosome. Reduced expression of CIN85 has a similar effect as reduced expression of ARAP1 on traffic of the EGFR. Cbl proteins regulate the endocytic trafficking of the EGFR by mediating ubiquitination of the EGFR. Overexpression of ARAP1 reduced ubiquitination of the EGFR by Cbl and slowed Cbl-dependent degradation of the EGFR. ...
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Golgi coated bud formation is blocked by ARF depletion and restored by purified ARF. Replicas of Golgi membranes after a 15-min transport incubation were prepa
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We have demonstrated previously the potent activation of PLD by the chemokine IL-8 in T lymphocytes (18). We have now extended our findings to include the C-C chemokine RANTES in demonstrating that in the Jurkat T cell line, the activation of this enzyme occurs at subnanomolar concentrations and is dependent on the activation of small GTP-binding protein cofactors. RANTES-induced PLD activation is consistently maximal at 1 nM, a concentration corresponding to the optimal chemotaxis-inducing dose in normal T lymphocytes. Interestingly, PLD activation in T lymphocytes and Jurkat T cells appears to be an important biologic consequence of chemokine action and more readily measurable (at nanomolar concentrations) than readouts of receptor activation such as calcium flux. It was also apparent that RANTES is the only chemokine tested to date (RANTES, MIP-1α, MIP-1β, MCP-1, MCP-3, lymphotactin) that induces as robust a response as seen in this study, although the others listed were capable of low ...
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Expression of ARFGAP2 (FLJ14576, IRZ, Zfp289, ZNF289) in epididymis tissue. Antibody staining with HPA016649 and HPA018152 in immunohistochemistry.
Component Of The Exomer Complex; Exomer Also Contains Csh6p, Bch1p, Bch2p, And Bud7p And Is Involved In Export Of Selected Proteins, Such As Chitin Synthase Chs3p, From The Golgi To The Plasma Membrane; Chs5p Is The Only Protein With A BRCT Domain That Is Not Localized To The Nucleus
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ADP-ribosylation is the addition of one or more ADP-ribose moieties to a protein. It is a reversible post-translational modification that is involved in many cellular processes, including cell signaling, DNA repair, gene regulation and apoptosis. Improper ADP-ribosylation has been implicated in some forms of cancer. It is also the basis for the toxicity of bacterial compounds such as cholera toxin, diphtheria toxin, and others. The first suggestion of ADP-ribosylation surfaced during the early 1960s. At this time, Pierre Chambon and coworkers observed the incorporation of ATP into hen liver nuclei extract. After extensive studies on the acid insoluble fraction, several different research laboratories were able to identify ADP-ribose, derived from NAD+, as the incorporated group. Several years later, the enzymes responsible for this incorporation were identified and given the name poly (ADP-ribose) polymerase. Originally, this group was thought to be a linear sequence of ADP-ribose units ...
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The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP-ribosylation, histone deacetylation, and in some Ca2+ signaling pathways. NMNAT (EC 2.7.7.1) is a central enzyme in NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD.[7] NMNAT1 is the most widely expressed of three orthologous genes with nicotinamide-nucleotide adenylyltransferase (NMNAT) activity. Genetically engineered mice lacking NMNAT1 die during early embryogenesis, indicating a critical role of this gene in organismal viability.[citation needed] In contrast, mice lacking NMNAT2, which is expressed predominantly in neural tissues, complete development but die shortly after birth. However, NMNAT1 is dispensable for cell viability, as homozygous deletion of this gene occurs in glioblastoma tumors and cell lines. NMNAT enzymatic activity is probably ...
OUTLINE: Using molecular laboratory techniques, this study examines the biochemical mechanisms by which LZAP activates transcriptional, tumor suppressive activity (both p53-dependent and p53-independent) of ARF and inhibits transcriptional, tumorigenic activity of NF-kB. LZAP regulation of newly identified ARF activities, such as S-phase delay and ARF-mediated B23 degradation are also evaluated. LZAPs tumor suppressive activity is assessed in vivo using a conditional knockout vector to target LZAP in mice and to observe for spontaneous and induced tumor formation. Laboratory analyses used to determine study endpoints include standard recombinant DNA, recombinant protein expression and purification, cell culture and transfection, cell labeling, reporter assays, flow cytometry, yeast-two hybrid, immunoprecipitation, immunoblotting, immunofluorescence, TUNEL assay, ELISA assay, Southern blotting, and protein and gene expression. ...
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TY - JOUR. T1 - An Integrated Chemical Proteomics Approach for Quantitative Profiling of Intracellular ADP-Ribosylation. AU - Kalesh, Karunakaran. AU - Lukauskas, Saulius. AU - Borg, Aaron J.. AU - Snijders, Ambrosius P.. AU - Ayyappan, Vinay. AU - Leung, Anthony K.L.. AU - Haskard, Dorian O.. AU - DiMaggio, Peter A.. PY - 2019/12/1. Y1 - 2019/12/1. N2 - ADP-ribosylation is integral to a diverse range of cellular processes such as DNA repair, chromatin regulation and RNA processing. However, proteome-wide investigation of its cellular functions has been limited due to numerous technical challenges including the complexity of the poly(ADP-ribose) (PAR) chains, low abundance of the modification and lack of sensitive enrichment methods. We herein show that an adenosine analogue with a terminal alkyne functionality at position 2 of the adenine (2-alkyne adenosine or 2YnAd) is suitable for selective enrichment, fluorescence detection and mass spectrometry proteomics analysis of the candidate ...
Arf-like protein 1 (Arl1) is a member of the Arf family of regulatory GTPases, within the Ras superfamily of GTPases, and with highly conserved orthologs throughout eukaryotes. Arl1 is essential for early embryonic development in Drosophila and in Caenorhabditis elegans. Arl1 is most similar in primary sequence, cellular location, and function (regulation of membrane traffic) to Arf1-6 and even shares several common binding partners. In addition to its function in membrane traffic at the Golgi/trans-Golgi network, there are reports indicating a possible role for Arl1 in ion homeostasis in yeast. ...
Expression of ARFGAP2 (FLJ14576, IRZ, Zfp289, ZNF289) in nasopharynx tissue. Antibody staining with HPA016649 and HPA018152 in immunohistochemistry.
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Frank S, Upender S, Hansen SH, Casanova JE (1998). "ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6 ... ADP-ribosylation factor 1 is a protein that in humans is encoded by the ARF1 gene. ADP-ribosylation factor 1 (ARF1) is a member ... 1991). "ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding ... "Entrez Gene: ARF1 ADP-ribosylation factor 1". Mitchell R, Robertson DN, Holland PJ, Collins D, Lutz EM, Johnson MS (September ...
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 ... Van Valkenburgh H, Shern JF, Sharer JD, Zhu X, Kahn RA (June 2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have ... Van Valkenburgh H, Shern JF, Sharer JD, Zhu X, Kahn RA (2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both ...
ADP-ribosylation factor-related protein 1 is a protein that in humans is encoded by the ARFRP1 gene. The protein encoded by ... "Entrez Gene: ARFRP1 ADP-ribosylation factor related protein 1". Schürmann A, Schmidt M, Asmus M, Bayer S, Fliegert F, Koling S ... It is related to the ADP-ribosylation factor (ARF) and ARF-like (ARL) genes. The gene is located in a gene cluster that ... 1999). "The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide ...
"Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA". FEBS Letters. 430 (3): 231-5. ... "Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA". FEBS Letters. 430 (3): 231-5. ... a pleckstrin homology domain containing guanine nucleotide exchange factor for Ral". The Journal of Biological Chemistry. 275 ( ... 4 (1): 73-8. doi:10.1038/ncb720. PMID 11744922. Clough RR, Sidhu RS, Bhullar RP (Aug 2002). "Calmodulin binds RalA and RalB and ...
ADP-ribosylation factor-like protein 6-interacting protein 1 is a protein that in humans is encoded by the ARL6IP1 gene. GRCh38 ... ARL6IP1 ADP-ribosylation factor-like 6 interacting protein 1". Human ARL6IP1 genome location and ARL6IP1 gene details page in ... "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 ...
Frank S, Upender S, Hansen SH, Casanova JE (1998). "ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6 ... Lee SY, Pohajdak B (2000). "N-terminal targeting of guanine nucleotide exchange factors (GEF) for ADP ribosylation factors (ARF ... Claing A, Chen W, Miller WE, Vitale N, Moss J, Premont RT, Lefkowitz RJ (2001). "beta-Arrestin-mediated ADP-ribosylation factor ... "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". J. Biol. Chem. 276 (45 ...
This protein is also a member of the ADP ribosylation factor family of guanine nucleotide-binding family of proteins. Its ... Vitale N, Horiba K, Ferrans VJ, Moss J, Vaughan M (Jul 1998). "Localization of ADP-ribosylation factor domain protein 1 (ARD1) ... Vitale N, Moss J, Vaughan M (Oct 1997). "Characterization of a GDP dissociation inhibitory region of ADP-ribosylation factor ... Vitale N, Moss J, Vaughan M (Jan 1998). "Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor ...
Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric ... ADP-ribosylation factor regulates hPLD2". J. Biol. Chem. 273 (21): 12846-52. doi:10.1074/jbc.273.21.12846. PMID 9582313. Kim JH ... "Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene ... "Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA". FEBS Lett. 430 (3): 231-5. doi: ...
Pacheco-Rodriguez G, Meacci E, Vitale N, Moss J, Vaughan M (1998). "Guanine nucleotide exchange on ADP-ribosylation factors ... "The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide exchange ... "The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide exchange ... Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1". Proc. Natl. Acad. Sci. U.S.A. 95 (14): 7909-14. doi ...
"Entrez Gene: ARFIP1 ADP-ribosylation factor interacting protein 1 (arfaptin 1)". Tsai SC, Adamik R, Hong JX, et al. (1998). " ... a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes". J Biol Chem. 272 (9): 5421-9 ... Arfaptin-1 is a protein that in humans is encoded by the ARFIP1 gene. ARFIP1 has been shown to interact with ARF3. GRCh38: ... 537 (1-3): 91-5. doi:10.1016/S0014-5793(03)00098-X. PMID 12606037. Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete ...
ADP-ribosylation factor 3 is a protein that in humans is encoded by the ARF3 gene. ADP-ribosylation factor 3 (ARF3) is a member ... "Entrez Gene: ARF3 ADP-ribosylation factor 3". Kanoh H, Williger BT, Exton JH (February 1997). "Arfaptin 1, a putative cytosolic ... Lee CM, Haun RS, Tsai SC, Moss J, Vaughan M (1992). "Characterization of the human gene encoding ADP-ribosylation factor 1, a ... Boman AL, Zhang Cj, Zhu X, Kahn RA (April 2000). "A family of ADP-ribosylation factor effectors that can alter membrane ...
1 (3): 287-92. doi:10.1093/embo-reports/kvd058. PMC 1083732 . PMID 11256614. Deloukas P, Matthews LH, Ashurst J, et al. (2002 ... 2000). "Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)". J. Biol. Chem ...
"Entrez Gene: ARFIP2 ADP-ribosylation factor interacting protein 2 (arfaptin 2)". D'Souza-Schorey, C; Boshans R L; McDonough M; ... Shin, O H; Exton J H (August 2001). "Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1". Biochem. ... Shin OH, Exton JH (2001). "Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1". Biochem. Biophys. Res ... a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes". J Biol Chem. 272 (9): 5421-9 ...
... binds to 2 molecules of ADP-ribosylation factor 1 (Arf1) as shown in this figure. A hinge region of exomer is thought to ...
ADP-ribosylation factor 5 is a protein that in humans is encoded by the ARF5 gene. ADP-ribosylation factor 5 (ARF5) is a member ... "Entrez Gene: ARF5 ADP-ribosylation factor 5". Kanoh, H; Williger B T; Exton J H (February 1997). "Arfaptin 1, a putative ... Shin OH, Couvillon AD, Exton JH (2001). "Arfophilin is a common target of both class II and class III ADP-ribosylation factors ... Shin, O H; Exton J H (August 2001). "Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1". Biochem. ...
2002). "Recruitment to Golgi membranes of ADP-ribosylation factor 1 is mediated by the cytoplasmic domain of p23". EMBO J. 20 ( ... 200 (1-2): 149-56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. Gommel D, Orci L, Emig EM, et al. (1999). "p24 and p23, the ... 138 (1-2): 171-4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). " ... 1 (1): 139-53. doi:10.1016/S1534-5807(01)00004-1. PMID 11703931. Gommel DU, Memon AR, Heiss A, et al. ( ...
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 ...
Van Valkenburgh H, Shern JF, Sharer JD, Zhu X, Kahn RA (Jun 2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have ... 2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1- ... 534 (1-3): 26-32. doi:10.1016/S0014-5793(02)03766-3. PMID 12527357. Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, ... 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039. Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and ...
Van Valkenburgh, H; Shern J F; Sharer J D; Zhu X; Kahn R A (June 2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) ... 2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1- ... 36 (1): 40-45. doi:10.1038/ng1285. PMID 14702039. Anderson NL, Polanski M, Pieper R, et al. (2004). "The human plasma proteome ... 6 (1): 37-44. doi:10.1093/dnares/6.1.37. PMID 10231028. Eichmuller S, Usener D, Dummer R, et al. (2001). "Serological detection ...
Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1)". J. Biol. Chem. ... Najpoznatiji članovi su Ras GTPaze, i iz tog razloga se ova familija enzima ponekad naziva Ras superfamilijom GTPaza.[1][2][3][ ...
ADP-ribosylation factor-like protein 3 is a protein that in humans is encoded by the ARL3 gene. ADP-ribosylation factor-like 3 ... Van Valkenburgh H, Shern JF, Sharer JD, Zhu X, Kahn RA (June 2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have ... Van Valkenburgh H, Shern JF, Sharer JD, Zhu X, Kahn RA (2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both ... Kim HS (March 1999). "Assignment of the human ADP-ribosylation factor-like 3 (ARL3) gene to chromosome 10 band q23.3 by ...
"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 ...
2005). "Exocytosis of CTLA-4 is dependent on phospholipase D and ADP ribosylation factor-1 and stimulated during activation of ... 2005). "Characterization of primate trypanosome lytic factors". Mol. Biochem. Parasitol. 138 (1): 9-20. doi:10.1016/j. ... 53 (1): 21-38. PMID 11939716. Jaworek J, Bonio J, Leja-Szpa A, et al. (2002). "Sensory nerves in central and peripheral control ... 325 (1-2): 59-70. doi:10.1016/S0009-8981(02)00248-6. PMID 12367767. Strausberg RL, Feingold EA, Grouse LH, et al. (2003). " ...
... 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. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, ...
... "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". J. Biol. Chem. 276 (45 ... "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- ... 1 (3): 227-33. doi:10.1038/79767. PMID 10973280. Shukla, A. K.; Westfield, G. H.; Xiao, K; Reis, R. I.; Huang, L. Y.; Tripathi- ...
ARL6IP1: encoding protein ADP-ribosylation factor-like protein 6-interacting protein 1 ... PMFBP1: encoding protein Polyamine-modulated factor 1-binding protein 1. *POLR3K: encoding enzyme DNA-directed RNA polymerase ... ISBN 978-1-136-84407-2.. *^ a b Genome Decoration Page, NCBI. Ideogram data for Homo sapience (850 bphs, Assembly GRCh38.p3). ... SHCBP1: encoding protein SHC SH2 domain-binding protein 1. *SLZ1: encoding protein SLX1 structure-specific endonuclease subunit ...
What is ADP-ribosylation factor-like tumour-suppressor protein 1? Meaning of ADP-ribosylation factor-like tumour-suppressor ... What does ADP-ribosylation factor-like tumour-suppressor protein 1 mean? ... ADP-ribosylation factor-like tumour-suppressor protein 1 explanation free. ... Looking for online definition of ADP-ribosylation factor-like tumour-suppressor protein 1 in the Medical Dictionary? ...
Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited) (Arfgef1), (10ug), 10 µg. ... Home » cDNA » Mouse cDNA » Arfgef1 (untagged) - Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A- ... Properties for Arfgef1 (untagged) - Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited) ( ... MC224976 Arfgef1 (untagged) - Mouse ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited) ( ...
ADP-ribosylation factor GTPase-activating protein 1 (ARFGAP1) Recombinant Protein-NP_001268411.1 (MBS1301288) product datasheet ... ADP-ribosylation factor GTPase-activating protein 1 isoform c NCBI Official Synonym Full Names ADP-ribosylation factor GTPase ... ADP-ribosylation factor GTPase-activating protein 1 (ARFGAP1), Recombinant Protein. Also Known As Recombinant Human ADP- ... ADP-ribosylation factor GTPase-activating protein 1 UniProt Synonym Protein Names ADP-ribosylation factor 1 GTPase-activating ...
Ver más] The small GTP-binding protein ADP-ribosylation factor 1 (ARF1) is an essential component of the molecular machinery ... The small GTP-binding protein ADP-ribosylation factor 1 (ARF1) is an essential component of the molecular machinery that ... Effect of protein kinase a activity on the association of ADP-ribosylation factor 1 to Golgi membranes. ...
Hara Y, Fukaya M, Hayashi K, Kawauchi T, Nakajima K, Sakagami H. ADP ribosylation factor 6 regulates neuronal migration in the ... Hara, Y., Fukaya, M., Hayashi, K., Kawauchi, T., Nakajima, K., & Sakagami, H. (2016). ADP ribosylation factor 6 regulates ... ADP ribosylation factor 6 (Arf6) is a critical small GTPase that regulates membrane trafficking between the plasma membrane and ... Hara, Y, Fukaya, M, Hayashi, K, Kawauchi, T, Nakajima, K & Sakagami, H 2016, ADP ribosylation factor 6 regulates neuronal ...
Among the small GTP-binding proteins, ARF1 (ADP-ribosylation factor 1) and SAR1 (Secretion-Associated RAS super family 1) are ... Coatomer and dimeric ADP ribosylation factor 1 promote distinct steps in membrane scission. J. Cell Biol 2011, 194, 765-777. [ ... Overexpression of ADP-ribosylation factor 1 in human gastric carcinoma and its clinicopathological. Cancer Sci 2012, 103, 1136- ... 2. ARF1 (ADP-Ribosylation Factor 1) and SAR1 (Secretion-Associated RAS Super Family 1) GTPases. Protein coats are classified ...
A role for ADP ribosylation factor in the control of cargo uptake during COPI-coated vesicle biogenesis. FEBS Lett. 462:267-272 ... The ADP-ribosylation factor GTPase-activating protein Glo3p is involved in ER retrieval. Eur. J. Cell Biol. 78:305-310. ... Myristoylation of ADP-ribosylation factor 1 facilitates nucleotide exchange at physiological Mg2+ levels. J. Biol. Chem. 270: ... Recruitment to Golgi membranes of ADP-ribosylation factor 1 is mediated by the cytoplasmic domain of p23. EMBO J. 20:6751-6760. ...
ADP-ribosylation factor-like 5C. Synonyms: Arl12. Gene nomenclature, locus information, and GO, OMIM, and PMID associations are ... Vega: OTTMUSG2915 (Arl5c, ADP-ribosylation factor-like 5C)*CCDS: 25334, 25334.1*Gene Ontology: Arl5c *Mouse Phenome DB: Arl5c * ... Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International + ... 1-530-752-KOMP, or for vectors [email protected] or +1-510-450-7917. ...
ADP-ribosylation factor-like) family of proteins, which are structurally related to ADP-ribosylation factors (ARFs). ARFs, ... ADP ribosylation factor like GTPase 1provided by HGNC. Primary source. HGNC:HGNC:692 See related. Ensembl:ENSG00000120805 MIM: ... ARL1 ADP ribosylation factor like GTPase 1 [Homo sapiens] ARL1 ADP ribosylation factor like GTPase 1 [Homo sapiens]. Gene ID: ... ARL1 ADP ribosylation factor like GTPase 1 [ Homo sapiens (human) ] Gene ID: 400, updated on 17-May-2020 ...
Q7KQL3 - Plasmodium falciparum 1 * Q3THZ2 - Mus musculus no matching PDB entries * P10947 - Homo sapiens no matching PDB ...
GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase ...
anti-ADP-Ribosylation Factor GTPase Activating Protein 2 Antibodies * anti-ADP-Ribosylation Factor GTPase Activating Protein 3 ... ADP-RIBOSYLATION FACTOR, ADP-ribosylation factor 1, ADP-RIBOSYLATION FACTOR 1A, arf1, arf2, arf3, ATARF, ATARF1, ATARFA1A, ... Vascular endothelial growth factor receptor-2 (show KDR Antibodies) activates ADP-ribosylation factor 1 to promote endothelial ... anti-ADP-Ribosylation Factor Guanine Nucleotide-Exchange Factor 1(brefeldin A-Inhibited) Antibodies ...
ADP-ribosylation factor guanine nucleotide-exchange factor 1 (brefeldin A-inhibited)Imported. ,p>Information which has been ... tr,I3K9S1,I3K9S1_ORENI ADP-ribosylation factor guanine nucleotide-exchange factor 1 (brefeldin A-inhibited) OS=Oreochromis ... ADP-ribosylation factor guanine nuc.... ADP-ribosylation factor guanine nucleotide-exchange factor 1 (brefeldin A-inhibited) ... 1.10.1000.11, 1 hit. InterProi. View protein in InterPro. IPR016024 ARM-type_fold. IPR032629 DCB_dom. IPR015403 Sec7_C. ...
GDP/GTP exchange modulates the interaction of the small G-protein ADP-ribosylation factor-1 with membrane lipids: if ARF(GDP) ... N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP ... from vesicles by factors of 7 and 100, respectively. This strongly suggests that, upon GDP/GTP exchange, the N-terminal helix ... Antonny B1, Beraud-Dufour S, Chardin P, Chabre M.. Author information. 1. CNRS, Institut de Pharmacologie Moleculaire et ...
ADP-ribosylation factor GTPase-activating protein 2 isoform 1Imported. ,p>Information which has been imported from another ... tr,F7A1C9,F7A1C9_CALJA ADP-ribosylation factor GTPase-activating protein 2 isoform 1 OS=Callithrix jacchus OX=9483 GN=ARFGAP2 ... ADP-ribosylation factor GTPase-activating protein 3. ). HUMAN. 516. UniRef50_Q9NP61. ADP-ribosylation factor GTPase-activating ... 3.30.40.160, 1 hit. InterProi. View protein in InterPro. IPR037278 ARFGAP/RecO. IPR001164 ArfGAP_dom. IPR038508 ArfGAP_dom_sf ...
OMIM: ADP-RIBOSYLATION FACTOR 1; ARF1*Gene Ontology: Arf1 *Mouse Phenome DB: Arf1 *UCSC: Chr.11:59,211,412-59,228,267(-)*IMPC: ... ADP-ribosylation factor 1. Gene nomenclature, locus information, and GO, OMIM, and PMID associations are updated daily from MGI ... Vega: OTTMUSG6340 (Arf1, ADP-ribosylation factor 1)*CCDS: 24765, 24765.1* ... Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International + ...
What is ADP-ribosylation factor-like 2-like 1? Meaning of ADP-ribosylation factor-like 2-like 1 medical term. What does ADP- ... Looking for online definition of ADP-ribosylation factor-like 2-like 1 in the Medical Dictionary? ADP-ribosylation factor-like ... redirected from ADP-ribosylation factor-like 2-like 1) ARL13B. A gene on chromosome 3q11.1 that encodes a GTP-binding protein ... ADP-Ribosylation Factor 4-Like. *ADP-Ribosylation Factor 5. *ADP-ribosylation factor 5, OTTHUMP00000024864, OTTHUMP00000196795 ...
Top performende anti-Maus ADP-Ribosylation Factor 1 Antikörper für Immunofluorescence (Paraffin-embedded Sections) (IF (p)) ... Recommended ADP-Ribosylation Factor 1 Antibody (geliefert von: Anmelden zum Anzeigen ) Antigen ADP-Ribosylation Factor 1 (ARF1 ... anti-ADP-Ribosylation Factor 1 Antikörper * anti-Maus ADP-Ribosylation Factor 1 Antikörper für Immunofluorescence (Paraffin- ... anti-Maus ADP-Ribosylation Factor 1 Antikörper für Immunofluorescence (Paraffin-embedded Sections). ...
ADP-Ribosylation Factor 1 Antikörper für Immunofluorescence (Paraffin-embedded Sections) (IF (p)) vergleichen & kaufen. ... Recommended ADP-Ribosylation Factor 1 Antibody (geliefert von: Anmelden zum Anzeigen ) Antigen ADP-Ribosylation Factor 1 (ARF1 ... anti-ADP-Ribosylation Factor 1 Antikörper * anti-Ratte (Rattus) ADP-Ribosylation Factor 1 Antikörper für Immunofluorescence ( ... anti-Ratte (Rattus) ADP-Ribosylation Factor 1 Antikörper für Immunofluorescence (Paraffin-embedded Sections). ...
Recombinant Human ADP-ribosylation Factor 1, His-tagged. Download Datasheet See All ARF1 Products. Bring this labeled protein ... ARF1, also known as ADP-ribosylation factor 1, is a small guanine nucleotide-binding protein that enhances the enzymatic ... Can be stored at +4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated ...
What is ADP-ribosylation factor-like protein 1? Meaning of ADP-ribosylation factor-like protein 1 medical term. What does ADP- ... Looking for online definition of ADP-ribosylation factor-like protein 1 in the Medical Dictionary? ADP-ribosylation factor-like ... ADP-ribosylation) factor-like family of proteins, which are structurally similar to ADP-ribosylation factors (ARFs), which ... redirected from ADP-ribosylation factor-like protein 1) ARL1. A gene on chromosome 12q23.2 that encodes a GTP-binding protein ...
HCA RNA Cell Line for ADP-ribosylation factor-like protein 6-interacting protein 1. ... Compartment GO Terms for ADP-ribosylation factor-like protein 6-interacting protein 1. ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
ADP-ribosylation factor 1 (ARF1) is a member of the human ARF gene family. The family members encode small guanine nucleotide- ... ADP ribosylation factor 1. Enable Javascript to view the expand/collapse boxes.. Open All Close All ... Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. ... binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking ...
The GGA (Golgi-localized, -ear containing, ADP-ribosylation factor binding) family of adaptor proteins serve a similar role. ... A cargo/PACS-1/AP-1A complex is necessary to drive the appropriate transport of several cargo proteins within the regulated ... We review the functions of AP-1A, PACS-1 and GGAs in facilitating the retrieval of proteins from immature SGs and review ... AP-1A recruitment to membranes can be modulated by PACS-1 (Phosphofurin Acidic Cluster Sorting protein 1), a cytosolic protein ...
  • This page contains a compilation of Rel/NF-kappaB target genes that is derived from the survey paper Activators and target genes of Rel/NF-kappaB transcription factors (Pahl, Oncogene 1999), the Rel/NF-kappaB transcription factors website of TD Gilmore, and additional search with PubMed. (lifl.fr)
  • Expression of apoA-V is increased by interaction of the heterodimer PPARα (peroxisome proliferator-activator receptor)/RXR (retinoid X receptor) with a "Direct Repeat"1 (DR1) sequence in the apoA-V promoter. (ahajournals.org)
  • 3,4 In this issue of Arteriosclerosis, Thrombosis, and Vascular Biology , Genoux et al 5 show that the retinoid-related orphan receptors alpha (RORα) 1 and 4 are also involved in the regulation of the apoA-V gene by interaction with the DR1 binding site. (ahajournals.org)
  • Previous studies have demonstrated that deficiency or inactivation of PARP-1 cause a high degree of genomic stability, characterized by aneuploidy, increased sister chromatid exchange, chromosome gain or loss, and telomere shortening [ 2 , 11 ]. (hindawi.com)
  • The SORT1 gene resides on chromosome 1 at the band 1p13.3 and includes 23 exons. (wikipedia.org)
  • In neurons, ephrin-As can use the p75 nerve growth factor receptor as a signaling partner to activate the FYN Src family kinase. (nih.gov)
  • Phosphatidylinositol-4-phosphate 5-kinase type-1 alpha is an enzyme that in humans is encoded by the PIP5K1A gene. (wikipedia.org)
  • The combined effects result in rapid fluid loss from the intestine, up to 2 liters per hour, leading to severe dehydration and other factors associated with cholera, including a rice-water stool. (wikipedia.org)
  • Treatment of cultured rodent neural stem cells with cholera toxin induces changes in the localization of the transcription factor Hes3 and increases their numbers. (wikipedia.org)
  • In cells that expressed no or low levels of YFP-PH, HA transport to the apical membrane was unaffected ( Fig. 1 , cells without asterisks or outlines). (rupress.org)
  • Phosphatidic Acid Increases Epidermal Growth Factor Receptor Expression by Stabilizing mRNA Decay and by Inhibiting Lysosomal and Proteasomal Degradation of the Internalized Receptor. (nih.gov)
  • Prieurianin/endosidin 1 is an actin-stabilizing small molecule identified from a chemical genetic screen for circadian clock effectors in Arabidopsis thaliana. (semanticscholar.org)
  • Several years later, the enzymes responsible for this incorporation were identified and given the name poly (ADP-ribose) polymerase. (wikipedia.org)
  • For over a decade it was thought that PARP1 was the only poly-ADP-ribose polymerase in mammalian cells, therefore this enzyme has been the most studied. (wikipedia.org)
  • Poly [ADP-ribose] polymerase 4 is an enzyme that in humans is encoded by the PARP4 gene. (wikipedia.org)
  • Poly(ADP-ribose) polymerase-1 (PARP-1) is a nuclear enzyme that is found universally in all eukaryotes and is encoded by the PARP-1 gene. (wikipedia.org)
  • Poly [ADP-ribose] polymerase 1 (PARP-1) also known as NAD+ ADP-ribosyltransferase 1 or poly[ADP-ribose] synthase 1 is an enzyme that in humans is encoded by the PARP1 gene. (wikipedia.org)
  • While necrosis is caused by acute cell injury resulting in traumatic cell death and apoptosis is a highly controlled process signalled by apoptotic intracellular signals, parthanatos is caused by the accumulation of PAR and the nuclear translocation of apoptosis-inducing factor (AIF) from mitochondria. (wikipedia.org)
  • PAR causes translocation of apoptosis-inducing factor (AIF) from the mitochondria to the nucleus where it induces DNA fragmentation and ultimately cell death. (wikipedia.org)
  • ADP-ribosylation toxin is one of the effector molecules secreted by several pathogenic bacteria and translocated through the TTSS and delivered into the host cytoplasm, which leads to interruption of the NF-κB pathway, cytoskeletal damage, and apoptosis. (wikipedia.org)
  • PARP-1 mediates parthanatos when it is over-activated in response to extreme genomic stress and synthesizes PAR which causes nuclear translocation of AIF. (wikipedia.org)