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A role for ADP-ribosylation factor in nuclear vesicle dynamics
Nature, 1992Two distinct steps in nuclear envelope assembly can be assayed in vitro: the protein-mediated binding of nuclear-specific vesicles to chromatin, and the subsequent fusion of these vesicles to enclose the chromatin within a double nuclear membrane. Nuclear vesicle fusion, like fusion in the secretory pathway, requires ATP and cytosol and is inhibited by
Paul Melançon +5 more
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The Biology of ADP-Ribosylation Factors [PDF]
, 1993 Adenosine diphosphate (ADP) ribosylation factor (ARF) was originally defined as an activity required for the efficient activation of the purified, stimulatory, regulatory component of adenylyl cyclase, Gs, by cholera toxin (Schleifer et al. 1982; Kahn 1989, 1991).
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ADP-Ribosylation Factor-1 Is Sensitive to N-Ethylmaleimide
Journal of Biochemistry, 1998The treatment of normal rat kidney cells with N-ethylmaleimide caused the release of beta-COP, a component of coatomer, from the Golgi apparatus without causing disassembly of the organelle. The release of beta-COP, which was not due to depolymerization of microtubules, was markedly blocked by the activation of GTP-binding proteins by aluminum fluoride
Katsuko Tani +5 more
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Cellular ADP-ribosylation of Elongation Factor 2
Molecular and Cellular Biochemistry, 1994A cellular ADP-ribosyltransferase activity has been found in a variety of animals and tissues. The enzyme transfers ADP-ribose from NAD to elongation factor 2, inactivating the factor and thus inhibiting in vitro protein synthesis. Although, the mechanism of action of the cellular enzyme appears similar to diphtheria toxin and Pseudomonas exotoxin A ...
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Archaebacterial elongation factor is ADP-ribosylated by diphtheria toxin
Nature, 1980Archaebacteria have been defined as a 'third primary kingdom' of cells in addition to the urkaryotes and the eubacteria. While the latter two correspond approximately to the conventional categories eukaryotes and prokaryotes respectively, the Archaebacteria have up to now comprised four groups of microorganisms: the methanogenic bacteria, the extremely
Friedrich Klink, Michael Kessel
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[33] Stimulation of phospholipase D by ADP-ribosylation factor
1995Publisher Summary Phospholipase D (PLD) activity hydrolyzes membrane phospholipids into phosphatidic acid and their respective polar headgroups. For example, phosphatidylcholine (PC) would yield phosphatidic acid (PA) and choline. While the production of choline is presumably not important to direct signaling, increases in PA can have profound ...
Paul C. Sternweis, H. A. Brown
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Biochemistry, 2002
We have used a site-specific photo-cross-linking approach to identify direct interactions between clathrin adaptor protein (AP)1 complexes and small GTPases of the ADP-ribosylation factor (ARF) family and to explore the specificity of this interaction on
Carol Austin, M. Boehm, S. Tooze
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We have used a site-specific photo-cross-linking approach to identify direct interactions between clathrin adaptor protein (AP)1 complexes and small GTPases of the ADP-ribosylation factor (ARF) family and to explore the specificity of this interaction on
Carol Austin, M. Boehm, S. Tooze
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Molecular Characterization of ADP-Ribosylation Factors
1993Cholera toxin (CT) is largely responsible for the pathogenesis of cholera, a devastating diarrheal disease characterized by marked abnormalities in fluid and electrolyte flux (Carpenter 1980; Finkelstein 1973; Kelly 1986). The toxin, a product of Vibrio cholerae, is an oligomeric protein composed of one A subunit (CTA) of about 29kDa and five B ...
M. Vaughan, J. Moss
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Journal of Biochemistry (Tokyo), 1996
ADP-ribosylation factors (ARFs) are a family of small GTP-binding proteins that are proposed to be involved in the formation of coated transport vesicles.
Masahiro Hosaka +5 more
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ADP-ribosylation factors (ARFs) are a family of small GTP-binding proteins that are proposed to be involved in the formation of coated transport vesicles.
Masahiro Hosaka +5 more
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ADP-ribosylation Factors Protein Activators of Cholera Toxin
1993Publisher Summary The toxins alter the activity of the guanine nucleotide-binding proteins (G proteins) by catalyzing the transfer of the ADP-ribose moiety of NAD to a critical amino acid in the a subunit. This ADP-ribosylation reaction results in either activation (e.g., cholera toxin, E.
Joel Moss, Martha Vaughan
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