Results 221 to 230 of about 46,966 (257)

Assays of ADP-Ribosylation factor Function

2002
ADP-ribosylation factors (ARFs) comprise a family of 20-kDa GTPases first identified as the protein cofactor required for the ADP ribosylation of the G s α protein, catalyzed by the A 1 subunits of the bacterial toxins cholera toxin (CT) and Escherichia colt heat-labile toxin (UF).
Jun, Kuai, Richard A, Kahn
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Cellular ADP-ribosylation of Elongation Factor 2

Molecular and Cellular Biochemistry, 1994
A 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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Molecular Characterization of ADP-Ribosylation Factors

1993
Cholera 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 ...
J. Moss, M. Vaughan
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ADP-ribosylation factor (ARF)

1994
Abstract Cloned ARF cDNA predicts a protein with a glycine at this position. Each of the three human ARF cDNAs hARF11314 (accession number P10947), hARF315 (accession number P16587), and hARF4,3,15 (accession numbers P18085, P21371) encode proteins of 180 or 181 amino acids with predicted molecular masses of 21-22 kDa.
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ADP-ribosylation Factors Protein Activators of Cholera Toxin

1993
Publisher 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.
J, Moss, M, Vaughan
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ADP-Ribosylation Factor-1 Is Sensitive to N-Ethylmaleimide

Journal of Biochemistry, 1998
The 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
T, Yamaguchi, K, Nakayama, K, Hatsuzawa, K, Tani, M, Himeno, M, Tagaya   +5 more
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ADP-ribosylation factors (Arfs)

1999
Abstract AP180 is an abundant neurone-specific clathrin-associated phosphoprotein, which supports in vitro the assembly of clathrin triskelia into a homogeneous population of cage-like structures. This function appears to be regulated by inositol polyphosphates. Proteins related to AP180 are also expressed in non-neuronal cells.
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Archaebacterial elongation factor is ADP-ribosylated by diphtheria toxin

Nature, 1980
Archaebacteria 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
M, Kessel, F, Klink
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Insulin and epidermal growth factor stimulate poly ADP-ribosylation

Biochemical and Biophysical Research Communications, 1981
Abstract Treatment of contact-inhibited BALBc 3T3 fibroblasts with insulin or epidermal growth factor elicited a considerable increase in the capacity of poly (ADP-ribose) synthesis. Stimulation of the poly ADP-ribosylation was observed after long-term hormone treatment (18 hours) but not after short-term treatment (1 hour) and it appeared to ...
Shimizu, Y, Shimizu, N
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Tumor necrosis factor-mediated cytotoxicity involves ADP-ribosylation.

The Journal of Immunology, 1988
Abstract The mechanism of TNF-mediated cytotoxicity was studied in several cell lines, including L929 murine fibroblasts. TNF caused a time- and dose-dependent increase of ADP-ribosylation in L929 target cells parallel to cell death.
S, Agarwal, B E, Drysdale, H S, Shin
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