S
S J Stanley
Researcher at National Institutes of Health
Publications - 24
Citations - 1266
S J Stanley is an academic researcher from National Institutes of Health. The author has contributed to research in topics: NAD+ kinase & Arginine. The author has an hindex of 18, co-authored 24 publications receiving 1237 citations.
Papers
More filters
Journal ArticleDOI
Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes.
TL;DR: An NAD- and guanidine-dependent ADP-ribosyltransferase has been purified more than 500,000-fold from turkey erythrocytes with an 18% yield and the specific activity of the purified enzyme is comparable to that reported for purified NAD glycohydrolases and poly(ADP- ribosyl)transferases.
Journal ArticleDOI
Activation by thiol of the latent NAD glycohydrolase and ADP-ribosyltransferase activities of Bordetella pertussis toxin (islet-activating protein).
TL;DR: In contrast to the bacterial toxins choleragen and Escherichia coli heat-labile enterotoxin that ADP-ribosylate stimulatory components of the cyclase system, pertussis toxin did not transfer ADp-ribose to low molecular weight guanidino compounds, such as arginine or agmatine.
Book ChapterDOI
Molecular and immunological characterization of ADP-ribosylarginine hydrolases.
Joel Moss,S J Stanley,Maria S. Nightingale,James J. Murtagh,Lucia Monaco,Kazuo Mishima,Hao-Chia Chen,Kim C. Williamson,Su-Chen Tsai +8 more
TL;DR: Hydrolase activities were present in a variety of animal species, with the highest specific activities found in rat and mouse brain, spleen, and testis.
Journal ArticleDOI
Amino acid-specific ADP-ribosylation.
Joel Moss,D A Yost,S J Stanley +2 more
TL;DR: The presence of ADP-ribose-arginine and ADP -ribosyltransferase and poly(ADP- ribose) synthetase, respectively, may be the chemical basis for the "hydroxylamine-stable" and "Hydroxylamin-labile" bonds described by Hilz.
Journal ArticleDOI
Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme
TL;DR: ADP-ribosylation may be a reversible modification of proteins that is dependent on NAD and the NAD:arginine ADP- ribosyltransferase.