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Cited by 283

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase.

Open access
Zhang, J, Snyder, S H·1992·Proceedings of the National Academy of Sciences

Abstract

Nitric oxide generation in brain cytosolic fractions markedly enhances ADP-ribosylation of a single 37-kDa protein. By utilizing a biotinylated NAD and avidin affinity chromatography, we purified this protein. Partial amino acid sequencing establishes its identity as glyceraldehyde-3-phosphate dehydrogenase (GAPDH). This is further confirmed by detection of GAPDH enzymatic activity in the purified 37-kDa protein. GAPDH is ADP-ribosylated in the absence of brain extract. This auto-ADP-ribosylation is enhanced by nitric oxide generation. ADP-ribosylation appears to involve the cysteine where NAD interacts with GAPDH so that ADP-ribosylation likely inhibits enzymatic activity. Such inhibition may play a role in nitric oxide-mediated neurotoxicity.

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Metadata

Authors
Zhang, J., & Snyder, S. H.
Venue
Proceedings of the National Academy of Sciences
Published
1992-10-15
Volume
89
Issue
20
Pages
9382-9385
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2082724267
Cited by
283
References
2
FWCI
13.41
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase. https://app.cochat.ai/papers/10.1073/pnas.89.20.9382
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Zhang, J., & Snyder, S. H. (1992). Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.89.20.9382

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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