The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
STRUCTURE-FUNCTION ASPECTS IN THE NITRIC OXIDE SYNTHASES
Abstract
▪ Abstract Research on the biological roles of nitric oxide has revealed that it functions as an important signal and effector molecule in a variety of physiologic and pathologic settings. In animals, nitric oxide is synthesized enzymatically from l-arginine through the actions of the nitric oxide synthases (NOSs). The three known NOS isoforms are all dimeric, bi-domain enzymes that contain iron protoporphyrin IX, flavin adenine dinucleotide, flavin mononucleotide, and tetrahydrobiopterin as bound prosthetic groups. This chapter summarizes information regarding the structure-function aspects of the NOSs, which includes composition of the domains, the protein residues and regions involved in prosthetic group binding, catalytic properties of the domains, the relationship between dimeric structure and prosthetic group binding and function, and factors that control assembly of NOS in cells. A general model for NOS structure and assembly is presented.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Baek, K. J., Thiel, B. A., Lucas, S., & Stuehr, D. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36901-7 · Cited by 389
Self-citationHydrogen Peroxide-Supported Oxidation of NG-Hydroxy-L-Arginine by Nitric Oxide Synthase
Pufahl, R. A., Wishnok, J. S., & Marletta, M. A. (1995) · Biochemistry · doi:10.1021/bi00006a014 · Cited by 168 · cited 1×
“However, it can convert the reaction intermediate N -hydroxy-L-arginine (L-NOHA) to NO and citrulline in the presence of H 2O2 (N Sennequier & DJ Stuehr, unpublished observations), consistent with H2O2 also supportingL-NOHA oxidation by the full-length iNOS dimer in the presence of H4biopterin (69).”
Background
Cited by
Arginine metabolism: nitric oxide and beyond
WU, G., & MORRIS, S. M. (1998) · Biochemical Journal · doi:10.1042/bj3360001 · Cited by 2,811
Landmesser, U., Dikalov, S., Price, S. R., McCann, L., Fukai, T., Holland, S. M., Mitch, W. E., & Harrison, D. G. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200314172 · Cited by 1,660
Cuzzocrea, S., Riley, D. P., Caputi, A. P., & Salvemini, D. (2001) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01484-4 · Cited by 1,087
Mammalian nitric oxide synthases
Stuehr, D. J. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00016-x · Cited by 996
Self-citationThe chemical biology of nitric oxide: Implications in cellular signaling
Thomas, D. D., Ridnour, L. A., Isenberg, J. S., Flores-Santana, W., Switzer, C. H., Donzelli, S., Hussain, P., Vecoli, C., Paolocci, N., Ambs, S., et al. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.020 · Cited by 975
Metadata
- Authors
- Stuehr, D. J.
- Venue
- Annual Review of Pharmacology and Toxicology
- Publisher
- Annual Reviews
- Published
- 1997-04
- Volume
- 37
- Issue
- 1
- Pages
- 339-359
- ISSN
- 0362-1642 (ISSN-L)
- 1545-4304
- OpenAlex
- W2114000416
- Cited by
- 539
- References
- 2
- FWCI
- 3.25
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: STRUCTURE-FUNCTION ASPECTS IN THE NITRIC OXIDE SYNTHASES. https://app.cochat.ai/papers/10.1146/annurev.pharmtox.37.1.339
- The paper
- Stuehr, D. J. (1997). STRUCTURE-FUNCTION ASPECTS IN THE NITRIC OXIDE SYNTHASES. Annual Review of Pharmacology and Toxicology. https://doi.org/10.1146/annurev.pharmtox.37.1.339
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
