This review describes NOS inhibitors as agents that interact with nitric oxide synthases through multiple sites and mechanisms, with differing time-dependence and isoform selectivity. The discussion is framed around inhibition of NOS family members rather than a single named compound.
First-pass extracted concept
nitric oxide synthase inhibitors
Candidate: concept label1 source documents8 linked claims
Live refresh every 5sNext refresh in 5s
Extracted Explainers
What the tool is doing
What problem it solves
What it does not solve
Evidence Snippets
A wide range of NOS inhibitors have been discussed, interacting with the enzyme in diverse ways in terms of site and mechanism of inhibition, time-dependence and selectivity for individual isoforms, although there are many pitfalls and misunderstandings of these aspects.
Supporting Sources
Linked Claims
NOS inhibitors act through diverse sites and mechanisms and differ in time-dependence and isoform selectivity.
The biopterin cofactor is implicated in one-electron redox cycling and multiple allosteric effects on NOS activity.
The exact nature of the NOS reaction, its mechanism, and its products remained controversial at the time of the review.
NOS regulation occurs at multiple levels including gene transcription, covalent modification, and allosteric regulation of the enzyme itself.
Substantial advances over the preceding seven years improved understanding of nitric oxide synthase structure, function, and inhibition.
Crystal structures of the oxygenase domains of iNOS and eNOS provide a framework for interpreting binding of haem, biopterin, L-arginine, and inhibitors.
Nitric oxide synthase family structure is described at multiple levels from primary sequence to quaternary organization including dimerization and association with other proteins.
Highly selective inhibitors of iNOS versus eNOS and nNOS have been identified and some have potential for treating inflammatory and other conditions in which iNOS is implicated.