Autoregulation and Autoinhibition of the Main NO Synthase Isoforms (Brief Review).

N A Popova, S K Soodaeva, I A Klimanov, V M Misharin, A A Temnov

Open access · diamondAbstract readReview

In one paragraph

Review in Sovremennye tekhnologii v meditsine, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

0.2field-weighted citation impact, top 48% of its field

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 1 citations in OpenAlex.

Structure and dynamics of a multidomain nitric oxide synthase regulated by a C2 domain.Science advances · 2026
Article

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

N A PopovaResearcher, Laboratory of Clinical and Experimental Biophysics; Pulmonology Research Institute, Federal Medical and Biological Agency of Russia, 28 Orekhovy Boulevard, Moscow, 115682, Russia; Researcher, Laboratory of Chemical and Biotechnological Synthesis; Moscow Institute of Physics and Technology (National Research University), 9 Institutskiy Per., Dolgoprudny, Moscow Region, 141701, Russia.

S K SoodaevaHead of Laboratory of Clinical and Experimental Biophysics; Pulmonology Research Institute, Federal Medical and Biological Agency of Russia, 28 Orekhovy Boulevard, Moscow, 115682, Russia; Leading Researcher, Laboratory of Chemical and Biotechnological Synthesis; Moscow Institute of Physics and Technology (National Research University), 9 Institutskiy Per., Dolgoprudny, Moscow Region, 141701, Russia.

I A KlimanovSenior Researcher, Laboratory of Clinical and Experimental Biophysics; Pulmonology Research Institute, Federal Medical and Biological Agency of Russia, 28 Orekhovy Boulevard, Moscow, 115682, Russia.

V M MisharinActing Director of the Institute; Pulmonology Research Institute, Federal Medical and Biological Agency of Russia, 28 Orekhovy Boulevard, Moscow, 115682, Russia.

A A TemnovHead of Laboratory of Chemical and Biotechnological Synthesis; Moscow Institute of Physics and Technology (National Research University), 9 Institutskiy Per., Dolgoprudny, Moscow Region, 141701, Russia.

Chemical Synthesis Lab · SGFederal Medical-Biological Agency · RUMoscow Power Engineering Institute · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nitric oxide (II) (NO) is the most important mediator of a wide range of physiological and pathophysiological processes. It is synthesized by NO synthases (NOSs), which have three main isoforms differing from each other in terms of activation and inhibition features, levels of NO production, subcellular localization, etc. At the same time, all isoforms are structurally very similar, and these differences are determined by NOS autoregulatory elements. The article presents an analysis of the autoregulatory and autoinhibitory mechanisms of the NOS reductase domain that determine differences in the productivity of isoforms, as well as their dependence on the concentration of Ca

Indexed as

CalmodulinNitric Oxide SynthaseElectron TransportFlavinsHomeostasisIonsCalmodulinFlavinsIonsNitric Oxide Synthaseautoinhibitory insertcalmodulinC-tailelectron transfer to NOSnitric oxideNOS autoregulationNOS modelingNO synthase

Identifiers

PMID38435476

DOI10.17691/stm2023.15.3.06

PMCPMC10904358

OpenAlexW4382723075

What OpenQuestion holds

Textmetadata

LicenceCC BY

Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.