Evidence map›Paper›PMID 33527205›Full record

ArticleJournal of molecular modeling2021

Molecular dynamics study of in silico mutations in the auto-inhibitory loop of human endothelial nitric oxide synthase FMN sub-domain.

D Preethi, Sharmila Anishetty, P Gautam

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of molecular modeling, 2021. 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
–field-weighted citation impact, top 99% 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.

  1. The Ever-Expanding Influence of the Endothelial Nitric Oxide Synthase.Basic & clinical pharmacology & toxicology · 2025
    Review
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

3 authors at 1 institution in 1 country.

D PreethiCentre for Biotechnology, Anna University, Chennai, Tamil Nadu, 600 025, India.ORCID https://orcid.org/0000-0002-5246-6668
Sharmila AnishettyCentre for Biotechnology, Anna University, Chennai, Tamil Nadu, 600 025, India. s_anishetty@annauniv.edu.ORCID https://orcid.org/0000-0003-1311-2709
P GautamCentre for Biotechnology, Anna University, Chennai, Tamil Nadu, 600 025, India. pgautam@annauniv.edu.ORCID https://orcid.org/0000-0003-3140-3796
Anna University, Chennai · IN

Funding

Council of Scientific and Industrial Research, India 09/468(0505)/2017-EMR-I
6 · The paper itself

Abstract

Structural flexibility of the peptide linker connecting two domains is essential for the functioning of multi-domain complex. Nitric oxide synthase (NOS) isoforms contain the oxygenase and the reductase domains connected by calmodulin binding linker (CBL) region. Additionally, the endothelial NOS (eNOS) isoform contain an auto-inhibitory loop (AI) in the FMN reductase sub-domain which represses the inter-domain electron transfer process. Binding of Ca

Indexed as

Molecular Dynamics SimulationFlavin MononucleotideHumansMutant ProteinsMutationNitric Oxide Synthase Type IIIProtein DomainsProtein Structure, SecondarySaltsFlavin MononucleotideMutant ProteinsNitric Oxide Synthase Type IIISaltsCalmodulin binding linker regionEndothelial nitric oxide synthaseHomology ModellingMolecular dynamic simulationS615D and S633D

Identifiers

PMID33527205
OpenAlexW3127253919

What OpenQuestion holds

Textmetadata
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.