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Deciphering mutational effects on inducible NO synthase conformational dynamics via quantitative cross-linking mass spectrometry and AlphaFold2 subsampling

Journal of Biological Chemistry(2025)10.1016/j.jbc.2025.110673Source: DataRank Database

Deciphering mutational effects on inducible NO synthase conformational dynamics via quantitative cross-linking mass spectrometry and AlphaFold2 subsampling is a research paper published in Journal of Biological Chemistry (2025). On theSindex it has a DataRank of 0. It has been cited 3 times.

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Open Access3 citations

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Enrichment:Funding (8 grants)Impact (FWCI 1.13)OA: goldTopics (40)IDs (PubMed, PMC, OpenAlex)Annotations (1)

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (5)

Haikun Zhang ORCID,Gabriel Monteiro da Silva ORCID,Yadav Prasad Gyawali,Changjian Feng ORCID,Ting Jiang ORCID

Live enrichment

PubMed:40889679 PMC:PMC12597282 OpenAlex:https://openalex.org/W4413854212

National Science Foundation Division of Molecular and Cellular Biosciences

Grant: 2041692

National Science Foundation

Grant: P30ES032755

National Science Foundation

Grant: S10OD032175

NIH National Institute of General Medical Sciences

Grant: P20GM130422

NIH National Institute of General Medical Sciences

Grant: GM156443

NIGMS NIH HHS

Grant: R35 GM156443

National Institutes of Health

NIEHS

FWCI

1.13

Citation Percentile

0.8%

Citation Trend

2025

2026

goldLicense: cc-by

journalhttps://www.jbc.org/article/S0021-9258(25)02525-6/pdf

publisherhttps://www.jbc.org/article/S0021-9258(25)02525-6/pdf

publisherhttps://api.elsevier.com/content/article/PII:S0021925825025256?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0021925825025256?httpAccept=text/plain

journalhttps://doi.org/10.1016/j.jbc.2025.110673

Fields of Study

Mass Spectrometry Techniques and ApplicationsNitric Oxide and Endothelin EffectsPhotosynthetic Processes and Mechanisms

MeSH Terms

AnimalsCalmodulinCross-Linking ReagentsFlavin MononucleotideHemeHumansMutationProtein ConformationMass SpectrometryMutation, MissenseNitric Oxide Synthase Type II

Keywords

Mass spectrometryChemistryATP synthaseDynamics (music)Computational biologyBiochemistryBiophysicsBiologyChromatographyEnzymePhysicsCalmodulinElectron transferHemeflavoproteinNitric Oxide SynthaseSubsamplingParallel Reaction MonitoringConformational EnsembleMultidomain ProteinConformationsCrosslinking Mass SpectrometryTimstofAlphafold2Quantitative Crosslinking Mass SpectrometryFunctional Protein Dynamics

Deciphering mutational effects on inducible NO synthase conformational dynamics via quantitative cross-linking mass spectrometry and AlphaFold2 subsampling

FAIR Checklist

Authors (5)

Funding (8 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)