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Dynamics of integrin α5β1, fibronectin, and their complex reveal sites of interaction and conformational change

Journal of Biological Chemistry(2022)10.1016/j.jbc.2022.102323Source: DataRank Database

Dynamics of integrin α5β1, fibronectin, and their complex reveal sites of interaction and conformational change is a research paper published in Journal of Biological Chemistry (2022). On theSindex it has a DataRank of 0.515. It has been cited 30 times.

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0.515DataRank · unranked

Scored on demand from live citation data

Open Access30 citations

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (4 grants)Impact (FWCI 3.00)OA: goldTopics (50)IDs (PubMed, PMC, OpenAlex)Annotations (2)SDGs (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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DataRank Breakdown

Base Score 100%Citation Network 0%

Base Score Contribution

0.515

From this paper's citation signal

Citation Network Contribution

Citation network not refreshed for this result

This paper's DataRank is currently driven only by its base citation score. Citation network data was not refreshed for this result.

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Authors (5)

Roxana E. Iacob ORCID,Jing Li ORCID,John R. Engen ORCID,Timothy A. Springer ORCID,Yang Su ORCID

Live enrichment

PubMed:35931112 PMC:PMC9483561 OpenAlex:https://openalex.org/W4289444060

NHLBI

Grant: R01-HL-131729

NHLBI NIH HHS

Grant: R01 HL131729

National Institutes of Health

Grant: 5R01HL131729-02

Structures and Conformational Equilibria of Integrin alpha5 beta1

National Institutes of Health

FWCI

3.00

Citation Percentile

0.9%

Citation Trend

2023

2024

2025

2026

goldLicense: cc-by-nc-nd

journalhttps://doi.org/10.1016/j.jbc.2022.102323

publisherhttps://doi.org/10.1016/j.jbc.2022.102323

publisherhttps://api.elsevier.com/content/article/PII:S0021925822007657?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0021925822007657?httpAccept=text/plain

repositoryhttps://pubmed.ncbi.nlm.nih.gov/35931112

Fields of Study

Cell Adhesion Molecules ResearchMonoclonal and Polyclonal Antibodies ResearchRNA Research and Splicing0301 basic medicine0303 health sciences03 medical and health sciences

MeSH Terms

Binding SitesCell AdhesionFibronectinsMutationOligopeptidesSolventsIntegrin alpha5beta1Deuterium Exchange MeasurementProtein Interaction Domains and Motifs

Keywords

FibronectinChemistryEctodomainIntegrinBinding siteBiophysicsHydrogen–deuterium exchangeFörster resonance energy transferConformational changePlasma protein bindingBinding domainProtein subunitStereochemistryExtracellular matrixBiochemistryCellBiologyReceptorMass spectrometryFluorescenceThermal stabilityAffinityLigand bindingHydrogen-deuterium Exchange Mass SpectrometryProtein–protein InteractionsBinding SitesMutationCell AdhesionSolventsDeuterium Exchange MeasurementProtein Interaction Domains and MotifsOligopeptidesResearch ArticleFibronectinsIntegrin alpha5beta1

Sustainable Development Goals

SDG 0: Affordable and clean energy

Dynamics of integrin α5β1, fibronectin, and their complex reveal sites of interaction and conformational change

FAIR Checklist

DataRank Breakdown

Authors (5)

Funding (4 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)