Pilot corpus: NIH-funded biomedical datasets. Any DOI can be scored on demand — network effects sharpen as coverage grows.

Protein unfolded states populated at high and ambient pressure are similarly compact

Biophysical Journal(2021)10.1016/j.bpj.2021.04.031Source: DataRank Database

Protein unfolded states populated at high and ambient pressure are similarly compact is a research paper published in Biophysical Journal (2021). On theSindex it has a DataRank of 0. It has been cited 20 times.

N/A

0DataRank · unranked

Scored on demand from live citation data

Open Access20 citations

Free full text

Cite:

DataRank reads this dataset's downstream impact straight off the citation graph — no black box, no proprietary weighting. How is this computed?

›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (6 grants)Impact (FWCI 1.11)OA: bronzeTopics (30)IDs (PubMed, OpenAlex)

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

FAIR checklist signals are shown for context only and do not affect DataRank scoring.

Run a calibrated FAIR evaluation for this paper →

We only score data papers we can read in full — never from an abstract alone.

Authors (6)

Richard E. Gillilan ORCID,Junjie Zou ORCID,Jinqiu Wang ORCID,Daniel P. Raleigh ORCID,Catherine A. Royer ORCID

Live enrichment

PubMed:33961866 OpenAlex:https://openalex.org/W3159279090

National Institutes of Health

Grant: 1-P30-GM124166-01A1

National Institutes of Health

Grant: GM 078114

National Science Foundation Division of Molecular and Cellular Biosciences

Grant: DMR-1829070

National Science Foundation Division of Molecular and Cellular Biosciences

Grant: MCB 1514575

NIGMS NIH HHS

Grant: P30 GM124166

NIGMS NIH HHS

Grant: R01 GM078114

FWCI

1.11

Citation Percentile

0.8%

Citation Trend

2022

2023

2024

2025

2026

bronzeLicense: http://www.elsevier.com/open-access/userlicense/1.0/

journalhttp://www.cell.com/article/S0006349521003702/pdf

publisherhttp://www.cell.com/article/S0006349521003702/pdf

publisherhttps://api.elsevier.com/content/article/PII:S0006349521003702?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0006349521003702?httpAccept=text/plain

journalhttps://doi.org/10.1016/j.bpj.2021.04.031

Fields of Study

Protein Structure and DynamicsEnzyme Structure and FunctionMaterial Dynamics and PropertiesCold TemperatureProtein ConformationProtein DenaturationProtein FoldingRibosomal ProteinsTemperature

MeSH Terms

Cold TemperatureProtein ConformationProtein DenaturationRibosomal ProteinsTemperatureProtein Folding

Keywords

Radius of gyrationAmbient pressureChemistryAtmospheric pressureHydrodynamic radiusThermodynamicsDenaturation (fissile materials)Protein foldingUnfolded protein responseGyrationChemical physicsCrystallographyPhysicsPolymerOrganic chemistry