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

Hydrophobicity in Intrinsically Disordered Protein Force Fields: Implications for Conformational Ensembles and Protein–Protein Interactions

The Journal of Physical Chemistry B(2025)10.1021/acs.jpcb.5c02360Source: DataRank Database

Hydrophobicity in Intrinsically Disordered Protein Force Fields: Implications for Conformational Ensembles and Protein–Protein Interactions is a research paper published in The Journal of Physical Chemistry B (2025). On theSindex it has a DataRank of 0. It has been cited 13 times.

N/A

0DataRank · unranked

Scored on demand from live citation data

Open Access13 citations

Download PDF

Cite:

Linked data & code

pdb

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 (11 grants)Impact (FWCI 5.00)OA: hybridTopics (23)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)

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 (4)

Saeed Najafi ORCID,M. Scott Shell ORCID,Joan‐Emma Shea ORCID,Samuel Lobo ORCID

Live enrichment

PubMed:40569578 PMC:PMC12257530 OpenAlex:https://openalex.org/W4411673450

National Institutes of Health

Grant: 5R01AG056058-09

Drivers of Pathological Tau Aggregation

National Institutes of Health

Grant: R01-GM118560-01A

National Science Foundation

Grant: ACI-1548562

National Science Foundation

Grant: CHEM-1800344

National Science Foundation

Grant: CNS-1725797

National Science Foundation

Grant: DMR-2308708

National Science Foundation

Grant: MCB-1716956

National Science Foundation

Grant: PHY 2423885

NIA NIH HHS

Grant: R01 AG056058

NIGMS NIH HHS

Grant: R01 GM118560

W. M. Keck Foundation

FWCI

5.00

Citation Percentile

1.0%

Citation Trend

2024

2025

2026

hybridLicense: cc-by-nc-nd

journalhttps://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.5c02360?ref=article_openPDF

publisherhttps://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.5c02360?ref=article_openPDF

publisherhttps://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.5c02360

journalhttps://doi.org/10.1021/acs.jpcb.5c02360

repositoryhttps://pubmed.ncbi.nlm.nih.gov/40569578

Fields of Study

Protein Structure and DynamicsEnzyme Structure and FunctionHemoglobin structure and function0301 basic medicine03 medical and health sciences

MeSH Terms

Protein ConformationThermodynamicsWaterMolecular Dynamics SimulationHydrophobic and Hydrophilic InteractionsIntrinsically Disordered Proteins

Keywords

Intrinsically disordered proteinsChemical physicsChemistryBiophysicsBiologyBiochemistryProtein ConformationWaterThermodynamicsMolecular Dynamics SimulationHydrophobic and Hydrophilic InteractionsArticle

Hydrophobicity in Intrinsically Disordered Protein Force Fields: Implications for Conformational Ensembles and Protein–Protein Interactions

FAIR Checklist

Authors (4)

Funding (11 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)