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

Identifying the minimal sets of distance restraints for FRET-assisted protein structural modeling.

PubMed(2024)10.1002/pro.5219Source: DataRank Database

Identifying the minimal sets of distance restraints for FRET-assisted protein structural modeling. is a research paper published in PubMed (2024). On theSindex it has a DataRank of 0.

N/A

0DataRank · unranked

Scored on demand from live citation data

Open Access0 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 (5 grants)OA: greenTopics (28)IDs (PubMed, PMC, OpenAlex)Annotations (1)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)

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)

Alex T. Grigas ORCID,Jacob Sumner ORCID,Edward Knab,Caitlin M. Davis ORCID,Corey S. O’Hern ORCID

Live enrichment

PubMed:39548730 PMC:PMC11568256 OpenAlex:https://openalex.org/W4396914184

National Institutes of Health

Grant: R35GM151146

National Institutes of Health

Grant: T32GM145452

National Institutes of Health

Grant: T15LM007056‐37

NLM NIH HHS

Grant: T15 LM007056

NIH HHS

Grant: T15LM007056-37

greenLicense: cc-by

repositoryhttps://arxiv.org/pdf/2405.07983

repositoryhttps://pmc.ncbi.nlm.nih.gov/articles/PMC11568256/

publisherhttps://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.5219

repositoryhttp://arxiv.org/abs/2405.07983

repositoryhttps://pubmed.ncbi.nlm.nih.gov/38800659

Fields of Study

Electron Spin Resonance StudiesPhotosynthetic Processes and MechanismsProtein Structure and DynamicsFluorescence Resonance Energy TransferMolecular Dynamics SimulationProteinsProtein Conformation

MeSH Terms

ProteinsFluorescence Resonance Energy TransferProtein ConformationMolecular Dynamics Simulation

Keywords

Förster resonance energy transferMolecular dynamicsBiophysicsBiological systemChemistryProtein structureNucleic acidAmino acidBiochemistryPhysicsComputational chemistryBiologyFluorescenceMolecular Dynamics SimulationsCellular CrowdingFret ExperimentsIn Vivo Protein Structure

Sustainable Development Goals

SDG 0: Affordable and clean energy

Identifying the minimal sets of distance restraints for FRET-assisted protein structural modeling.

FAIR Checklist

Authors (6)

Funding (5 grants)

Open Access

Topics

Annotations (Europe PMC)