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

Cryo-EM structures of the D290V mutant of the hnRNPA2 low-complexity domain suggests how D290V affects phase separation and aggregation

Journal of Biological Chemistry(2023)10.1016/j.jbc.2023.105531Source: DataRank Database

Cryo-EM structures of the D290V mutant of the hnRNPA2 low-complexity domain suggests how D290V affects phase separation and aggregation is a research paper published in Journal of Biological Chemistry (2023). On theSindex it has a DataRank of 0. It has been cited 5 times.

N/A

0DataRank · unranked

Scored on demand from live citation data

Open Access5 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 (7 grants)OA: goldTopics (23)IDs (PubMed, PMC)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 (10)

P. Ge ORCID,M.R. Sawaya ORCID,Michael P. Hughes ORCID,David R. Boyer ORCID,Qin Cao ORCID

Live enrichment

PubMed:38072051 PMC:PMC10844680

National Science Foundation

Grant: MCB 1616265

National Institutes of Health

Grant: 1R01AG070895

National Institutes of Health

Grant: 1RF1AG065407

National Institutes of Health

Grant: R01 AG048120

U.S. Department of Energy

Grant: DE-FC02-02ER63421

NIA NIH HHS

Grant: RF1 AG065407

NIA NIH HHS

Grant: R01 AG070895

goldLicense: cc-by-nc-nd

publisherhttp://www.jbc.org/article/S0021925823025590/pdf

publisherhttps://api.elsevier.com/content/article/PII:S0021925823025590?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0021925823025590?httpAccept=text/plain

repositoryhttps://escholarship.org/content/qt4cz3d712/qt4cz3d712.pdf?t=s93etb

repositoryhttps://pmc.ncbi.nlm.nih.gov/articles/PMC10844680/pdf/main.pdf

MeSH Terms

HumansHeterogeneous-Nuclear Ribonucleoprotein Group A-BCryoelectron MicroscopyProtein Structure, TertiaryMutationHydrogen-Ion ConcentrationModels, MolecularProtein StabilityProtein DomainsPhase Separation

Keywords

AmyloidPhase separationAlzheimer's diseaseNuclear localization signalPolymorphProtein aggregationCryoemCondensateMultisystem ProteinopathyLow Complexity DomainMembraneless OrganelleLarksRibonucleoprotein A2

Cryo-EM structures of the D290V mutant of the hnRNPA2 low-complexity domain suggests how D290V affects phase separation and aggregation

FAIR Checklist

Authors (10)

Funding (7 grants)

Open Access

Topics

Annotations (Europe PMC)