🏆 Finalist — NIH Data Sharing Index (“S-Index”) Challenge

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

Phosphorylation of a Cleaved Tau Proteoform at a Single Residue Inhibits Binding to the E3 Ubiquitin Ligase, CHIP

bioRxiv (Cold Spring Harbor Laboratory)(2023)10.1101/2023.08.16.553575Source: DataRank Database

Phosphorylation of a Cleaved Tau Proteoform at a Single Residue Inhibits Binding to the E3 Ubiquitin Ligase, CHIP is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2023). On theSindex it has a DataRank of 0. It has been cited 1 time.

N/A

0DataRank · unranked

Scored on demand from live citation data

Open Access1 citations

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 (2 grants)OA: greenTopics (15)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 (10)

Kristin Wucherer ORCID,Abby Oehler,Aye C. Thwin ORCID,Koli Basu,Matthew Callahan ORCID

Live enrichment

PubMed:37645969 OpenAlex:https://openalex.org/W4385952960

National Institutes of Health

Grant: 5P01AG019724-03

FRONTOTEMPORAL DEMENTIA: GENES, IMAGES, AND EMOTIONS

National Institutes of Health

Grant: 5P50AG023501-03

DATA MANAGEMENT AND BIOSTATISTICS

greenLicense: cc-by-nc-nd

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2023/08/16/2023.08.16.553575.full.pdf

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2023/08/16/2023.08.16.553575.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2023.08.16.553575

repositoryhttps://doi.org/10.1101/2023.08.16.553575

repositoryhttps://pubmed.ncbi.nlm.nih.gov/37645969

Fields of Study

Microtubule and mitosis dynamicsUbiquitin and proteasome pathways0301 basic medicine03 medical and health sciences

Keywords

Ubiquitin ligasePhosphorylationDNA ligaseUbiquitinChemistryCell biologyBiochemistryBiologyEnzymeGeneArticle