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

A capped Tudor domain within a core subunit of the Sin3L/Rpd3L histone deacetylase complex binds to nucleic acid G-quadruplexes

Journal of Biological Chemistry(2022)10.1016/j.jbc.2021.101558Source: DataRank Database

A capped Tudor domain within a core subunit of the Sin3L/Rpd3L histone deacetylase complex binds to nucleic acid G-quadruplexes is a research paper published in Journal of Biological Chemistry (2022). On theSindex it has a DataRank of 0. It has been cited 7 times.

N/A

0DataRank · unranked

Scored on demand from live citation data

Open Access7 citations

Download PDF

Cite:

Linked data & code

gen uniprot pdb doi

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)Impact (FWCI 0.47)OA: goldTopics (43)IDs (PubMed, PMC, OpenAlex)Annotations (4)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 (7)

Joseph Hsieh ORCID,Maksim Giljen,Emily Justice,Nicolas Daffern ORCID,Yongbo Zhang ORCID

Live enrichment

PubMed:34979096 PMC:PMC8800102 OpenAlex:https://openalex.org/W4206768416

American Heart Association Inc

Grant: 16PRE27260041

American Heart Association Inc

Grant: 17GRNT33680167

National Institutes of Health

Grant: S10 OD012016

National Institutes of Health

Grant: 1S10OD012016-01

600 MHz NMR Instrument Upgrade at Northwestern University

Northwestern University

FWCI

0.47

Citation Percentile

0.6%

Citation Trend

2023

2024

2026

goldLicense: cc-by-nc-nd

journalhttp://www.jbc.org/article/S0021925821013685/pdf

publisherhttp://www.jbc.org/article/S0021925821013685/pdf

publisherhttps://api.elsevier.com/content/article/PII:S0021925821013685?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0021925821013685?httpAccept=text/plain

journalhttps://doi.org/10.1016/j.jbc.2021.101558

Fields of Study

Histone Deacetylase Inhibitors ResearchEpigenetics and DNA MethylationCancer Mechanisms and Therapy0301 basic medicine0303 health sciences03 medical and health sciences

MeSH Terms

Tudor DomainAmino Acid SequenceAnimalsHistone DeacetylasesMammalsProtein BindingTranscription FactorsG-QuadruplexesSin3 Histone Deacetylase and Corepressor Complex

Keywords

Nucleic acidHistone deacetylaseChemistryProtein subunitG-quadruplexBiochemistryHistoneDomain (mathematical analysis)Molecular biologyStereochemistryComputational biologyDNABiologyGeneSolution NmrTranscriptional CorepressorProtein-nucleic Acid InteractionsChromatin-modifying ComplexG-QuadruplexesMammalsSin3 Histone Deacetylase and Corepressor ComplexTudor DomainAnimalsAmino Acid SequenceHistone DeacetylasesResearch ArticleProtein BindingTranscription Factors

Sustainable Development Goals

SDG 0: Life in Land

A capped Tudor domain within a core subunit of the Sin3L/Rpd3L histone deacetylase complex binds to nucleic acid G-quadruplexes

FAIR Checklist

Authors (7)

Funding (5 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)