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Regulation of the Dot1 histone H3K79 methyltransferase by histone H4K16 acetylation

Science(2021)10.1126/science.abc6663Source: DataRank Database

Regulation of the Dot1 histone H3K79 methyltransferase by histone H4K16 acetylation is a research paper published in Science (2021). On theSindex it has a DataRank of 3.0. It has been cited 115 times, with 105 citing works in its 1-hop citation network.

N/A

3.0DataRank · unranked

Scored on demand from live citation data

115 citations · 105 citing works in its network

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Linked data & code

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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 (6 grants)Impact (FWCI 7.38)OA: greenTopics (52)IDs (PubMed, PMC, OpenAlex)Annotations (2)SDGs (2)

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (0/2)

Interoperable (0/2)

Reusable (0/3)

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DataRank Breakdown

Base Score 24%Citation Network 76%

Base Score Contribution

0.713

From this paper's citation signal

Citation Network Contribution

2.3

From 85 citing papers with measurable signal

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Authors (8)

Pablo De Ioannes ORCID,Miao Wang ORCID,David M. Truong ORCID,Rachel Lee ORCID,Jean‐Paul Armache ORCID

Live enrichment

PubMed:33479126 PMC:PMC8279004 OpenAlex:https://openalex.org/W3123057917

National Science Foundation

Grant: MCB-1921641

National Institutes of Health

Grant: 5R01GM115882

NIGMS NIH HHS

Grant: R01 GM115882

National Science Foundation

Grant: 1921641

URoL: Epigenetics 2: Reverse Engineering Human Epigenetic Machinery in Yeast

National Institutes of Health

Grant: 3R01GM115882-02S1

Structural and functional analysis of gene silencing

David and Lucile Packard Foundation

FWCI

7.38

Citation Percentile

1.0%

Citation Trend

2021

2022

2023

2024

2025

2026

green

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/8279004

publisherhttps://syndication.highwire.org/content/doi/10.1126/science.abc6663

publisherhttps://www.science.org/doi/pdf/10.1126/science.abc6663

journalhttps://doi.org/10.1126/science.abc6663

Fields of Study

Genomics and Chromatin DynamicsRNA modifications and cancerUbiquitin and proteasome pathways0301 basic medicine03 medical and health sciencesAcetylationChromatin Assembly and DisassemblyHistone-Lysine N-MethyltransferaseHistonesNuclear ProteinsNucleosomesProtein ConformationProtein Processing, Post-TranslationalSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins

MeSH Terms

AcetylationHistonesNuclear ProteinsNucleosomesProtein ConformationHistone-Lysine N-MethyltransferaseProtein Processing, Post-TranslationalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsChromatin Assembly and Disassembly

Keywords

Histone methyltransferaseHistone codeHistone H2AHistone H1Histone H3Histone methylationBiologyHistone H4Histone octamerHistoneCell biologyBiochemistryGene expressionNucleosomeDNAGeneDNA methylationSaccharomyces cerevisiae ProteinsProtein ConformationNuclear ProteinsAcetylationHistone-Lysine N-MethyltransferaseSaccharomyces cerevisiaeChromatin Assembly and DisassemblyNucleosomesHistonesProtein Processing, Post-Translational

Sustainable Development Goals

SDG 2: 2. Zero hungerSDG 3: 3. Good health