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Human protein arginine methyltransferases (PRMTs) can be optimally active under nonphysiological conditions

Journal of Biological Chemistry(2022)10.1016/j.jbc.2022.102290Source: DataRank Database

Human protein arginine methyltransferases (PRMTs) can be optimally active under nonphysiological conditions is a research paper published in Journal of Biological Chemistry (2022). On theSindex it has a DataRank of 0.373. It has been cited 11 times.

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0.373DataRank · unranked

Scored on demand from live citation data

Open Access11 citations

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (5 grants)Impact (FWCI 0.78)OA: goldTopics (68)IDs (PubMed, PMC, 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)

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DataRank Breakdown

Base Score 100%Citation Network 0%

Base Score Contribution

0.373

From this paper's citation signal

Citation Network Contribution

Citation network not refreshed for this result

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Authors (2)

Steven Clarke ORCID,Troy L. Lowe ORCID

Live enrichment

PubMed:35868559 PMC:PMC9418908 OpenAlex:https://openalex.org/W4286252630

National Science Foundation

Grant: MCB-1714569

National Institutes of Health

Grant: GM007185

NIGMS NIH HHS

Grant: T32 GM007185

National Science Foundation

Grant: 1714569

Role of Protein Methylation in Translation

University of California, Los Angeles

FWCI

0.78

Citation Percentile

0.7%

Citation Trend

2023

2024

2025

2026

goldLicense: cc-by-nc-nd

journalhttps://doi.org/10.1016/j.jbc.2022.102290

GOLDhttps://doi.org/10.1016/j.jbc.2022.102290

publisherhttps://doi.org/10.1016/j.jbc.2022.102290

publisherhttps://api.elsevier.com/content/article/PII:S0021925822007323?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0021925822007323?httpAccept=text/plain

Fields of Study

Cancer-related gene regulationEpigenetics and DNA MethylationMedicineBiologyChemistry0301 basic medicine03 medical and health sciences0303 health sciencesArginineHumansHydrogen-Ion ConcentrationMethylationOsmolar ConcentrationProtein Processing, Post-TranslationalProtein-Arginine N-MethyltransferasesTemperatureRepressor Proteins

MeSH Terms

ArginineHumansHydrogen-Ion ConcentrationMethylationOsmolar ConcentrationProtein-Arginine N-MethyltransferasesProtein Processing, Post-TranslationalRepressor ProteinsTemperature

Keywords

Protein arginine methyltransferase 5MethyltransferaseMethylationArginineIonic strengthChemistryEnzymeBiochemistryIonic bondingBiophysicsBiologyAmino acidIonAqueous solutionOrganic chemistryhistone methylationTemperature DependenceProtein MethylationS-adenosylmethionine (Sam)Ph EffectsProtein Arginine N-methyltransferase 5 (Prmt5)Posttranslational Modification (Ptm)Intracellular Stress570Biochemistry & Molecular BiologyProtein-Arginine N-Methyltransferases610Medical and Health SciencesHumansProtein Processingposttranslational modificationS-adenosylmethionineprotein arginine N-methyltransferase 5Osmolar ConcentrationPost-TranslationalTemperatureBiological SciencesHydrogen-Ion ConcentrationRepressor ProteinsChemical SciencesProtein Processing, Post-TranslationalResearch Article