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

Elucidation of the substrate of tRNA-modifying enzymes MnmEG leads to in vitro reconstitution of an evolutionarily conserved uridine hypermodification

Journal of Biological Chemistry(2022)10.1016/j.jbc.2022.102548Source: DataRank Database

Elucidation of the substrate of tRNA-modifying enzymes MnmEG leads to in vitro reconstitution of an evolutionarily conserved uridine hypermodification is a research paper published in Journal of Biological Chemistry (2022). On theSindex it has a DataRank of 0. It has been cited 18 times.

N/A

0DataRank · unranked

Scored on demand from live citation data

Open Access18 citations

Download PDF

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 (5 grants)Impact (FWCI 1.18)OA: goldTopics (31)IDs (PubMed, PMC, OpenAlex)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 (3)

Anthony P. Young ORCID,Vahe Bandarian ORCID,Praneeth Bommisetti ORCID

Live enrichment

PubMed:36181794 PMC:PMC9626948 OpenAlex:https://openalex.org/W4297473002

University of Utah

Grant: SG13000009

National Institute of General Medical Sciences

Grant: R35 GM126956

National Institutes of Health

Grant: 5R35GM126956-05

Discovery and Mechanism of Biosynthetic Enzymes

National Institutes of Health

University of Wisconsin-Madison

FWCI

1.18

Citation Percentile

0.8%

Citation Trend

2023

2024

2025

2026

goldLicense: cc-by

journalhttp://www.jbc.org/article/S0021925822009929/pdf

publisherhttp://www.jbc.org/article/S0021925822009929/pdf

publisherhttps://api.elsevier.com/content/article/PII:S0021925822009929?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0021925822009929?httpAccept=text/plain

journalhttps://doi.org/10.1016/j.jbc.2022.102548

Fields of Study

RNA modifications and cancerRNA and protein synthesis mechanismsATP Synthase and ATPases Research0301 basic medicine0303 health sciences03 medical and health sciences

MeSH Terms

RNA, TransferUridineReducing AgentsOne-Carbon Group TransferasesEscherichia coli Proteins

Keywords

Transfer RNAUridineIn vitroEnzymeSubstrate (aquarium)BiochemistryBiologyChemistryRNAGeneEcologytRNARna ModificationsNucleic Acid EnzymologyTrna MethyltransferaseRNA, TransferReducing AgentsEscherichia coli ProteinsResearch ArticleOne-Carbon Group Transferases

Sustainable Development Goals

SDG 0: Life in Land