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Effects of Distal Mutations on Prolyl-Adenylate Formation of Escherichia coli Prolyl-tRNA Synthetase

The Protein Journal(2020)10.1007/s10930-020-09910-3Source: DataRank Database

Effects of Distal Mutations on Prolyl-Adenylate Formation of Escherichia coli Prolyl-tRNA Synthetase is a research paper published in The Protein Journal (2020). On theSindex it has a DataRank of 0. It has been cited 7 times.

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0DataRank · unranked

Scored on demand from live citation data

Open Access7 citations

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (4 grants)Impact (FWCI 0.22)OA: greenTopics (43)IDs (PubMed, PMC, OpenAlex)Annotations (1)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)

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Authors (17)

Heidi Anderson,Lauren Adams ORCID,Dechen Wangmo ORCID,Shanzay Suhail ORCID,Aimee Almen

Live enrichment

PubMed:32681406 PMC:PMC7704565 OpenAlex:https://openalex.org/W3043267345

National Institutes of Health

Grant: GM117510-01

NIGMS NIH HHS

Grant: R15 GM117510

National Institutes of Health

Grant: 1R15GM117510-01

Exploring the Dynamics of Prolyl-tRNA Synthetases: Towards Developing a Screening Method for Species-Specific Inhibitors

Office of Research and Sponsored Programs, University of Wisconsin - Eau Claire

FWCI

0.22

Citation Percentile

0.5%

Citation Trend

2022

2024

2025

greenLicense: Springer TDM

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/7704565

GREENhttps://europepmc.org/articles/pmc7704565?pdf=render

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/7704565

publisherhttps://link.springer.com/content/pdf/10.1007/s10930-020-09910-3.pdf

publisherhttps://link.springer.com/article/10.1007/s10930-020-09910-3/fulltext.html

Fields of Study

RNA and protein synthesis mechanismsRNA modifications and cancerEnzyme Structure and FunctionChemistryMedicineBiology0301 basic medicine0303 health sciences03 medical and health sciencesAmino Acyl-tRNA SynthetasesCatalysisCatalytic DomainEscherichia coliEscherichia coli ProteinsMutation

MeSH Terms

Amino Acyl-tRNA SynthetasesCatalysisEscherichia coliMutationCatalytic DomainEscherichia coli Proteins

Keywords

EnzymeBiochemistryEscherichia coliTransfer RNAChemistryResidue (chemistry)Active siteBiologyAdenylate kinaseStereochemistryRNAGeneAminoacyl-tRNA synthetaseProtein FlexibilityProlyl-trna SynthetaseNon-catalytic ResidueDynamutAmino Acyl-tRNA SynthetasesCatalytic DomainEscherichia coli ProteinsMutationCatalysis

Sustainable Development Goals

SDG 3: 3. Good health