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Burst kinetics and CNNM binding are evolutionarily conserved properties of phosphatases of regenerating liver

Journal of Biological Chemistry(2023)10.1016/j.jbc.2023.103055Source: DataRank Database

Burst kinetics and CNNM binding are evolutionarily conserved properties of phosphatases of regenerating liver is a research paper published in Journal of Biological Chemistry (2023). 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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pdb doi

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (11 grants)Impact (FWCI 0.74)OA: goldTopics (51)IDs (PubMed, PMC, OpenAlex)Annotations (2)

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 (4)

Robert H. Goldstein ORCID,Guennadi Kozlov ORCID,Kalle Gehring ORCID,Rayan Fakih ORCID

Live enrichment

PubMed:36822330 PMC:PMC10040874 OpenAlex:https://openalex.org/W4321438830

Natural Sciences and Engineering Research Council of Canada

Grant: RGPIN-2020-07195

Natural Sciences and Engineering Research Council of Canada

Grant: HHSN272201700059C

Natural Sciences and Engineering Research Council of Canada

Grant: unidentified

unidentified

Canada Foundation for Innovation

National Institute of Allergy and Infectious Diseases

National Research Council

U.S. Department of Health and Human Services

Jewish Community Foundation

National Institutes of Health

Canadian Institutes of Health Research

University of Saskatchewan

FWCI

0.74

Citation Percentile

0.7%

Citation Trend

2023

2024

2025

2026

goldLicense: cc-by

journalhttp://www.jbc.org/article/S0021925823001874/pdf

publisherhttp://www.jbc.org/article/S0021925823001874/pdf

publisherhttps://api.elsevier.com/content/article/PII:S0021925823001874?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0021925823001874?httpAccept=text/plain

journalhttps://doi.org/10.1016/j.jbc.2023.103055

Fields of Study

Protein Tyrosine PhosphatasesMicrotubule and mitosis dynamicsMetalloenzymes and iron-sulfur proteins0301 basic medicine0303 health sciences03 medical and health sciencesAnimalsHumansKineticsDrosophila melanogasterSignal TransductionLiverMammals

MeSH Terms

AnimalsDrosophila melanogasterHumansKineticsLiverMammalsSignal TransductionProtein Tyrosine Phosphatases

Keywords

PhosphataseBiologyBiochemistryIsothermal titration calorimetryEnzyme kineticsEnzymeFunction (biology)Conserved sequenceAllosteric regulationCell biologyGeneticsGeneActive sitePeptide sequenceProtein phosphataseX-ray crystallographyCell signalingAnalytical UltracentrifugationDual-specificity Phosphoprotein PhosphatasePhosphocysteineUex ProteinMammalsKineticsDrosophila melanogasterLiverAnimalsHumansProtein Tyrosine PhosphatasesResearch ArticleSignal Transduction