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Division of labor between the pore-1 loops of the D1 and D2 AAA+ rings coordinates substrate selectivity of the ClpAP protease

Journal of Biological Chemistry(2021)10.1016/j.jbc.2021.101407Source: DataRank Database

Division of labor between the pore-1 loops of the D1 and D2 AAA+ rings coordinates substrate selectivity of the ClpAP protease is a research paper published in Journal of Biological Chemistry (2021). On theSindex it has a DataRank of 0. It has been cited 6 times.

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Open Access6 citations

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Enrichment:Funding (6 grants)Impact (FWCI 0.24)OA: goldTopics (45)IDs (PubMed, PMC, OpenAlex)Annotations (2)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 (4)

Sora Kim ORCID,Robert T. Sauer ORCID,Tania A. Baker ORCID,Kristin L Zuromski ORCID

Live enrichment

PubMed:34780718 PMC:PMC8666677 OpenAlex:https://openalex.org/W3212427487

National Science Foundation

Grant: 1745302

Graduate Research Fellowship Program (GRFP)

NIH

Grant: AI-016892

NIAID NIH HHS

Grant: R01 AI016892

National Institutes of Health

Grant: 5R01AI016892-23

REPRESSOR AND ANTIREPRESSOR PROTEINS OF BACTERIOPHAGE

HHMI

NSF

FWCI

0.24

Citation Percentile

0.6%

Citation Trend

2022

2024

2026

goldLicense: cc-by-nc-nd

journalhttp://www.jbc.org/article/S002192582101214X/pdf

publisherhttp://www.jbc.org/article/S002192582101214X/pdf

publisherhttps://api.elsevier.com/content/article/PII:S002192582101214X?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S002192582101214X?httpAccept=text/plain

journalhttps://doi.org/10.1016/j.jbc.2021.101407

Fields of Study

Peptidase Inhibition and AnalysisSignaling Pathways in DiseaseCellular transport and secretion0301 basic medicine0303 health sciences03 medical and health sciencesEndopeptidase ClpEscherichia coliEscherichia coli ProteinsProtein MultimerizationProtein Structure, SecondarySubstrate Specificity

MeSH Terms

Escherichia coliSubstrate SpecificityProtein Structure, SecondaryEscherichia coli ProteinsEndopeptidase ClpProtein Multimerization

Keywords

DegronAAA proteinsAdapter (computing)BiophysicsProteaseATPaseSubstrate (aquarium)Protein engineeringChemistryBiochemistryBiologyUbiquitinEnzymeUbiquitin ligaseStructure-functionProtein degradationEnzyme MechanismEnzyme MutationCysteine-mediated Cross-linkingAtpases Associated With Diverse Cellular ActivitiesEscherichia coli ProteinsEscherichia coliEndopeptidase ClpProtein MultimerizationProtein Structure, SecondaryResearch ArticleSubstrate Specificity

Sustainable Development Goals

SDG 0: Decent work and economic growth

Division of labor between the pore-1 loops of the D1 and D2 AAA+ rings coordinates substrate selectivity of the ClpAP protease

FAIR Checklist

Authors (4)

Funding (6 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)