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Enterococcus NlpC/p60 Peptidoglycan Hydrolase SagA Localizes to Sites of Cell Division and Requires Only a Catalytic Dyad for Protease Activity

Biochemistry(2020)10.1021/acs.biochem.0c00755Source: DataRank Database

Enterococcus NlpC/p60 Peptidoglycan Hydrolase SagA Localizes to Sites of Cell Division and Requires Only a Catalytic Dyad for Protease Activity is a research paper published in Biochemistry (2020). On theSindex it has a DataRank of 0. It has been cited 18 times.

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Open Access18 citations

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (9 grants)Impact (FWCI 0.65)OA: greenTopics (53)IDs (PubMed, OpenAlex)SDGs (2)

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Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (6)

Ti‐Yu Lin,Yadyvic Estrella,Byung-Chul Kim ORCID,Henrik Molina ORCID,Howard C. Hang ORCID

Live enrichment

PubMed:33136372 OpenAlex:https://openalex.org/W3095242996

National Cancer Institute

Grant: R01 CA245292

Kenneth Rainin Foundation

Grant: Synergy Award

Leona M. and Harry B. Helmsley Charitable Trust

Grant: Postdoctoral fellowship

National Institutes of Health

Grant: T32 A1070084

National Institute of General Medical Sciences

Grant: R01 GM103593

National Institutes of Health

Grant: 7R01CA245292-03

Translation of commensal bacteria mechanism for immunotherapy

National Institutes of Health

Grant: 2R01GM103593-05

Elucidation of Commensal Bacteria Mechanisms Required for Host Protection

NIAID NIH HHS

Grant: R21 AI156674

NIAID NIH HHS

Grant: T32 AI070084

FWCI

0.65

Citation Percentile

0.7%

Citation Trend

2022

2023

2024

2025

2026

greenLicense: STM Policy #29

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/8191637

publisherhttps://pubs.acs.org/doi/pdf/10.1021/acs.biochem.0c00755

journalhttps://doi.org/10.1021/acs.biochem.0c00755

repositoryhttps://pubmed.ncbi.nlm.nih.gov/33136372

Fields of Study

Bacterial Genetics and BiotechnologyRNA and protein synthesis mechanismsBiochemical and Structural Characterization0301 basic medicine0303 health sciences03 medical and health sciencesBacterial ProteinsCatalytic DomainCell DivisionEnterococcusMicroscopy, Electron, TransmissionMicroscopy, FluorescenceMolecular Docking SimulationMutagenesis, Site-DirectedN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationStructure-Activity Relationship

MeSH Terms

Bacterial ProteinsCell DivisionMicroscopy, FluorescenceN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanStructure-Activity RelationshipMutagenesis, Site-DirectedEnterococcusSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationCatalytic DomainMicroscopy, Electron, TransmissionMolecular Docking Simulation

Keywords

PeptidoglycanBiologyHydrolaseCatalytic triadCell wallBiochemistryMutagenesisMicrobiologyCell biologyEnzymeActive siteMutationN-Acetylmuramoyl-L-alanine AmidaseMolecular Docking SimulationStructure-Activity RelationshipBacterial ProteinsMicroscopy, Electron, TransmissionMicroscopy, FluorescenceCatalytic DomainSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationMutagenesis, Site-DirectedCell DivisionEnterococcus

Sustainable Development Goals

SDG 3: 3. Good healthSDG 0: Life in Land