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Charge neutralization of the active site glutamates does not limit substrate binding and transport by small multidrug resistance transporter EmrE

Journal of Biological Chemistry(2022)10.1016/j.jbc.2022.102805Source: DataRank Database

Charge neutralization of the active site glutamates does not limit substrate binding and transport by small multidrug resistance transporter EmrE is a research paper published in Journal of Biological Chemistry (2022). On theSindex it has a DataRank of 0. It has been cited 4 times.

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Open Access4 citations

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (7 grants)Impact (FWCI 0.19)OA: goldTopics (63)IDs (PubMed, OpenAlex)SDGs (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 (6)

Merissa Brousseau ORCID,Grant S. Hisao ORCID,M. Soltani ORCID,James H. Davis ORCID,Katherine A. Henzler‐Wildman ORCID

Live enrichment

PubMed:36529287 OpenAlex:https://openalex.org/W4311775285

National Institutes of Health

Grant: R24GM141526

National Institute of General Medical Sciences

Grant: R35GM141748

National Institute of General Medical Sciences

Grant: R01GM095839

National Institutes of Health

Grant: 5R35GM141748-03

Molecular Mechanisms of Channels and Transporters

National Institutes of Health

Grant: 5R01GM095839-07

Transport Mechanism of the Multidrug Resistance Efflux Protein, EmrE

National Institutes of Health

Grant: 1F32GM013039-01

MOLECULAR ANALYSIS OF THE YEAST HEAT SHOCK TRANSCRIPTION

National Institutes of Health

Grant: 1R24GM141526-01

NMR User Program at NMRFAM

FWCI

0.19

Citation Percentile

0.5%

Citation Trend

2024

2025

2026

goldLicense: cc-by

journalhttp://www.jbc.org/article/S0021925822012480/pdf

publisherhttp://www.jbc.org/article/S0021925822012480/pdf

publisherhttps://api.elsevier.com/content/article/PII:S0021925822012480?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0021925822012480?httpAccept=text/plain

journalhttps://doi.org/10.1016/j.jbc.2022.102805

Fields of Study

Drug Transport and Resistance MechanismsAmino Acid Enzymes and MetabolismDNA and Nucleic Acid Chemistry0301 basic medicine0303 health sciences03 medical and health sciencesAntiportersCatalytic DomainEscherichia coliEscherichia coli ProteinsGlutamatesProtonsSubstrate SpecificityStatic ElectricityProtein BindingNuclear Magnetic Resonance, BiomolecularHydrogen-Ion ConcentrationDrug Resistance, Multiple, BacterialIon Transport

MeSH Terms

Escherichia coliGlutamatesHydrogen-Ion ConcentrationProtein BindingProtonsSubstrate SpecificityIon TransportAntiportersNuclear Magnetic Resonance, BiomolecularCatalytic DomainDrug Resistance, Multiple, BacterialEscherichia coli ProteinsStatic Electricity

Keywords

NeutralizationSubstrate (aquarium)TransporterMultiple drug resistanceChemistryBinding siteCharge (physics)BiophysicsBiologyBiochemistryVirologyPhysicsEcologyIon TransportEscherichia coli ProteinsStatic ElectricityHydrogen-Ion ConcentrationAntiportersSubstrate SpecificityGlutamatesCatalytic DomainDrug Resistance, Multiple, BacterialEscherichia coliProtonsNuclear Magnetic Resonance, BiomolecularResearch ArticleProtein Bindingelectrophysiologyglutamatemembrane transportmultidrug transporter

Sustainable Development Goals

SDG 3: 3. Good healthSDG 0: Clean water and sanitation