Structural and functional comparison of hexahistidine tagged and untagged forms of small multidrug resistance protein, EmrE-Reference-Cited by-同舟云学术

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Structural and functional comparison of hexahistidine tagged and untagged forms of small multidrug resistance protein, EmrE

Published:2015-05 Issue: Volume:1 Page:22-32
ISSN:2405-5808
Container-title:Biochemistry and Biophysics Reports
language:en
Short-container-title:Biochemistry and Biophysics Reports

Author:

Qazi S. Junaid S.,Chew Raymond,Bay Denice C.,Turner Raymond J.

Funder

Alberta Innovates – Health Solutions (AIHS)

Natural Sciences and Engineering Research Council of Canada (NSERC)

Publisher

Elsevier BV

Subject

Biochemistry,Biophysics

Reference40 articles.

1. The SMR family: a novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs;Paulsen;Mol. Microbiol.,1996

2. Small multidrug resistance proteins: a multidrug transporter family that continues to grow;Bay;Biochim. Biophys. Acta (BBA) – Biomembr.,2008

3. EmrE, an Escherichia coli 12-kDa multidrug transporter, exchanges toxic cations and H+ and is soluble in organic solvents;Yerushalmi;J. Biol. Chem.,1995

4. Negative dominance studies demonstrate the oligomeric structure of EmrE, a multidrug antiporter from Escherichia coli;Yerushalmi;J. Biol. Chem.,1996

5. A membrane‐embedded glutamate is required for ligand binding to the multidrug transporter EmrE;Muth;EMBO J.,2000

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