(Q41628403)

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Prevention of drug access to bacterial targets: permeability barriers and active efflux

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Antibiotic resistance caused by gram-negative multidrug efflux pumps

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

The SMR family: a novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

The projection structure of EmrE, a proton-linked multidrug transporter from Escherichia coli, at 7 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Conformational changes in the multidrug transporter EmrE associated with substrate binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Cloning and characterization of themvrCgene ofEscherichia coliK-12 which confers resistance against methyl viologen toxicity

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

A model for coupling of H(+) and substrate fluxes based on "time-sharing" of a common binding site

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

A common binding site for substrates and protons in EmrE, an ion-coupled multidrug transporter.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

A single carboxyl mutant of the multidrug transporter EmrE is fully functional

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

An amino acid cluster around the essential Glu-14 is part of the substrate- and proton-binding domain of EmrE, a multidrug transporter from Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Structure of the substrate binding pocket of the multidrug transporter EmrE: site-directed spin labeling of transmembrane segment 1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Determining the secondary structure and orientation of EmrE, a multi-drug transporter, indicates a transmembrane four-helix bundle.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

NMR investigation of the multidrug transporter EmrE, an integral membrane protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

High level cell-free expression and specific labeling of integral membrane proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Quaternary structure and function of transport proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Glucose transporter function is controlled by transporter oligomeric structure. A single, intramolecular disulfide promotes GLUT1 tetramerization

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

The phosphate carrier from yeast mitochondria. Dimerization is a prerequisite for function.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Oligomerization of NhaA, the Na+/H+ antiporter of Escherichia coli in the membrane and its functional and structural consequences.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

The lactose transport protein is a cooperative dimer with two sugar translocation pathways

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Negative dominance studies demonstrate the oligomeric structure of EmrE, a multidrug antiporter from Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Identification of the Dimer Interface of the Lactose Transport Protein from Streptococcus thermophilus

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Scanning Cysteine Accessibility of EmrE, an H+-coupled Multidrug Transporter fromEscherichia coli, Reveals a Hydrophobic Pathway for Solutes

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

Functional analysis of novel multidrug transporters from human pathogens

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

EmrE, an Escherichia coli 12-kDa multidrug transporter, exchanges toxic cations and H+ and is soluble in organic solvents

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5

In VitroMonomer Swapping in EmrE, a Multidrug Transporter fromEscherichia coli,Reveals That the Oligomer Is the Functional Unit

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900228-5