Negative Dominance Studies Demonstrate the Oligomeric Structure of EmrE, a Multidrug Antiporter fromEscherichia Coli

Journal of Biological Chemistry - United States
doi 10.1074/jbc.271.49.31044
Full Text
Abstract

Available in full text

Date
Authors
Publisher

American Society for Biochemistry & Molecular Biology (ASBMB)

Related search

Oligomeric Structure of the Carnitine Transporter CaiT fromEscherichia Coli

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
2005English

An Amino Acid Cluster Around the Essential Glu-14 Is Part of the Substrate- And Proton-Binding Domain of EmrE, a Multidrug Transporter fromEscherichia Coli

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
2003English

Structure and Activity of ClpB fromEscherichia Coli

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
2000English

The Structure and Mechanism of Serine Acetyltransferase fromEscherichia Coli

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
2004English

Structural Dynamics of the Small Multidrug Transporter EMRE

Biophysical Journal
Biophysics
2016English

Crystal Structure of the Thermostable Mutant of Hygromycin Phosphotransferase fromEscherichia Coli

Acta Crystallographica Section A Foundations of Crystallography
2008English

Crystal Structure of Conserved Hypothetical Protein YBEY fromEscherichia Coli

Acta Crystallographica Section A Foundations of Crystallography
2005English

Chemical Modification of Single-Cys EmrE, a Small Multidrug Transporter in Escherichia Coli, by Biotin-Pe-Maleimide.

Seibutsu Butsuri
2003English

Glutaredoxin-3 fromEscherichia Coli

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
1996English

Amanote Research

Note-taking for researchers

Follow Amanote

© 2024 Amaplex Software S.P.R.L. All rights reserved.

Privacy PolicyRefund Policy