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References from Structural and functional comparison of hexahistidine tagged and untagged forms of small multidrug resistance protein, EmrE. Local targets link to admitted publications; unresolved targets remain external evidence.
The SMR family: a novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs
10.1111/j.1365-2958.1996.tb02462.x · 1996 · External reference
Small multidrug resistance proteins: a multidrug transporter family that continues to grow
10.1016/j.bbamem.2007.08.015 · 2008 · External reference
EmrE, an Escherichia coli 12-kDa multidrug transporter, exchanges toxic cations and H+ and is soluble in organic solvents
10.1074/jbc.270.12.6856 · 1995 · External reference
Negative dominance studies demonstrate the oligomeric structure of EmrE, a multidrug antiporter from Escherichia coli
10.1074/jbc.271.49.31044 · 1996 · External reference
A membrane‐embedded glutamate is required for ligand binding to the multidrug transporter EmrE
10.1093/emboj/19.2.234 · 2000 · External reference
Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer
10.1093/emboj/cdg611 · 2003 · External reference
Organic solvent extracted EmrE solubilized in dodecyl maltoside is monomeric and binds drug ligand
10.1016/j.bbrc.2004.11.164 · 2005 · External reference
X-ray structure of EmrE supports dual topology model
10.1073/pnas.0709387104 · 2007 · External reference
Multimeric forms of the small multidrug resistance protein EmrE in anionic detergent
10.1016/j.bbamem.2009.12.017 · 2010 · External reference
NMR investigation of the multidrug transporter EmrE, an integral membrane protein
10.1046/j.1432-1327.1998.2540610.x · 1998 · External reference
Metal chelate affinity chromatography, a new approach to protein fractionation
10.1038/258598a0 · 1975 · External reference
Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems
10.1007/s00253-002-1158-6 · 2003 · External reference
EmrE, a model for studying evolution and mechanism of ion-coupled transporters
1794 · External reference
Conformational changes in the multidrug transporter EmrE associated with substrate binding
10.1016/s0022-2836(03)00895-7 · 2003 · External reference
Comparison of three structures of the multidrug transporter EmrE
10.1016/j.sbi.2006.06.005 · 2006 · External reference
The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric
10.1074/jbc.m707899200 · 2008 · External reference
Substrate-induced tryptophan fluorescence changes in EmrE, the smallest ion-coupled multidrug transporter
10.1021/bi050356t · 2005 · External reference
In vitro monomer swapping in EmrE, a multidrug transporter from Escherichia coli, reveals that the oligomer is the functional unit
10.1074/jbc.m108229200 · 2001 · External reference
The Escherichia coli multidrug transporter EmrE is a dimer in the detergent-solubilised state
10.1016/j.jmb.2004.05.014 · 2004 · External reference
Investigation of ligand binding to the multidrug resistance protein EmrE by isothermal titration calorimetry
10.1529/biophysj.104.049247 · 2005 · External reference
Optimization of expression and the purification by organic extraction of the integral membrane protein EmrE
10.1016/s1046-5928(02)00525-9 · 2002 · External reference
In vitro unfolding and refolding of the small multidrug transporter EmrE
10.1016/j.jmb.2009.08.039 · 2009 · External reference
Small multidrug resistance protein EmrE reduces host pH and osmotic tolerance to metabolic quaternary cation osmoprotectants
10.1128/jb.00666-12 · 2012 · External reference
Outer membrane protein OmpW participates with small multidrug resistance protein member EmrE in quaternary cationic compound efflux
10.1128/jb.01483-14 · 2014 · External reference
A simplification of the protein assay method of Lowry et al. which is more generally applicable
10.1016/0003-2697(77)90043-4 · 1977 · External reference
Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
10.1006/jmbi.1996.0399 · 1996 · External reference
Visible fluorescent detection of proteins in polyacrylamide gels without staining
10.1016/j.ab.2003.10.047 · 2004 · External reference
Spectroscopic analysis of small multidrug resistance protein EmrE in the presence of various quaternary cation compounds
10.1016/j.bbamem.2012.01.022 · 2012 · External reference
Red-edge excitation of fluorescence and dynamic properties of proteins and membranes
10.1021/bi00308a026 · 1984 · External reference
Oxidative stress-induced cellular damage caused by UV and methyl viologen in Euglena gracilis and its suppression with rutin
10.1016/s1011-1344(02)00271-3 · 2002 · External reference
Autocatalytic oscillations in the early phase of the photoreduced methyl viologen-initiated fast kinetic reaction of hydrogenase
10.1074/jbc.m300623200 · 2003 · External reference
Use of wide-angle X-ray diffraction to measure shape and size of dispersed colloidal particles
10.1016/j.jcis.2009.06.006 · 2009 · External reference
Quasielastic light-scattering studies of aqueous biliary lipid systems. Mixed micelle formation in bile salt-lecithin solutions
10.1021/bi00545a001 · 1980 · External reference
Real-time imaging of lipid domains and distinct coexisting membrane protein clusters
10.1016/j.chemphyslip.2011.12.012 · 2012 · External reference
Visualizing a multidrug resistance protein, EmrE, with major bacterial lipids using Brewster angle microscopy
10.1016/j.chemphyslip.2013.01.007 · 2013 · External reference
Examination of EmrE conformational differences in various membrane mimetic environments
10.1139/o03-031 · 2003 · External reference
Exploring the binding domain of EmrE, the smallest multidrug transporter
10.1074/jbc.m504910200 · 2005 · External reference
Intermolecular orientational upward relaxation in viscous solutions of organic compounds
1979 · External reference
Direct evidence for substrate-induced proton release in detergent-solubilized EmrE, a multidrug transporter
10.1074/jbc.m312853200 · 2004 · External reference
Cation–pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp
10.1126/science.271.5246.163 · 1996 · External reference