Multicomponent drug efflux complexes: architecture and mechanism of assembly

The multidrug resistance efflux complex, EmrAB from Escherichia coli forms a dimer in vitro

(2009) Mikio Tanabe et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Crystal Structure of the Periplasmic Region of MacB, a Noncanonic ABC Transporter,

(2009) Yongbin Xu et al.   BIOCHEMISTRY

Assembly and transport mechanism of tripartite drug efflux systems

(2009) Rajeev Misra et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Drug transport mechanism of the AcrB efflux pump

(2009) Klaas M. Pos   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

EmrE, a model for studying evolution and mechanism of ion-coupled transporters

(2009) Shimon Schuldiner   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

The C-Terminal Domain of AcrA Is Essential for the Assembly and Function of the Multidrug Efflux Pump AcrAB-TolC

(2009) Q. Ge et al.   JOURNAL OF BACTERIOLOGY

Crystal Structure of the Multidrug Exporter MexB from Pseudomonas aeruginosa

(2009) Gaby Sennhauser et al.   JOURNAL OF MOLECULAR BIOLOGY

Crystal Structure of the Periplasmic Component of a Tripartite Macrolide-Specific Efflux Pump

(2009) Soohwan Yum et al.   JOURNAL OF MOLECULAR BIOLOGY

Tracking Membrane Protein Association in Model Membranes

(2009) Myriam Reffay et al.   PLoS One

The assembled structure of a complete tripartite bacterial multidrug efflux pump

(2009) M. F. Symmons et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Kinetic behavior of the major multidrug efflux pump AcrB of Escherichia coli

(2009) K. Nagano et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structure of P-Glycoprotein Reveals a Molecular Basis for Poly-Specific Drug Binding

(2009) S. G. Aller et al.   SCIENCE

Bacterial multidrug transport through the lens of the major facilitator superfamily

(2008) Nir Fluman et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Structural and functional diversity of bacterial membrane fusion proteins

(2008) Helen I. Zgurskaya et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Molecular basis of multidrug transport by ABC transporters

(2008) Markus A. Seeger et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Mechanisms of RND multidrug efflux pumps

(2008) Hiroshi Nikaido et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Multidrug efflux transporter, AcrB—the pumping mechanism

(2008) S MURAKAMI   CURRENT OPINION IN STRUCTURAL BIOLOGY

Structural insights into ABC transporter mechanism

(2008) Michael L Oldham et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Covalently Linked Trimer of the AcrB Multidrug Efflux Pump Provides Support for the Functional Rotating Mechanism

(2008) Y. Takatsuka et al.   JOURNAL OF BACTERIOLOGY

MacAB Is Involved in the Secretion of Escherichia coli Heat-Stable Enterotoxin II

(2008) H. Yamanaka et al.   JOURNAL OF BACTERIOLOGY

MacB ABC Transporter Is a Dimer Whose ATPase Activity and Macrolide-binding Capacity Are Regulated by the Membrane Fusion Protein MacA

(2008) Hong Ting Lin et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems

(2008) A. L. Davidson et al.   MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS

Genetic and functional characterization of the gene cluster directing the biosynthesis of putisolvin I and II in Pseudomonas putida strain PCL1445

(2008) J.-F. Dubern et al.   MICROBIOLOGY-SGM

Assembly and Channel Opening in a Bacterial Drug Efflux Machine

(2008) Vassiliy N. Bavro et al.   MOLECULAR CELL

Engineered disulfide bonds support the functional rotation mechanism of multidrug efflux pump AcrB

(2008) Markus A Seeger et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Structure and mechanism of ATP-binding cassette transporters

(2008) K. P Locher   PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES

Opening and closing of the periplasmic gate in lactose permease

(2008) Y. Zhou et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA