Essential Role of a GXXXG Motif for Membrane Channel Formation by Helicobacter pylori Vacuolating Toxin
Open Access
- 1 April 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (14), 12101-12108
- https://doi.org/10.1074/jbc.m212595200
Abstract
No abstract availableKeywords
This publication has 83 references indexed in Scilit:
- Identification of amino acid residues lining the pore of a gap junction channelThe Journal of cell biology, 2002
- Multiple Oligomeric States of the Helicobacter pylori Vacuolating Toxin Demonstrated by Cryo-electron MicroscopyJournal of Molecular Biology, 2002
- Motifs of serine and threonine can drive association of transmembrane helicesJournal of Molecular Biology, 2002
- The GxxxG motif: A framework for transmembrane helix-helix associationJournal of Molecular Biology, 2000
- 3D imaging of the 58 kda cell binding subunit of the Helicobacter pylori cytotoxinJournal of Molecular Biology, 1999
- The Acid Activation ofHelicobacter pyloriToxin VacA: Structural and Membrane Binding StudiesBiochemical and Biophysical Research Communications, 1998
- The Structure of the Potassium Channel: Molecular Basis of K + Conduction and SelectivityScience, 1998
- Bacillus thuringiensisCrylA(a) Insecticidal Toxin: Crystal Structure and Channel FormationJournal of Molecular Biology, 1995
- Packing of Coat Protein Amphipathic and Transmembrane Helices in Filamentous Bacteriophage M13: Role of Small Residues in Protein Oligomeriza tionJournal of Molecular Biology, 1995
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982