Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers

Role of the Protective Antigen Octamer in the Molecular Mechanism of Anthrax Lethal Toxin Stabilization in Plasma

(2010) Alexander F. Kintzer et al.   JOURNAL OF MOLECULAR BIOLOGY

Toward an atomic model of the 26S proteasome

(2009) Yifan Cheng   CURRENT OPINION IN STRUCTURAL BIOLOGY

The 26 S Proteasome: From Basic Mechanisms to Drug Targeting

(2009) Ami Navon et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Protective Antigen Component of Anthrax Toxin Forms Functional Octameric Complexes

(2009) Alexander F. Kintzer et al.   JOURNAL OF MOLECULAR BIOLOGY

Lethal factor unfolding is the most force-dependent step of anthrax toxin translocation

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

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side

(2008) Yali Li et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Peptide and Protein Binding in the Axial Channel of Hsp104

(2008) Ronnie Lum et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Structure of a complex of the ATPase SecA and the protein-translocation channel

(2008) Jochen Zimmer et al.   NATURE

GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore

(2008) Hiroo Katayama et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Protein unfolding by a AAA+ protease is dependent on ATP-hydrolysis rates and substrate energy landscapes

(2008) Andreas Martin et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY