Solution structure of subunit γ (γ1-204) of the Mycobacterium tuberculosis F-ATP synthase and the unique loop of γ165-178, representing a novel TB drug target

Rotation and structure of FoF1-ATP synthase

(2011) D. Okuno et al.   JOURNAL OF BIOCHEMISTRY

Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an autoinhibited conformation

(2011) Gino Cingolani et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

ATP synthase in slow- and fast-growing mycobacteria is active in ATP synthesis and blocked in ATP hydrolysis direction

(2010) Anna C. Haagsma et al.   FEMS MICROBIOLOGY LETTERS

Mycobacterial Subversion of Chemotherapeutic Reagents and Host Defense Tactics: Challenges in Tuberculosis Drug Development

(2009) Liem Nguyen et al.   Annual Review of Pharmacology and Toxicology

The Mycobacterium tuberculosis DosR Regulon Assists in Metabolic Homeostasis and Enables Rapid Recovery from Nonrespiring Dormancy

(2009) R. L. Leistikow et al.   JOURNAL OF BACTERIOLOGY

The Past and Future of Tuberculosis Research

(2009) Iñaki Comas et al.   PLoS Pathogens

Unique Rotary ATP Synthase and Its Biological Diversity

(2008) Christoph von Ballmoos et al.   Annual Review of Biophysics

The protonmotive force is required for maintaining ATP homeostasis and viability of hypoxic, nonreplicating Mycobacterium tuberculosis

(2008) S. P. S. Rao et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA