The β Subunit Loop That Couples Catalysis and Rotation in ATP Synthase Has a Critical Length

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

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

Analysis of the Open and Closed Conformations of the β Subunits in Thermophilic F1-ATPase by Solution NMR

(2010) Masumi Kobayashi et al.   JOURNAL OF MOLECULAR BIOLOGY

ATP Synthase with Its γ Subunit Reduced to the N-terminal Helix Can Still Catalyze ATP Synthesis

(2009) Nelli Mnatsakanyan et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Role of the βDELSEED-loop of ATP Synthase

(2009) Nelli Mnatsakanyan et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Mechanism of Inhibition by C-terminal α-Helices of the ϵ Subunit ofEscherichia coliFoF1-ATP Synthase

(2009) Ryota Iino et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Torque generation and elastic power transmission in the rotary FOF1-ATPase

(2009) Wolfgang Junge et al.   NATURE

The rotary mechanism of the ATP synthase

(2008) Robert K. Nakamoto et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

A Rotor-Stator Cross-link in the F1-ATPase Blocks the Rate-limiting Step of Rotational Catalysis

(2008) Joanne A. Baylis Scanlon et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Stepwise Propagation of the ATP-induced Conformational Change of the F1-ATPase β Subunit Revealed by NMR

(2008) Hiromasa Yagi et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

How subunit coupling produces the  -subunit rotary motion in F1-ATPase

(2008) J. Pu et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA