Fof1-atp Synthase
FoF1-ATP Synthase is a transmembrane enzyme complex that catalyzes the synthesis of adenosine triphosphate (ATP) through the coupling of proton motive force-driven conformational changes in its Fo and F1 domains, distinguishing it from other ATP-generating systems by its rotary mechanical mechanism and chemiosmotic dependence.
543
Publications
33.1K
Citations
1.7K
Authors
496
Institutions
Publications per year
2017–2026
75
Variants
F1f0-atp Synthase
Parents
543
Direct observation of the rotation of F1-ATPase
Hiroyuki Noji, Ryohei Yasuda, Masasuke Yoshida et al. · Nature · 1997 · 2.2K citations
Hiromi Imamura, Kim Phuong Huynh Nhat, Hiroko Togawa et al. · Proceedings of the National Academy of Sciences · 2009 · 1.1K citations · Full text
Mechanically driven ATP synthesis by F1-ATPase
Hiroyasu Itoh, Akira Takahashi, Kengo Adachi et al. · Nature · 2004 · 551 citations
1–5 of 543
1.7K
30
h-index
21
h-index
18
h-index
14
h-index
13
h-index
1–5 of 1.7K
496
Tokyo Institute of Technology
Tokyo, Japan
28 h-index
95 publications
13.5K citations
University of Wisconsin–Madison
Madison, United States
21 h-index
56 publications
4.9K citations
Japan Science and Technology Agency
Tokyo, Japan
20 h-index
56 publications
6.5K citations
The University of Osaka
Osaka, Japan
19 h-index
71 publications
9.5K citations
The University of Tokyo
Tokyo, Japan
17 h-index
68 publications
5.8K citations

Osnabrück University
Osnabrück, Germany
16 h-index
68 publications
2.3K citations
Max Planck Institute of Biophysics
Frankfurt am Main, Germany
16 h-index
57 publications
7.1K citations

MRC Laboratory of Molecular Biology
Cambridge, United Kingdom
14 h-index
45 publications
4.3K citations
1–8 of 496
JBC · 74 publications · 4.2K citations
42
h-index
53 publications · 1.9K citations
26
h-index
PNAS · 25 publications · 3.5K citations
22
h-index
29 publications · 1.6K citations
22
h-index
21 publications · 564 citations
16
h-index
1–5