Structures of the thermophilic F1-ATPase ε subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1

By H. Yagi, N. Kajiwara, Hideaki Tanaka, T. Tsukihara, Y. Kato-Yamada, Masasuke Yoshida, H. Akutsu. Proceedings of the National Academy of Sciences of the United States of America, 2007

117 citations recorded by the source corpus.

Subfields: Molecular Biology, Structural Biology

View Paper: https://www.semanticscholar.org/paper/1e6b9689701f2746689f89040eb5758c996a65d0

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1. H. Imamura
2. K. P. Huynh Nhat
3. H. Togawa
4. Kenta Saito
5. R. Iino
6. Y. Kato-Yamada
7. H. Noji
8. T. Nagai

Citations in the corpus

• Visualization of ATP levels inside single living cells with fluorescence resonance energy transfer-based genetically encoded indicators (2009, background): “Furthermore, the subunit undergoes a large conformational change into a folded form upon ATP binding, by bundling the two -helices, which are relaxed in the absence of ATP (13, 14) (Fig.”