Gromet-Elhanan Z, Sokolov M
Photosynth Res. 2013; 46(1-2):79-86.
PMID: 24301570
DOI: 10.1007/BF00020418.
La T, Clark-Walker G, Wang X, Wilkens S, Chen X
Eukaryot Cell. 2013; 12(11):1451-61.
PMID: 24014764
PMC: 3837939.
DOI: 10.1128/EC.00177-13.
Jose-Nunez C, Torres-Larios A, Ramirez-Silva L, Mendoza G, Salcedo G, Gomez-Puyou A
J Bioenerg Biomembr. 2009; 40(6):561-8.
PMID: 19139978
DOI: 10.1007/s10863-008-9192-4.
Kobayashi M, Yagi H, Yamazaki T, Yoshida M, Akutsu H
J Biomol NMR. 2008; 40(3):165-74.
PMID: 18183492
DOI: 10.1007/s10858-007-9216-0.
Pedersen M, Koebmann B, Jensen P, Nilsson D
Appl Environ Microbiol. 2002; 68(11):5249-57.
PMID: 12406711
PMC: 129885.
DOI: 10.1128/AEM.68.11.5249-5257.2002.
Partial assembly of the yeast mitochondrial ATP synthase.
Mueller D
J Bioenerg Biomembr. 2002; 32(4):391-400.
PMID: 11768301
DOI: 10.1023/a:1005532104617.
The gamma-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli.
Omote H, Sambonmatsu N, Saito K, Sambongi Y, Yanagida T, Wada Y
Proc Natl Acad Sci U S A. 1999; 96(14):7780-4.
PMID: 10393898
PMC: 22138.
DOI: 10.1073/pnas.96.14.7780.
Modification of domains of alpha and beta subunits of F1-ATPase from the thermophylic bacterium PS3, in their isolated and associated forms, by 3'-O-(4-benzoyl)benzoyl adenosine 5'-triphosphate (BzATP).
Bar-Zvi D, Yoshida M, Shavit N
J Bioenerg Biomembr. 1996; 28(6):471-81.
PMID: 8953379
DOI: 10.1007/BF02110437.
The energy transmission in ATP synthase: from the gamma-c rotor to the alpha 3 beta 3 oligomer fixed by OSCP-b stator via the beta DELSEED sequence.
Kagawa Y, Hamamoto T
J Bioenerg Biomembr. 1996; 28(5):421-31.
PMID: 8951089
DOI: 10.1007/BF02113984.
The TF1-ATPase and ATPase activities of assembled alpha 3 beta 3 gamma, alpha 3 beta 3 gamma delta, and alpha 3 beta 3 gamma epsilon complexes are stimulated by low and inhibited by high concentrations of rhodamine 6G whereas the dye only inhibits....
Paik S, Yokoyama K, Yoshida M, Ohta T, Kagawa Y, Allison W
J Bioenerg Biomembr. 1993; 25(6):679-84.
PMID: 8144495
DOI: 10.1007/BF00770254.
Ligand-dependent structural variations in Escherichia coli F1 ATPase revealed by cryoelectron microscopy.
Gogol E, Johnston E, Aggeler R, Capaldi R
Proc Natl Acad Sci U S A. 1990; 87(24):9585-9.
PMID: 2148209
PMC: 55217.
DOI: 10.1073/pnas.87.24.9585.
Interaction of Mg2+ with F0.F1 mitochondrial ATPase as related to its slow active/inactive transition.
Bulygin V, Vinogradov A
Biochem J. 1991; 276 ( Pt 1):149-56.
PMID: 1828147
PMC: 1151157.
DOI: 10.1042/bj2760149.
Kinetic studies of ATP synthase: the case for the positional change mechanism.
LaNoue K, Duszynski J
J Bioenerg Biomembr. 1992; 24(5):499-506.
PMID: 1429543
DOI: 10.1007/BF00762368.
Identification of subunits required for the catalytic activity of the F1-ATPase.
Gromet-Elhanan Z
J Bioenerg Biomembr. 1992; 24(5):447-52.
PMID: 1429538
DOI: 10.1007/BF00762361.
The alpha beta complexes of ATP synthase: the alpha 3 beta 3 oligomer and alpha 1 beta 1 protomer.
Kagawa Y, Ohta S, Harada M, Kihara H, Ito Y, Sato M
J Bioenerg Biomembr. 1992; 24(5):441-5.
PMID: 1429537
DOI: 10.1007/BF00762360.