318 related articles for article (PubMed ID: 10393898)
1. 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; Iwamoto-Kihara A; Yanagida T; Wada Y; Futai M
Proc Natl Acad Sci U S A; 1999 Jul; 96(14):7780-4. PubMed ID: 10393898
[TBL] [Abstract][Full Text] [Related]
2. Subunit rotation of ATP synthase embedded in membranes: a or beta subunit rotation relative to the c subunit ring.
Nishio K; Iwamoto-Kihara A; Yamamoto A; Wada Y; Futai M
Proc Natl Acad Sci U S A; 2002 Oct; 99(21):13448-52. PubMed ID: 12357031
[TBL] [Abstract][Full Text] [Related]
3. Mechanism of energy coupling in the FOF1-ATP synthase: the uncoupling mutation, gammaM23K, disrupts the use of binding energy to drive catalysis.
Al-Shawi MK; Nakamoto RK
Biochemistry; 1997 Oct; 36(42):12954-60. PubMed ID: 9335555
[TBL] [Abstract][Full Text] [Related]
4. Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation.
Sambongi Y; Iko Y; Tanabe M; Omote H; Iwamoto-Kihara A; Ueda I; Yanagida T; Wada Y; Futai M
Science; 1999 Nov; 286(5445):1722-4. PubMed ID: 10576736
[TBL] [Abstract][Full Text] [Related]
5. Effects of mutations of conserved Lys-155 and Thr-156 residues in the phosphate-binding glycine-rich sequence of the F1-ATPase beta subunit of Escherichia coli.
Omote H; Maeda M; Futai M
J Biol Chem; 1992 Oct; 267(29):20571-6. PubMed ID: 1400377
[TBL] [Abstract][Full Text] [Related]
6. Beta-gamma subunit interaction is required for catalysis by H(+)-ATPase (ATP synthase). Beta subunit amino acid replacements suppress a gamma subunit mutation having a long unrelated carboxyl terminus.
Jeanteur-De Beukelaer C; Omote H; Iwamoto-Kihara A; Maeda M; Futai M
J Biol Chem; 1995 Sep; 270(39):22850-4. PubMed ID: 7559418
[TBL] [Abstract][Full Text] [Related]
7. Rotation of a complex of the gamma subunit and c ring of Escherichia coli ATP synthase. The rotor and stator are interchangeable.
Tanabe M; Nishio K; Iko Y; Sambongi Y; Iwamoto-Kihara A; Wada Y; Futai M
J Biol Chem; 2001 May; 276(18):15269-74. PubMed ID: 11279047
[TBL] [Abstract][Full Text] [Related]
8. Determination of the partial reactions of rotational catalysis in F1-ATPase.
Scanlon JA; Al-Shawi MK; Le NP; Nakamoto RK
Biochemistry; 2007 Jul; 46(30):8785-97. PubMed ID: 17620014
[TBL] [Abstract][Full Text] [Related]
9. Catalytic control and coupling efficiency of the Escherichia coli FoF1 ATP synthase: influence of the Fo sector and epsilon subunit on the catalytic transition state.
Peskova YB; Nakamoto RK
Biochemistry; 2000 Sep; 39(38):11830-6. PubMed ID: 10995251
[TBL] [Abstract][Full Text] [Related]
10. The gamma subunit of the Escherichia coli ATP synthase. Mutations in the carboxyl-terminal region restore energy coupling to the amino-terminal mutant gamma Met-23-->Lys.
Nakamoto RK; Maeda M; Futai M
J Biol Chem; 1993 Jan; 268(2):867-72. PubMed ID: 8419364
[TBL] [Abstract][Full Text] [Related]
11. Rotation of Escherichia coli F(1)-ATPase.
Noji H; Häsler K; Junge W; Kinosita K; Yoshida M; Engelbrecht S
Biochem Biophys Res Commun; 1999 Jul; 260(3):597-9. PubMed ID: 10403811
[TBL] [Abstract][Full Text] [Related]
12. The Escherichia coli FOF1 gammaM23K uncoupling mutant has a higher K0.5 for Pi. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway.
Al-Shawi MK; Ketchum CJ; Nakamoto RK
Biochemistry; 1997 Oct; 36(42):12961-9. PubMed ID: 9335556
[TBL] [Abstract][Full Text] [Related]
13. Rotation of the epsilon subunit during catalysis by Escherichia coli FOF1-ATP synthase.
Bulygin VV; Duncan TM; Cross RL
J Biol Chem; 1998 Nov; 273(48):31765-9. PubMed ID: 9822640
[TBL] [Abstract][Full Text] [Related]
14. Subunit interactions of Escherichia coli F1-ATPase: mutants of the gamma subunits defective in interaction with the epsilon subunit isolated by the yeast two-hybrid system.
Sawada K; Watanabe H; Moritani-Otsuka C; Kanazawa H
Arch Biochem Biophys; 1997 Dec; 348(1):183-9. PubMed ID: 9390190
[TBL] [Abstract][Full Text] [Related]
15. The carboxyl-terminal helical domain of the ATP synthase γ subunit is involved in ε subunit conformation and energy coupling.
Yamakita A; Liu Y; Futai M; Iwamoto-Kihara A
Biochim Biophys Acta Bioenerg; 2019 May; 1860(5):361-368. PubMed ID: 30876890
[TBL] [Abstract][Full Text] [Related]
16. ATP synthase F(1) sector rotation. Defective torque generation in the beta subunit Ser-174 to Phe mutant and its suppression by second mutations.
Iko Y; Sambongi Y; Tanabe M; Iwamoto-Kihara A; Saito K; Ueda I; Wada Y; Futai M
J Biol Chem; 2001 Dec; 276(50):47508-11. PubMed ID: 11590180
[TBL] [Abstract][Full Text] [Related]
17. Intergenic suppression of the gammaM23K uncoupling mutation in F0F1 ATP synthase by betaGlu-381 substitutions: the role of the beta380DELSEED386 segment in energy coupling.
Ketchum CJ; Al-Shawi MK; Nakamoto RK
Biochem J; 1998 Mar; 330 ( Pt 2)(Pt 2):707-12. PubMed ID: 9480879
[TBL] [Abstract][Full Text] [Related]
18. Evidence that the NH2 terminus of vph1p, an integral subunit of the V0 sector of the yeast V-ATPase, interacts directly with the Vma1p and Vma13p subunits of the V1 sector.
Landolt-Marticorena C; Williams KM; Correa J; Chen W; Manolson MF
J Biol Chem; 2000 May; 275(20):15449-57. PubMed ID: 10747882
[TBL] [Abstract][Full Text] [Related]
19. Direct observation of the rotation of F1-ATPase.
Noji H; Yasuda R; Yoshida M; Kinosita K
Nature; 1997 Mar; 386(6622):299-302. PubMed ID: 9069291
[TBL] [Abstract][Full Text] [Related]
20. F1ATPase of Escherichia coli: a mutation (uncA401) located in the middle of the alpha subunit affects the conformation essential for F1 activity.
Kanazawa H; Noumi T; Matsuoka I; Hirata T; Futai M
Arch Biochem Biophys; 1984 Jan; 228(1):258-69. PubMed ID: 6230047
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
