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Results: 6

1.

Regulatory conformational changes of the ε subunit in single FRET-labeled FoF1-ATP synthase.

Duncan TM, Düser MG, Heitkamp T, McMillan DG, Börsch M.

Proc Soc Photo Opt Instrum Eng. 2014 Feb 28;8948:89481J.

PMID:
25076824
[PubMed]
Free PMC Article
2.

F1-ATPase of Escherichia coli: the ε- inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands.

Shah NB, Hutcheon ML, Haarer BK, Duncan TM.

J Biol Chem. 2013 Mar 29;288(13):9383-95. doi: 10.1074/jbc.M113.451583. Epub 2013 Feb 11.

PMID:
23400782
[PubMed - indexed for MEDLINE]
Free PMC Article
3.

Single molecule behavior of inhibited and active states of Escherichia coli ATP synthase F1 rotation.

Sekiya M, Hosokawa H, Nakanishi-Matsui M, Al-Shawi MK, Nakamoto RK, Futai M.

J Biol Chem. 2010 Dec 31;285(53):42058-67. doi: 10.1074/jbc.M110.176701. Epub 2010 Oct 25.

PMID:
20974856
[PubMed - indexed for MEDLINE]
Free PMC Article
4.

Crystal structure of the Mg·ADP-inhibited state of the yeast F1c10-ATP synthase.

Dautant A, Velours J, Giraud MF.

J Biol Chem. 2010 Sep 17;285(38):29502-10. doi: 10.1074/jbc.M110.124529. Epub 2010 Jul 7.

PMID:
20610387
[PubMed - indexed for MEDLINE]
Free PMC Article
5.

ATP synthase with its gamma subunit reduced to the N-terminal helix can still catalyze ATP synthesis.

Mnatsakanyan N, Hook JA, Quisenberry L, Weber J.

J Biol Chem. 2009 Sep 25;284(39):26519-25. doi: 10.1074/jbc.M109.030528. Epub 2009 Jul 27.

PMID:
19636076
[PubMed - indexed for MEDLINE]
Free PMC Article
6.

A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis.

Scanlon JA, Al-Shawi MK, Nakamoto RK.

J Biol Chem. 2008 Sep 19;283(38):26228-40. doi: 10.1074/jbc.M804858200. Epub 2008 Jul 15.

PMID:
18628203
[PubMed - indexed for MEDLINE]
Free PMC Article

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