Dunn SD - Search Results

1

The role of the epsilon subunit in the Escherichia coli ATP synthase. The C-terminal domain is required for efficient energy coupling.

Cipriano DJ, Dunn SD. Cipriano DJ, et al. Among authors: dunn sd. J Biol Chem. 2006 Jan 6;281(1):501-7. doi: 10.1074/jbc.M509986200. Epub 2005 Nov 2. J Biol Chem. 2006. PMID: 16267041 Free article.

2

Stochastic high-speed rotation of Escherichia coli ATP synthase F1 sector: the epsilon subunit-sensitive rotation.

Nakanishi-Matsui M, Kashiwagi S, Hosokawa H, Cipriano DJ, Dunn SD, Wada Y, Futai M. Nakanishi-Matsui M, et al. Among authors: dunn sd. J Biol Chem. 2006 Feb 17;281(7):4126-31. doi: 10.1074/jbc.M510090200. Epub 2005 Dec 12. J Biol Chem. 2006. PMID: 16352612 Free article.

3

Mutations in the dimerization domain of the b subunit from the Escherichia coli ATP synthase. Deletions disrupt function but not enzyme assembly.

Cipriano DJ, Wood KS, Bi Y, Dunn SD. Cipriano DJ, et al. Among authors: dunn sd. J Biol Chem. 2006 May 5;281(18):12408-13. doi: 10.1074/jbc.M513368200. Epub 2006 Mar 10. J Biol Chem. 2006. PMID: 16531410 Free article.

4

Tethering polypeptides through bifunctional PEG cross-linking agents to probe protein function: application to ATP synthase.

Cipriano DJ, Dunn SD. Cipriano DJ, et al. Among authors: dunn sd. Proteins. 2008 Nov 1;73(2):458-67. doi: 10.1002/prot.22079. Proteins. 2008. PMID: 18442134

5

Genetic fusions of globular proteins to the epsilon subunit of the Escherichia coli ATP synthase: Implications for in vivo rotational catalysis and epsilon subunit function.

Cipriano DJ, Bi Y, Dunn SD. Cipriano DJ, et al. Among authors: dunn sd. J Biol Chem. 2002 May 10;277(19):16782-90. doi: 10.1074/jbc.M201349200. Epub 2002 Mar 1. J Biol Chem. 2002. PMID: 11875079 Free article.

6

The b subunit of Escherichia coli ATP synthase.

Dunn SD, Revington M, Cipriano DJ, Shilton BH. Dunn SD, et al. J Bioenerg Biomembr. 2000 Aug;32(4):347-55. doi: 10.1023/a:1005571818730. J Bioenerg Biomembr. 2000. PMID: 11768296 Review.

7

Role of the asymmetry of the homodimeric b2 stator stalk in the interaction with the F1 sector of Escherichia coli ATP synthase.

Wood KS, Dunn SD. Wood KS, et al. Among authors: dunn sd. J Biol Chem. 2007 Nov 2;282(44):31920-7. doi: 10.1074/jbc.M706259200. Epub 2007 Aug 31. J Biol Chem. 2007. PMID: 17766239 Free article.

8

36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase.

Düser MG, Zarrabi N, Cipriano DJ, Ernst S, Glick GD, Dunn SD, Börsch M. Düser MG, et al. Among authors: dunn sd. EMBO J. 2009 Sep 16;28(18):2689-96. doi: 10.1038/emboj.2009.213. Epub 2009 Jul 30. EMBO J. 2009. PMID: 19644443 Free PMC article.

9

Characterization of a b2delta complex from Escherichia coli ATP synthase.

Dunn SD, Chandler J. Dunn SD, et al. J Biol Chem. 1998 Apr 10;273(15):8646-51. doi: 10.1074/jbc.273.15.8646. J Biol Chem. 1998. PMID: 9535839 Free article.

10

The dimerization domain of the b subunit of the Escherichia coli F(1)F(0)-ATPase.

Revington M, McLachlin DT, Shaw GS, Dunn SD. Revington M, et al. Among authors: dunn sd. J Biol Chem. 1999 Oct 22;274(43):31094-101. doi: 10.1074/jbc.274.43.31094. J Biol Chem. 1999. PMID: 10521510 Free article.

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