Dunn SD - Search Results

1

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.

2

The "second stalk" of Escherichia coli ATP synthase: structure of the isolated dimerization domain.

Del Rizzo PA, Bi Y, Dunn SD, Shilton BH. Del Rizzo PA, et al. Among authors: dunn sd. Biochemistry. 2002 May 28;41(21):6875-84. doi: 10.1021/bi025736i. Biochemistry. 2002. PMID: 12022893

3

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.

4

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.

5

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.

6

ATP synthase b subunit dimerization domain: a right-handed coiled coil with offset helices.

Del Rizzo PA, Bi Y, Dunn SD. Del Rizzo PA, et al. Among authors: dunn sd. J Mol Biol. 2006 Dec 8;364(4):735-46. doi: 10.1016/j.jmb.2006.09.028. Epub 2006 Sep 14. J Mol Biol. 2006. PMID: 17028022

7

Probing the functional tolerance of the b subunit of Escherichia coli ATP synthase for sequence manipulation through a chimera approach.

Bi Y, Watts JC, Bamford PK, Briere LK, Dunn SD. Bi Y, et al. Among authors: dunn sd. Biochim Biophys Acta. 2008 Jul-Aug;1777(7-8):583-91. doi: 10.1016/j.bbabio.2008.03.004. Epub 2008 Mar 16. Biochim Biophys Acta. 2008. PMID: 18395001 Free article.

8

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

9

The proton-translocating a subunit of F0F1-ATP synthase is allocated asymmetrically to the peripheral stalk.

Düser MG, Bi Y, Zarrabi N, Dunn SD, Börsch M. Düser MG, et al. Among authors: dunn sd. J Biol Chem. 2008 Nov 28;283(48):33602-10. doi: 10.1074/jbc.M805170200. Epub 2008 Sep 11. J Biol Chem. 2008. PMID: 18786919 Free PMC article.

10

A re-examination of the structural and functional consequences of mutation of alanine-128 of the b subunit of Escherichia coli ATP synthase to aspartic acid.

Dunn SD, Bi Y, Revington M. Dunn SD, et al. Biochim Biophys Acta. 2000 Aug 15;1459(2-3):521-7. doi: 10.1016/s0005-2728(00)00192-4. Biochim Biophys Acta. 2000. PMID: 11004471 Free article.

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