Distefano MD - Search Results

1

Purification, crystallization, and preliminary x-ray diffraction studies of the flavoenzyme mercuric ion reductase from Bacillus sp. strain RC607.

Moore MJ, Distefano MD, Walsh CT, Schiering N, Pai EF. Moore MJ, et al. Among authors: distefano md. J Biol Chem. 1989 Aug 25;264(24):14386-8. J Biol Chem. 1989. PMID: 2668287 Free article.

2

Structure of the detoxification catalyst mercuric ion reductase from Bacillus sp. strain RC607.

Schiering N, Kabsch W, Moore MJ, Distefano MD, Walsh CT, Pai EF. Schiering N, et al. Among authors: distefano md. Nature. 1991 Jul 11;352(6331):168-72. doi: 10.1038/352168a0. Nature. 1991. PMID: 2067577

3

Active site of mercuric reductase resides at the subunit interface and requires Cys135 and Cys140 from one subunit and Cys558 and Cys559 from the adjacent subunit: evidence from in vivo and in vitro heterodimer formation.

Distefano MD, Moore MJ, Walsh CT. Distefano MD, et al. Biochemistry. 1990 Mar 20;29(11):2703-13. doi: 10.1021/bi00463a013. Biochemistry. 1990. PMID: 2189495

4

Use of a site-directed triple mutant to trap intermediates: demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase.

Miller SM, Massey V, Ballou D, Williams CH Jr, Distefano MD, Moore MJ, Walsh CT. Miller SM, et al. Among authors: distefano md. Biochemistry. 1990 Mar 20;29(11):2831-41. doi: 10.1021/bi00463a028. Biochemistry. 1990. PMID: 2189497

5

Mutagenesis of the redox-active disulfide in mercuric ion reductase: catalysis by mutant enzymes restricted to flavin redox chemistry.

Distefano MD, Au KG, Walsh CT. Distefano MD, et al. Biochemistry. 1989 Feb 7;28(3):1168-83. doi: 10.1021/bi00429a035. Biochemistry. 1989. PMID: 2653436

6

Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase.

Miller SM, Moore MJ, Massey V, Williams CH Jr, Distefano MD, Ballou DP, Walsh CT. Miller SM, et al. Among authors: distefano md. Biochemistry. 1989 Feb 7;28(3):1194-205. doi: 10.1021/bi00429a037. Biochemistry. 1989. PMID: 2653437

7

Molecular basis of bacterial resistance to organomercurial and inorganic mercuric salts.

Walsh CT, Distefano MD, Moore MJ, Shewchuk LM, Verdine GL. Walsh CT, et al. Among authors: distefano md. FASEB J. 1988 Feb;2(2):124-30. doi: 10.1096/fasebj.2.2.3277886. FASEB J. 1988. PMID: 3277886 Review.

8

Mutagenesis of paired cysteine residues in the disulphide-containing flavoprotein mercuric ion reductase from mercury-resistant bacteria.

Walsh C, Distefano M, Moore M. Walsh C, et al. Biochem Soc Trans. 1988 Apr;16(2):90-1. doi: 10.1042/bst0160090. Biochem Soc Trans. 1988. PMID: 3371539 No abstract available.

9

X-ray crystallographic studies of the alanine-specific racemase from Bacillus stearothermophilus. Overproduction, crystallization, and preliminary characterization.

Neidhart DJ, Distefano MD, Tanizawa K, Soda K, Walsh CT, Petsko GA. Neidhart DJ, et al. Among authors: distefano md. J Biol Chem. 1987 Nov 15;262(32):15323-6. J Biol Chem. 1987. PMID: 3680197 Free article.

10

The chaperone protein SmgGDS interacts with small GTPases entering the prenylation pathway by recognizing the last amino acid in the CAAX motif.

Schuld NJ, Vervacke JS, Lorimer EL, Simon NC, Hauser AD, Barbieri JT, Distefano MD, Williams CL. Schuld NJ, et al. Among authors: distefano md. J Biol Chem. 2014 Mar 7;289(10):6862-6876. doi: 10.1074/jbc.M113.527192. Epub 2014 Jan 10. J Biol Chem. 2014. PMID: 24415755 Free PMC article.

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