David SS - Search Results

1

Formation of a Schiff base intermediate is not required for the adenine glycosylase activity of Escherichia coli MutY.

Williams SD, David SS. Williams SD, et al. Among authors: david ss. Biochemistry. 1999 Nov 23;38(47):15417-24. doi: 10.1021/bi992013z. Biochemistry. 1999. PMID: 10569924

2

A substrate recognition role for the [4Fe-4S]2+ cluster of the DNA repair glycosylase MutY.

Porello SL, Cannon MJ, David SS. Porello SL, et al. Among authors: david ss. Biochemistry. 1998 May 5;37(18):6465-75. doi: 10.1021/bi972433t. Biochemistry. 1998. PMID: 9572864

3

Single-turnover and pre-steady-state kinetics of the reaction of the adenine glycosylase MutY with mismatch-containing DNA substrates.

Porello SL, Leyes AE, David SS. Porello SL, et al. Among authors: david ss. Biochemistry. 1998 Oct 20;37(42):14756-64. doi: 10.1021/bi981594+. Biochemistry. 1998. PMID: 9778350

4

Evidence that MutY is a monofunctional glycosylase capable of forming a covalent Schiff base intermediate with substrate DNA.

Williams SD, David SS. Williams SD, et al. Among authors: david ss. Nucleic Acids Res. 1998 Nov 15;26(22):5123-33. doi: 10.1093/nar/26.22.5123. Nucleic Acids Res. 1998. PMID: 9801309 Free PMC article.

5

Site-directed mutagenesis of the cysteine ligands to the [4Fe-4S] cluster of Escherichia coli MutY.

Golinelli MP, Chmiel NH, David SS. Golinelli MP, et al. Among authors: david ss. Biochemistry. 1999 Jun 1;38(22):6997-7007. doi: 10.1021/bi982300n. Biochemistry. 1999. PMID: 10353811

6

Substrate recognition by Escherichia coli MutY using substrate analogs.

Chepanoske CL, Porello SL, Fujiwara T, Sugiyama H, David SS. Chepanoske CL, et al. Among authors: david ss. Nucleic Acids Res. 1999 Aug 1;27(15):3197-204. doi: 10.1093/nar/27.15.3197. Nucleic Acids Res. 1999. PMID: 10454618 Free PMC article.

7

Recognition of the nonpolar base 4-methylindole in DNA by the DNA repair adenine glycosylase MutY.

Chepanoske CL, Langelier CR, Chmiel NH, David SS. Chepanoske CL, et al. Among authors: david ss. Org Lett. 2000 May 4;2(9):1341-4. doi: 10.1021/ol005831o. Org Lett. 2000. PMID: 10810743

8

Positively charged residues within the iron-sulfur cluster loop of E. coli MutY participate in damage recognition and removal.

Chepanoske CL, Golinelli MP, Williams SD, David SS. Chepanoske CL, et al. Among authors: david ss. Arch Biochem Biophys. 2000 Aug 1;380(1):11-9. doi: 10.1006/abbi.2000.1890. Arch Biochem Biophys. 2000. PMID: 10900127

9

A single engineered point mutation in the adenine glycosylase MutY confers bifunctional glycosylase/AP lyase activity.

Williams SD, David SS. Williams SD, et al. Among authors: david ss. Biochemistry. 2000 Aug 22;39(33):10098-109. doi: 10.1021/bi0004652. Biochemistry. 2000. PMID: 10955998

10

Removal of hydantoin products of 8-oxoguanine oxidation by the Escherichia coli DNA repair enzyme, FPG.

Leipold MD, Muller JG, Burrows CJ, David SS. Leipold MD, et al. Among authors: david ss. Biochemistry. 2000 Dec 5;39(48):14984-92. doi: 10.1021/bi0017982. Biochemistry. 2000. PMID: 11101315

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