Ollis DL - Search Results

1

Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, et al. Ollis DL, et al. Protein Eng. 1992 Apr;5(3):197-211. doi: 10.1093/protein/5.3.197. Protein Eng. 1992. PMID: 1409539

2

Substrate-induced activation of dienelactone hydrolase: an enzyme with a naturally occurring Cys-His-Asp triad.

Cheah E, Austin C, Ashley GW, Ollis D. Cheah E, et al. Protein Eng. 1993 Aug;6(6):575-83. doi: 10.1093/protein/6.6.575. Protein Eng. 1993. PMID: 8234228

3

Catalysis by dienelactone hydrolase: a variation on the protease mechanism.

Cheah E, Ashley GW, Gary J, Ollis D. Cheah E, et al. Proteins. 1993 May;16(1):64-78. doi: 10.1002/prot.340160108. Proteins. 1993. PMID: 8497485

4

A theoretical study of substrate-induced activation of dienelactone hydrolase.

Beveridge AJ, Ollis DL. Beveridge AJ, et al. Among authors: ollis dl. Protein Eng. 1995 Feb;8(2):135-42. doi: 10.1093/protein/8.2.135. Protein Eng. 1995. PMID: 7630883

5

A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly.

Newcomb RD, Campbell PM, Ollis DL, Cheah E, Russell RJ, Oakeshott JG. Newcomb RD, et al. Among authors: ollis dl. Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7464-8. doi: 10.1073/pnas.94.14.7464. Proc Natl Acad Sci U S A. 1997. PMID: 9207114 Free PMC article.

6

GlnK, a PII-homologue: structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition.

Xu Y, Cheah E, Carr PD, van Heeswijk WC, Westerhoff HV, Vasudevan SG, Ollis DL. Xu Y, et al. Among authors: ollis dl. J Mol Biol. 1998 Sep 11;282(1):149-65. doi: 10.1006/jmbi.1998.1979. J Mol Biol. 1998. PMID: 9733647

7

Structure of the Escherichia coli signal transducing protein PII.

Cheah E, Carr PD, Suffolk PM, Vasudevan SG, Dixon NE, Ollis DL. Cheah E, et al. Among authors: ollis dl. Structure. 1994 Oct 15;2(10):981-90. doi: 10.1016/s0969-2126(94)00100-6. Structure. 1994. PMID: 7866749

8

Compensatory stabilizing role of surface mutations during the directed evolution of dienelactone hydrolase for enhanced activity.

Porter JL, Collyer CA, Ollis DL. Porter JL, et al. Among authors: ollis dl. Protein J. 2015 Feb;34(1):82-9. doi: 10.1007/s10930-015-9600-7. Protein J. 2015. PMID: 25600287

9

Crystallization and preliminary X-ray analysis of IND, an enzyme with indole oxygenase activity from Chromobacterium violaceum.

Cheah E, MacPherson K, Quiggin D, Keese P, Ollis DL. Cheah E, et al. Among authors: ollis dl. Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):657-8. doi: 10.1107/s0907444997018994. Acta Crystallogr D Biol Crystallogr. 1998. PMID: 9761866

10

X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A.

Carr PD, Cheah E, Suffolk PM, Vasudevan SG, Dixon NE, Ollis DL. Carr PD, et al. Among authors: ollis dl. Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):93-104. doi: 10.1107/S0907444995007293. Acta Crystallogr D Biol Crystallogr. 1996. PMID: 15299730

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