Pinitglang S - Search Results

1

Improvement in hydrolytic antibody activity by change in haptenic structure from phosphate to phosphonate with retention of a common leaving-group determinant: evidence for the 'flexibility' hypothesis.

Gul S, Sonkaria S, Pinitglang S, Florez-Alvarez J, Hussain S, Thomas EW, Ostler EL, Gallacher G, Resmini M, Brocklehurst K. Gul S, et al. Among authors: pinitglang s. Biochem J. 2003 Dec 15;376(Pt 3):813-21. doi: 10.1042/BJ20030716. Biochem J. 2003. PMID: 12946271 Free PMC article.

2

Variation in the pH-dependent pre-steady-state and steady-state kinetic characteristics of cysteine-proteinase mechanism: evidence for electrostatic modulation of catalytic-site function by the neighbouring carboxylate anion.

Hussain S, Pinitglang S, Bailey TS, Reid JD, Noble MA, Resmini M, Thomas EW, Greaves RB, Verma CS, Brocklehurst K. Hussain S, et al. Among authors: pinitglang s. Biochem J. 2003 Jun 15;372(Pt 3):735-46. doi: 10.1042/BJ20030177. Biochem J. 2003. PMID: 12643810 Free PMC article.

3

Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulations.

Reid JD, Hussain S, Sreedharan SK, Bailey TS, Pinitglang S, Thomas EW, Verma CS, Brocklehurst K. Reid JD, et al. Among authors: pinitglang s. Biochem J. 2001 Jul 15;357(Pt 2):343-52. doi: 10.1042/0264-6021:3570343. Biochem J. 2001. PMID: 11439083 Free PMC article.

4

Existence of the Cys-His ion-pair state of cysteine proteinases may be an insufficient condition for catalytic competence.

Pinitglang S, Patel M, Thomas EW, Brocklehurst K. Pinitglang S, et al. Biochem Soc Trans. 1994 May;22(2):215S. doi: 10.1042/bst022215s. Biochem Soc Trans. 1994. PMID: 7958277 No abstract available.

5

Studies on the enhancement of the reactivity of the (Cys-25)-S-/(His159)-Im+H ion-pair of papain by deprotonation across pKa 4.

Pinitglang S, Noble M, Verma C, Thomas EW, Brocklehurst K. Pinitglang S, et al. Biochem Soc Trans. 1996 Aug;24(3):468S. doi: 10.1042/bst024468s. Biochem Soc Trans. 1996. PMID: 8879012 No abstract available.

6

Actinidin and chymopapain B provide variation in the common electrostatic environment of Glu50 in papain and caricain.

Reid JD, Pinitglang S, Topham CM, Verma C, Thomas EW, Brocklehurst K. Reid JD, et al. Among authors: pinitglang s. Biochem Soc Trans. 1997 Feb;25(1):89S. doi: 10.1042/bst025089s. Biochem Soc Trans. 1997. PMID: 9056987 No abstract available.

7

Investigation of the electrostatic field of the papain active centre by using monoprotonated and diprotonated pyridyl (Py) disulphides as reactivity probes.

Gul S, Clarke A, Field B, Thomas MP, Willenbrock F, Pinitglang S, Verma C, Thomas EW, Brocklehurst K. Gul S, et al. Among authors: pinitglang s. Biochem Soc Trans. 1997 Feb;25(1):91S. doi: 10.1042/bst025091s. Biochem Soc Trans. 1997. PMID: 9056989 No abstract available.

8

Sensitivities of transition state geometries to P1-P2 binding in reactions of papain and actinidin.

Gul S, Pinitglang S, Thomas EW, Verma C, Brocklehurst K. Gul S, et al. Among authors: pinitglang s. Biochem Soc Trans. 1998 May;26(2):S171. doi: 10.1042/bst026s171. Biochem Soc Trans. 1998. PMID: 9649846 No abstract available.

9

Characterization of the electrostatic perturbation of a catalytic site (Cys)-S-/(His)-Im+H ion-pair in one type of serine proteinase architecture by kinetic and computational studies on chemically mutated subtilisin variants.

Plou FJ, Kowlessur D, Malthouse JP, Mellor GW, Hartshorn MJ, Pinitglang S, Patel H, Topham CM, Thomas EW, Verma C, Brocklehurst K. Plou FJ, et al. Among authors: pinitglang s. J Mol Biol. 1996 Apr 19;257(5):1088-111. doi: 10.1006/jmbi.1996.0225. J Mol Biol. 1996. PMID: 8632470

10

Effects of the quality of the P2-S2 hydrophobic contacts on the catalytic activities of papain, caricain and ficin and their generation by electrostatic switches.

Pinitglang S, Patel M, Noble M, Sreedharan SK, Verma C, Thomas EW, Brocklehurst K. Pinitglang S, et al. Biochem Soc Trans. 1997 Feb;25(1):88S. doi: 10.1042/bst025088s. Biochem Soc Trans. 1997. PMID: 9056986 No abstract available.

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