Derek Parsonage to Kinetics
This is a "connection" page, showing publications Derek Parsonage has written about Kinetics.
Connection Strength
0.527
-
Parsonage D, Nelson KJ, Ferrer-Sueta G, Alley S, Karplus PA, Furdui CM, Poole LB. Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC. Biochemistry. 2015 Feb 24; 54(7):1567-75.
Score: 0.123
-
Parsonage D, Karplus PA, Poole LB. Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin. Proc Natl Acad Sci U S A. 2008 Jun 17; 105(24):8209-14.
Score: 0.075
-
Parsonage D, Luba J, Mallett TC, Claiborne A. The soluble alpha-glycerophosphate oxidase from Enterococcus casseliflavus. Sequence homology with the membrane-associated dehydrogenase and kinetic analysis of the recombinant enzyme. J Biol Chem. 1998 Sep 11; 273(37):23812-22.
Score: 0.039
-
Portillo-Ledesma S, Randall LM, Parsonage D, Dalla Rizza J, Karplus PA, Poole LB, Denicola A, Ferrer-Sueta G. Differential Kinetics of Two-Cysteine Peroxiredoxin Disulfide Formation Reveal a Novel Model for Peroxide Sensing. Biochemistry. 2018 06 19; 57(24):3416-3424.
Score: 0.038
-
Nelson KJ, Perkins A, Van Swearingen AED, Hartman S, Brereton AE, Parsonage D, Salsbury FR, Karplus PA, Poole LB. Experimentally Dissecting the Origins of Peroxiredoxin Catalysis. Antioxid Redox Signal. 2018 Mar 01; 28(7):521-536.
Score: 0.036
-
Maenpuen S, Watthaisong P, Supon P, Sucharitakul J, Parsonage D, Karplus PA, Claiborne A, Chaiyen P. Kinetic mechanism of L-a-glycerophosphate oxidase from Mycoplasma pneumoniae. FEBS J. 2015 Aug; 282(16):3043-59.
Score: 0.031
-
Parsonage D, Claiborne A. Analysis of the kinetic and redox properties of NADH peroxidase C42S and C42A mutants lacking the cysteine-sulfenic acid redox center. Biochemistry. 1995 Jan 17; 34(2):435-41.
Score: 0.031
-
Parsonage D, Miller H, Ross RP, Claiborne A. Purification and analysis of streptococcal NADH peroxidase expressed in Escherichia coli. J Biol Chem. 1993 Feb 15; 268(5):3161-7.
Score: 0.027
-
Nelson KJ, Parsonage D, Karplus PA, Poole LB. Evaluating peroxiredoxin sensitivity toward inactivation by peroxide substrates. Methods Enzymol. 2013; 527:21-40.
Score: 0.027
-
Reeves SA, Parsonage D, Nelson KJ, Poole LB. Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin. Biochemistry. 2011 Oct 18; 50(41):8970-81.
Score: 0.024
-
Parsonage D, Al-Shawi MK, Senior AE. Directed mutations of the strongly conserved lysine 155 in the catalytic nucleotide-binding domain of beta-subunit of F1-ATPase from Escherichia coli. J Biol Chem. 1988 Apr 05; 263(10):4740-4.
Score: 0.019
-
Colussi T, Parsonage D, Boles W, Matsuoka T, Mallett TC, Karplus PA, Claiborne A. Structure of alpha-glycerophosphate oxidase from Streptococcus sp.: a template for the mitochondrial alpha-glycerophosphate dehydrogenase. Biochemistry. 2008 Jan 22; 47(3):965-77.
Score: 0.019
-
Crane EJ, Parsonage D, Claiborne A. The active-site histidine-10 of enterococcal NADH peroxidase is not essential for catalytic activity. Biochemistry. 1996 Feb 20; 35(7):2380-7.
Score: 0.008
-
Crane EJ, Parsonage D, Poole LB, Claiborne A. Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme forms. Biochemistry. 1995 Oct 31; 34(43):14114-24.
Score: 0.008
-
Day AG, Parsonage D, Ebel S, Brown T, Fersht AR. Barnase has subsites that give rise to large rate enhancements. Biochemistry. 1992 Jul 21; 31(28):6390-5.
Score: 0.006
-
al-Shawi MK, Parsonage D, Senior AE. Thermodynamic analyses of the catalytic pathway of F1-ATPase from Escherichia coli. Implications regarding the nature of energy coupling by F1-ATPases. J Biol Chem. 1990 Mar 15; 265(8):4402-10.
Score: 0.005
-
al-Shawi MK, Parsonage D, Senior AE. Kinetic characterization of the unisite catalytic pathway of seven beta-subunit mutant F1-ATPases from Escherichia coli. J Biol Chem. 1989 Sep 15; 264(26):15376-83.
Score: 0.005
-
Al-Shawi MK, Parsonage D, Senior AE. Directed mutagenesis of the strongly conserved aspartate 242 in the beta-subunit of Escherichia coli proton-ATPase. J Biol Chem. 1988 Dec 25; 263(36):19633-9.
Score: 0.005