Derek Parsonage to Catalysis
This is a "connection" page, showing publications Derek Parsonage has written about Catalysis.
Connection Strength
0.604
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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: 0.145
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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: 0.076
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Parsonage D, Youngblood DS, Sarma GN, Wood ZA, Karplus PA, Poole LB. Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. Biochemistry. 2005 Aug 09; 44(31):10583-92.
Score: 0.064
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Claiborne A, Mallett TC, Yeh JI, Luba J, Parsonage D. Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulation. Adv Protein Chem. 2001; 58:215-76.
Score: 0.047
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Claiborne A, Yeh JI, Mallett TC, Luba J, Crane EJ, Charrier V, Parsonage D. Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry. 1999 Nov 23; 38(47):15407-16.
Score: 0.043
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Perkins A, Parsonage D, Nelson KJ, Ogba OM, Cheong PH, Poole LB, Karplus PA. Peroxiredoxin Catalysis at Atomic Resolution. Structure. 2016 Oct 04; 24(10):1668-1678.
Score: 0.035
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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
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Elkhal CK, Kean KM, Parsonage D, Maenpuen S, Chaiyen P, Claiborne A, Karplus PA. Structure and proposed mechanism of L-a-glycerophosphate oxidase from Mycoplasma pneumoniae. FEBS J. 2015 Aug; 282(16):3030-42.
Score: 0.031
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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
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Hall A, Parsonage D, Poole LB, Karplus PA. Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization. J Mol Biol. 2010 Sep 10; 402(1):194-209.
Score: 0.023
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Wallen JR, Mallett TC, Boles W, Parsonage D, Furdui CM, Karplus PA, Claiborne A. Crystal structure and catalytic properties of Bacillus anthracis CoADR-RHD: implications for flavin-linked sulfur trafficking. Biochemistry. 2009 Oct 13; 48(40):9650-67.
Score: 0.022
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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
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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
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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
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Mande SS, Parsonage D, Claiborne A, Hol WG. Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg 303. Biochemistry. 1995 May 30; 34(21):6985-92.
Score: 0.008
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Claiborne A, Miller H, Parsonage D, Ross RP. Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. FASEB J. 1993 Dec; 7(15):1483-90.
Score: 0.007
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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: 0.006