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Connection

Derek Parsonage to Oxidation-Reduction

This is a "connection" page, showing publications Derek Parsonage has written about Oxidation-Reduction.
Connection Strength

1.446
  1. Randall LM, Dalla Rizza J, Parsonage D, Santos J, Mehl RA, Lowther WT, Poole LB, Denicola A. Unraveling the effects of peroxiredoxin 2 nitration; role of C-terminal tyrosine 193. Free Radic Biol Med. 2019 09; 141:492-501.
    View in: PubMed
    Score: 0.161
  2. Parsonage D, Sheng F, Hirata K, Debnath A, McKerrow JH, Reed SL, Abagyan R, Poole LB, Podust LM. X-ray structures of thioredoxin and thioredoxin reductase from Entamoeba histolytica and prevailing hypothesis of the mechanism of Auranofin action. J Struct Biol. 2016 May; 194(2):180-90.
    View in: PubMed
    Score: 0.127
  3. 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.
    View in: PubMed
    Score: 0.119
  4. Parsonage D, Newton GL, Holder RC, Wallace BD, Paige C, Hamilton CJ, Dos Santos PC, Redinbo MR, Reid SD, Claiborne A. Characterization of the N-acetyl-a-D-glucosaminyl l-malate synthase and deacetylase functions for bacillithiol biosynthesis in Bacillus anthracis . Biochemistry. 2010 Sep 28; 49(38):8398-414.
    View in: PubMed
    Score: 0.088
  5. Parsonage D, Reeves SA, Karplus PA, Poole LB. Engineering of fluorescent reporters into redox domains to monitor electron transfers. Methods Enzymol. 2010; 474:1-21.
    View in: PubMed
    Score: 0.086
  6. Parsonage D, Desrosiers DC, Hazlett KR, Sun Y, Nelson KJ, Cox DL, Radolf JD, Poole LB. Broad specificity AhpC-like peroxiredoxin and its thioredoxin reductant in the sparse antioxidant defense system of Treponema pallidum. Proc Natl Acad Sci U S A. 2010 Apr 06; 107(14):6240-5.
    View in: PubMed
    Score: 0.084
  7. 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.
    View in: PubMed
    Score: 0.072
  8. 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.
    View in: PubMed
    Score: 0.061
  9. 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.
    View in: PubMed
    Score: 0.045
  10. 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.
    View in: PubMed
    Score: 0.041
  11. Bolduc JA, Nelson KJ, Haynes AC, Lee J, Reisz JA, Graff AH, Clodfelter JE, Parsonage D, Poole LB, Furdui CM, Lowther WT. Novel hyperoxidation resistance motifs in 2-Cys peroxiredoxins. J Biol Chem. 2018 07 27; 293(30):11901-11912.
    View in: PubMed
    Score: 0.037
  12. 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.
    View in: PubMed
    Score: 0.037
  13. Keyes JD, Parsonage D, Yammani RD, Rogers LC, Kesty C, Furdui CM, Nelson KJ, Poole LB. Endogenous, regulatory cysteine sulfenylation of ERK kinases in response to proliferative signals. Free Radic Biol Med. 2017 11; 112:534-543.
    View in: PubMed
    Score: 0.035
  14. 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.
    View in: PubMed
    Score: 0.034
  15. Wallen JR, Mallett TC, Okuno T, Parsonage D, Sakai H, Tsukihara T, Claiborne A. Structural Analysis of Streptococcus pyogenes NADH Oxidase: Conformational Dynamics Involved in Formation of the C(4a)-Peroxyflavin Intermediate. Biochemistry. 2015 Nov 17; 54(45):6815-29.
    View in: PubMed
    Score: 0.031
  16. Buchko GW, Perkins A, Parsonage D, Poole LB, Karplus PA. Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics. Biomol NMR Assign. 2016 Apr; 10(1):57-61.
    View in: PubMed
    Score: 0.031
  17. Langston PK, Yang M, Bierbach U, Parsonage D, Poole LB, Price MJ, Grayson JM. Au-ACRAMTU-PEt3 Alters Redox Balance To Inhibit T Cell Proliferation and Function. J Immunol. 2015 Sep 01; 195(5):1984-94.
    View in: PubMed
    Score: 0.031
  18. 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.
    View in: PubMed
    Score: 0.030
  19. 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.
    View in: PubMed
    Score: 0.030
  20. 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.
    View in: PubMed
    Score: 0.030
  21. Nelson KJ, Parsonage D, Karplus PA, Poole LB. Evaluating peroxiredoxin sensitivity toward inactivation by peroxide substrates. Methods Enzymol. 2013; 527:21-40.
    View in: PubMed
    Score: 0.026
  22. Claiborne A, Ross RP, Parsonage D. Flavin-linked peroxide reductases: protein-sulfenic acids and the oxidative stress response. Trends Biochem Sci. 1992 May; 17(5):183-6.
    View in: PubMed
    Score: 0.024
  23. Cho SH, Parsonage D, Thurston C, Dutton RJ, Poole LB, Collet JF, Beckwith J. A new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelope. mBio. 2012; 3(2).
    View in: PubMed
    Score: 0.024
  24. 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.
    View in: PubMed
    Score: 0.023
  25. 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.
    View in: PubMed
    Score: 0.022
  26. 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.
    View in: PubMed
    Score: 0.020
  27. Hall A, Parsonage D, Horita D, Karplus PA, Poole LB, Barbar E. Redox-dependent dynamics of a dual thioredoxin fold protein: evolution of specialized folds. Biochemistry. 2009 Jun 30; 48(25):5984-93.
    View in: PubMed
    Score: 0.020
  28. 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.
    View in: PubMed
    Score: 0.018
  29. Nicely NI, Parsonage D, Paige C, Newton GL, Fahey RC, Leonardi R, Jackowski S, Mallett TC, Claiborne A. Structure of the type III pantothenate kinase from Bacillus anthracis at 2.0 A resolution: implications for coenzyme A-dependent redox biology. Biochemistry. 2007 Mar 20; 46(11):3234-45.
    View in: PubMed
    Score: 0.017
  30. Mallett TC, Parsonage D, Claiborne A. Equilibrium analyses of the active-site asymmetry in enterococcal NADH oxidase: role of the cysteine-sulfenic acid redox center. Biochemistry. 1999 Mar 09; 38(10):3000-11.
    View in: PubMed
    Score: 0.010
  31. 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.
    View in: PubMed
    Score: 0.008
  32. 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.
    View in: PubMed
    Score: 0.008
  33. Miller H, Mande SS, Parsonage D, Sarfaty SH, Hol WG, Claiborne A. An L40C mutation converts the cysteine-sulfenic acid redox center in enterococcal NADH peroxidase to a disulfide. Biochemistry. 1995 Apr 18; 34(15):5180-90.
    View in: PubMed
    Score: 0.008
  34. Claiborne A, Buckley E, Parsonage D, Ross RP, Ward DP. Molecular analysis of enterococcal loci involved in novel catabolic pathways. Dev Biol Stand. 1995; 85:129-33.
    View in: PubMed
    Score: 0.007
Connection Strength

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