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Derek Parsonage PhD

TitleAssistant Professor
InstitutionWake Forest School of Medicine
DepartmentBiochemistry
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    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
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    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. PMID: 31323313.
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    2. Shapiro JA, Varga JJ, Parsonage D, Walton W, Redinbo MR, Ross LJ, White EL, Bostwick R, Wuest WM, Claiborne A, Goldberg JB. Identification of Specific and Nonspecific Inhibitors of Bacillus anthracis Type III Pantothenate Kinase (PanK). ChemMedChem. 2019 01 08; 14(1):78-82. PMID: 30376607.
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    3. 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. PMID: 29884768.
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    4. 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. PMID: 29553725.
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    5. Blevins LK, Parsonage D, Oliver MB, Domzalski E, Swords WE, Alexander-Miller MA. A Novel Function for the Streptococcus pneumoniae Aminopeptidase N: Inhibition of T Cell Effector Function through Regulation of TCR Signaling. Front Immunol. 2017; 8:1610. PMID: 29230212.
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    6. Wang F, Zahid OK, Swain BE, Parsonage D, Hollis T, Harvey S, Perrino FW, Kohli RM, Taylor EW, Hall AR. Solid-State Nanopore Analysis of Diverse DNA Base Modifications Using a Modular Enzymatic Labeling Process. . 2017 11 08; 17(11):7110-7116. PMID: 28967259.
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    7. 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. PMID: 28843779.
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    8. 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. PMID: 28375740.
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    9. 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. PMID: 27594682.
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    10. 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. PMID: 26876147.
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    11. 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. PMID: 26506002.
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    12. 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. PMID: 26438558.
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    13. 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. PMID: 26209624.
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    14. Perkins A, Nelson KJ, Parsonage D, Poole LB, Karplus PA. Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling. Trends Biochem Sci. 2015 Aug; 40(8):435-45. PMID: 26067716.
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    15. 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. PMID: 25712468.
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    16. 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. PMID: 25688572.
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    17. Summitt CB, Johnson LC, Jönsson TJ, Parsonage D, Holmes RP, Lowther WT. Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria. Biochem J. 2015 Mar 01; 466(2):273-81. PMID: 25697095.
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    18. 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. PMID: 25633283.
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    19. Huhn AJ, Parsonage D, Horita DA, Torti FM, Torti SV, Hollis T. The high-molecular-weight kininogen domain 5 is an intrinsically unstructured protein and its interaction with ferritin is metal mediated. Protein Sci. 2014 Aug; 23(8):1013-22. PMID: 24810540.
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    20. Perkins A, Nelson KJ, Williams JR, Parsonage D, Poole LB, Karplus PA. The sensitive balance between the fully folded and locally unfolded conformations of a model peroxiredoxin. Biochemistry. 2013 Dec 03; 52(48):8708-21. PMID: 24175952.
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    21. Nelson KJ, Parsonage D, Karplus PA, Poole LB. Evaluating peroxiredoxin sensitivity toward inactivation by peroxide substrates. Methods Enzymol. 2013; 527:21-40. PMID: 23830624.
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    22. Debnath A, Parsonage D, Andrade RM, He C, Cobo ER, Hirata K, Chen S, García-Rivera G, Orozco E, Martínez MB, Gunatilleke SS, Barrios AM, Arkin MR, Poole LB, McKerrow JH, Reed SL. A high-throughput drug screen for Entamoeba histolytica identifies a new lead and target. Nat Med. 2012 Jun; 18(6):956-60. PMID: 22610278.
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    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). PMID: 22493033.
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    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. PMID: 21910476.
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    25. Nelson KJ, Parsonage D. Measurement of peroxiredoxin activity. Curr Protoc Toxicol. 2011 Aug; Chapter 7:Unit7.10. PMID: 21818753.
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    26. Nirudodhi S, Parsonage D, Karplus PA, Poole LB, Maier CS. Conformational studies of the robust 2-Cys peroxiredoxin Salmonella typhimurium AhpC by solution phase hydrogen/deuterium (H/D) exchange monitored by electrospray ionization mass spectrometry. Int J Mass Spectrom. 2011 Apr 30; 302(1-3):93-100. PMID: 21516234.
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    27. 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. PMID: 20799687.
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    28. 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. PMID: 20643143.
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    29. 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. PMID: 20609901.
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    30. Gaballa A, Newton GL, Antelmann H, Parsonage D, Upton H, Rawat M, Claiborne A, Fahey RC, Helmann JD. Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli. Proc Natl Acad Sci U S A. 2010 Apr 06; 107(14):6482-6. PMID: 20308541.
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    31. 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. PMID: 20304799.
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    32. 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. PMID: 19725515.
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    33. 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. PMID: 19459661.
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    34. Coffman LG, Parsonage D, D'Agostino R, Torti FM, Torti SV. Regulatory effects of ferritin on angiogenesis. Proc Natl Acad Sci U S A. 2009 Jan 13; 106(2):570-5. PMID: 19126685.
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    35. Nelson KJ, Parsonage D, Hall A, Karplus PA, Poole LB. Cysteine pK(a) values for the bacterial peroxiredoxin AhpC. Biochemistry. 2008 Dec 02; 47(48):12860-8. PMID: 18986167.
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    36. 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. PMID: 18165315.
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    37. 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. PMID: 18154320.
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    38. 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. PMID: 17323930.
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    39. 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. PMID: 16060667.
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    40. 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. PMID: 11665489.
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    41. Charrier V, Luba J, Parsonage D, Claiborne A. Limited proteolysis as a structural probe of the soluble alpha-glycerophosphate oxidase from Streptococcus sp. Biochemistry. 2000 May 02; 39(17):5035-44. PMID: 10819968.
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    42. Granok AB, Parsonage D, Ross RP, Caparon MG. The RofA binding site in Streptococcus pyogenes is utilized in multiple transcriptional pathways. J Bacteriol. 2000 Mar; 182(6):1529-40. PMID: 10692357.
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    43. 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. PMID: 10569923.
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    44. Lee MH, Nittayajarn A, Ross RP, Rothschild CB, Parsonage D, Claiborne A, Rubens CE. Characterization of Enterococcus faecalis alkaline phosphatase and use in identifying Streptococcus agalactiae secreted proteins. J Bacteriol. 1999 Sep; 181(18):5790-9. PMID: 10482522.
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    45. 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. PMID: 10074352.
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    46. 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. PMID: 9726992.
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    47. Charrier V, Buckley E, Parsonage D, Galinier A, Darbon E, Jaquinod M, Forest E, Deutscher J, Claiborne A. Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system-catalyzed phosphorylation of a single histidyl residue. J Biol Chem. 1997 May 30; 272(22):14166-74. PMID: 9162046.
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    48. 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. PMID: 8652580.
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    49. 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. PMID: 7578008.
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    50. 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. PMID: 7766608.
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    51. 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. PMID: 7711038.
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    52. 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. PMID: 7819235.
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    53. 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. PMID: 8586163.
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    54. 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. PMID: 8262333.
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    55. 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. PMID: 8428993.
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    56. 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. PMID: 1633151.
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    57. 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. PMID: 1595127.
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    58. al-Shawi MK, Parsonage D, Senior AE. Adenosine triphosphatase and nucleotide binding activity of isolated beta-subunit preparations from Escherichia coli F1F0-ATP synthase. J Biol Chem. 1990 Apr 05; 265(10):5595-601. PMID: 2156822.
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    59. 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. PMID: 2137823.
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    60. 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. PMID: 2527851.
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    61. Kironde FA, Parsonage D, Senior AE. Random mutagenesis of the gene for the beta-subunit of F1-ATPase from Escherichia coli. Biochem J. 1989 Apr 15; 259(2):421-6. PMID: 2524189.
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    62. 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. PMID: 2904440.
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    63. 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. PMID: 2895106.
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    64. Maggio MB, Parsonage D, Senior AE. A mutation in the alpha-subunit of F1-ATPase from Escherichia coli affects the binding of F1 to the membrane. J Biol Chem. 1988 Apr 05; 263(10):4619-23. PMID: 2895104.
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