| Year |
Citation |
Score |
| 2018 |
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 Non-specific Inhibitors of Bacillus anthracis Type III Pantothenate Kinase (PanK). Chemmedchem. PMID 30376607 DOI: 10.1002/Cmdc.201800652 |
0.339 |
|
| 2015 |
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. PMID 26506002 DOI: 10.1021/Acs.Biochem.5B00676 |
0.488 |
|
| 2015 |
Maenpuen S, Watthaisong P, Supon P, Sucharitakul J, Parsonage D, Karplus PA, Claiborne A, Chaiyen P. Kinetic mechanism of L-α-glycerophosphate oxidase from Mycoplasma pneumoniae. The Febs Journal. 282: 3043-59. PMID 25712468 DOI: 10.1111/Febs.13247 |
0.402 |
|
| 2015 |
Elkhal CK, Kean KM, Parsonage D, Maenpuen S, Chaiyen P, Claiborne A, Karplus PA. Structure and proposed mechanism of L-α-glycerophosphate oxidase from Mycoplasma pneumoniae. The Febs Journal. 282: 3030-42. PMID 25688572 DOI: 10.1111/Febs.13233 |
0.499 |
|
| 2013 |
Fang Z, Roberts AA, Weidman K, Sharma SV, Claiborne A, Hamilton CJ, Dos Santos PC. Cross-functionalities of Bacillus deacetylases involved in bacillithiol biosynthesis and bacillithiol-S-conjugate detoxification pathways. The Biochemical Journal. 454: 239-47. PMID 23758290 DOI: 10.1042/Bj20130415 |
0.445 |
|
| 2012 |
Wallace BD, Edwards JS, Wallen JR, Moolman WJ, van der Westhuyzen R, Strauss E, Redinbo MR, Claiborne A. Turnover-dependent covalent inactivation of Staphylococcus aureus coenzyme A-disulfide reductase by coenzyme A-mimetics: mechanistic and structural insights. Biochemistry. 51: 7699-711. PMID 22954034 DOI: 10.1021/Bi301026C |
0.55 |
|
| 2011 |
Eggers CH, Caimano MJ, Malizia RA, Kariu T, Cusack B, Desrosiers DC, Hazlett KR, Claiborne A, Pal U, Radolf JD. The coenzyme A disulphide reductase of Borrelia burgdorferi is important for rapid growth throughout the enzootic cycle and essential for infection of the mammalian host. Molecular Microbiology. 82: 679-97. PMID 21923763 DOI: 10.1111/J.1365-2958.2011.07845.X |
0.413 |
|
| 2010 |
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-α-D-glucosaminyl l-malate synthase and deacetylase functions for bacillithiol biosynthesis in Bacillus anthracis . Biochemistry. 49: 8398-414. PMID 20799687 DOI: 10.1021/Bi100698N |
0.737 |
|
| 2010 |
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. Proceedings of the National Academy of Sciences of the United States of America. 107: 6482-6. PMID 20308541 DOI: 10.1073/Pnas.1000928107 |
0.425 |
|
| 2009 |
Rowan AS, Nicely NI, Cochrane N, Wlassoff WA, Claiborne A, Hamilton CJ. Nucleoside triphosphate mimicry: a sugar triazolyl nucleoside as an ATP-competitive inhibitor of B. anthracis pantothenate kinase. Organic & Biomolecular Chemistry. 7: 4029-36. PMID 19763307 DOI: 10.1039/B909729E |
0.326 |
|
| 2009 |
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. 48: 9650-67. PMID 19725515 DOI: 10.1021/Bi900887K |
0.54 |
|
| 2009 |
Newton GL, Rawat M, La Clair JJ, Jothivasan VK, Budiarto T, Hamilton CJ, Claiborne A, Helmann JD, Fahey RC. Bacillithiol is an antioxidant thiol produced in Bacilli. Nature Chemical Biology. 5: 625-7. PMID 19578333 DOI: 10.1038/Nchembio.189 |
0.412 |
|
| 2008 |
Paige C, Reid SD, Hanna PC, Claiborne A. The type III pantothenate kinase encoded by coaX is essential for growth of Bacillus anthracis. Journal of Bacteriology. 190: 6271-5. PMID 18641144 DOI: 10.1128/Jb.00860-08 |
0.707 |
|
| 2008 |
Wallen JR, Paige C, Mallett TC, Karplus PA, Claiborne A. Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity. Biochemistry. 47: 5182-93. PMID 18399646 DOI: 10.1021/Bi8002204 |
0.739 |
|
| 2008 |
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. 47: 965-77. PMID 18154320 DOI: 10.1021/Bi701685U |
0.676 |
|
| 2007 |
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. 46: 3234-45. PMID 17323930 DOI: 10.1021/bi062299p |
0.756 |
|
| 2006 |
Mallett TC, Wallen JR, Karplus PA, Sakai H, Tsukihara T, Claiborne A. Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution. Biochemistry. 45: 11278-89. PMID 16981688 DOI: 10.1021/Bi061139A |
0.528 |
|
| 2004 |
Yeh JI, Charrier V, Paulo J, Hou L, Darbon E, Claiborne A, Hol WG, Deutscher J. Structures of enterococcal glycerol kinase in the absence and presence of glycerol: correlation of conformation to substrate binding and a mechanism of activation by phosphorylation. Biochemistry. 43: 362-73. PMID 14717590 DOI: 10.1021/Bi034258O |
0.47 |
|
| 2002 |
Finnerty CM, Charrier V, Claiborne A, Karplus PA. Crystallization and preliminary crystallographic analysis of the soluble alpha-glycerophosphate oxidase from Streptococcus sp. Acta Crystallographica. Section D, Biological Crystallography. 58: 165-6. PMID 11752801 DOI: 10.1107/S0907444901018169 |
0.379 |
|
| 2001 |
Claiborne A, Mallett TC, Yeh JI, Luba J, Parsonage D. Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulation. Advances in Protein Chemistry. 58: 215-76. PMID 11665489 DOI: 10.1016/S0065-3233(01)58006-7 |
0.414 |
|
| 2000 |
Crane EJ, Yeh JI, Luba J, Claiborne A. Analysis of the kinetic and redox properties of the NADH peroxidase R303M mutant: correlation with the crystal structure. Biochemistry. 39: 10353-10364. PMID 10956025 DOI: 10.1021/Bi000553M |
0.487 |
|
| 2000 |
Charrier V, Luba J, Parsonage D, Claiborne A. Limited Proteolysis as a Structural Probe of the Soluble α-Glycerophosphate Oxidase from Streptococcus sp.† Biochemistry. 39: 5035-5044. PMID 10819968 DOI: 10.1021/Bi992499J |
0.409 |
|
| 2000 |
Ward DE, van Der Weijden CC, van Der Merwe MJ, Westerhoff HV, Claiborne A, Snoep JL. Branched-chain alpha-keto acid catabolism via the gene products of the bkd operon in Enterococcus faecalis: a new, secreted metabolite serving as a temporary redox sink. Journal of Bacteriology. 182: 3239-46. PMID 10809705 DOI: 10.1128/Jb.182.11.3239-3246.2000 |
0.349 |
|
| 2000 |
Gibson CM, Mallett TC, Claiborne A, Caparon MG. Contribution of NADH oxidase to aerobic metabolism of Streptococcus pyogenes Journal of Bacteriology. 182: 448-455. PMID 10629192 DOI: 10.1128/Jb.182.2.448-455.2000 |
0.367 |
|
| 1999 |
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. 38: 15407-16. PMID 10569923 DOI: 10.1021/Bi992025K |
0.416 |
|
| 1999 |
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. Journal of Bacteriology. 181: 5790-9. PMID 10482522 DOI: 10.1128/Jb.181.18.5790-5799.1999 |
0.385 |
|
| 1999 |
Ward DE, Ross RP, van der Weijden CC, Snoep JL, Claiborne A. Catabolism of branched-chain alpha-keto acids in Enterococcus faecalis: the bkd gene cluster, enzymes, and metabolic route. Journal of Bacteriology. 181: 5433-42. PMID 10464218 DOI: 10.1128/Jb.181.17.5433-5442.1999 |
0.392 |
|
| 1999 |
Luba J, Charrier V, Claiborne A. Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction with pyridine nucleotides. Biochemistry. 38: 2725-2737. PMID 10052943 DOI: 10.1021/Bi9825899 |
0.517 |
|
| 1998 |
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. The Journal of Biological Chemistry. 273: 23812-22. PMID 9726992 DOI: 10.1074/Jbc.273.37.23812 |
0.383 |
|
| 1997 |
Ross RP, Claiborne A. Evidence for regulation of the NADH peroxidase gene (npr) from Enterococcus faecalis by OxyR Fems Microbiology Letters. 151: 177-183. PMID 9228751 DOI: 10.1111/J.1574-6968.1997.Tb12567.X |
0.332 |
|
| 1997 |
Crane EJ, Vervoort J, Claiborne A. 13C NMR Analysis of the Cysteine-Sulfenic Acid Redox Center of Enterococcal NADH Peroxidase† Biochemistry. 36: 8611-8618. PMID 9214307 DOI: 10.1021/Bi9707990 |
0.345 |
|
| 1997 |
Charrier V, Buckley E, Parsonage D, Galinier A, Darbon E, Jaquinod M, Forest E, Deutscher J, Claiborne A. Cloning and Sequencing of two Enterococcal glpKGenes and Regulation of the Encoded Glycerol Kinases by Phosphoenolpyruvate-dependent, Phosphotransferase System-catalyzed Phosphorylation of a Single Histidyl Residue Journal of Biological Chemistry. 272: 14166-14174. PMID 9162046 DOI: 10.1074/Jbc.272.22.14166 |
0.406 |
|
| 1996 |
Crane EJ, Parsonage D, Claiborne A. The Active-Site Histidine-10 of Enterococcal NADH Peroxidase Is Not Essential for Catalytic Activity† Biochemistry. 35: 2380-2387. PMID 8652580 DOI: 10.1021/Bi952347Y |
0.431 |
|
| 1995 |
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. 34: 435-441. PMID 7819235 DOI: 10.1021/Bi00002A007 |
0.461 |
|
| 1995 |
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. 34: 6985-92. PMID 7766608 DOI: 10.1021/Bi00021A010 |
0.51 |
|
| 1995 |
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. 34: 5180-90. PMID 7711038 DOI: 10.1021/Bi00015A032 |
0.502 |
|
| 1995 |
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. 34: 14114-14124. PMID 7578008 DOI: 10.1021/Bi00043A016 |
0.429 |
|
| 1993 |
Stehle T, Claiborne A, Schulz GE. NADH binding site and catalysis of NADH peroxidase. European Journal of Biochemistry. 211: 221-6. PMID 8425532 DOI: 10.1111/J.1432-1033.1993.Tb19889.X |
0.491 |
|
| 1993 |
Claiborne A, Miller H, Parsonage D, Ross RP. Protein‐sulfenic acid stabilization and function in enzyme catalysis and gene regulation The Faseb Journal. 7: 1483-1490. PMID 8262333 DOI: 10.1096/Fasebj.7.15.8262333 |
0.392 |
|
| 1992 |
Claiborne A, Ross RP, Parsonage D. Flavin-linked peroxide reductases: protein-sulfenic acids and the oxidative stress response Trends in Biochemical Sciences. 17: 183-186. PMID 1595127 DOI: 10.1016/0968-0004(92)90263-9 |
0.37 |
|
| 1991 |
Ross RP, Claiborne A. Cloning, sequence and overexpression of NADH peroxidase from Streptococcus faecalis 10C1. Structural relationship with the flavoprotein disulfide reductases. Journal of Molecular Biology. 221: 857-871. PMID 1719212 DOI: 10.1016/0022-2836(91)80180-3 |
0.443 |
|
| 1991 |
Stehle T, Ahmed S, Claiborne A, Schulz G. Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16Åresolution Journal of Molecular Biology. 221: 1325-1344. DOI: 10.1016/0022-2836(91)90936-Z |
0.477 |
|
| 1990 |
Stehle T, Ahmed SA, Claiborne A, Schulz GE. The structure of NADH peroxidase from Streptococcus faecalis at 3.3 A resolution. Febs Letters. 267: 186-8. PMID 2116319 DOI: 10.1016/0014-5793(90)80921-5 |
0.506 |
|
| 1979 |
Claiborne A, Fridovich I. Chemical and enzymatic intermediates in the peroxidation of o-dianisidine by horseradish peroxidase. 2. Evidence for a substrate radical--enzyme complex and its reaction with nucleophiles. Biochemistry. 18: 2329-35. PMID 444459 DOI: 10.1021/Bi00578A030 |
0.354 |
|
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