Year |
Citation |
Score |
2019 |
Bashiri G, Grove TL, Hegde SS, Lagautriere T, Gerfen GJ, Almo SC, Squire CJ, Blanchard JS, Baker EN. The active site of the branched-chain amino acid biosynthesis enzyme dihydroxyacid dehydratase contains a 2Fe-2S cluster. The Journal of Biological Chemistry. PMID 31315931 DOI: 10.1074/Jbc.Ra119.009498 |
0.365 |
|
2019 |
Almo SC, Grove TL, Bashiri G, Hegde ss, Lagautriere tl, Gerfen G, Squire CJ, Blanchard js, Baker EN. Dihydroxyacid dehydratase (IlvD) from Mycobacterium tuberculosis is an essential biosynthetic enzyme with an Fe2-S2 cluster at its active site Journal of Biological Chemistry. DOI: 10.2210/Pdb6Ovt/Pdb |
0.361 |
|
2018 |
Favrot L, Amorim Franco T, Blanchard JS. Biochemical Characterization of the Mycobacterium smegmatis Threonine Deaminase. Biochemistry. PMID 30226377 DOI: 10.1021/Acs.Biochem.8B00871 |
0.403 |
|
2017 |
Franco TMA, Blanchard JS. Bacterial Branched-Chain Amino Acid Biosynthesis: Structures, Mechanisms and Drugability. Biochemistry. PMID 28977745 DOI: 10.1021/Acs.Biochem.7B00849 |
0.386 |
|
2017 |
Chow C, Hegde SS, Blanchard JS. Mechanistic Characterization of Escherichia coli L-Aspartate Oxidase from Kinetic Isotope Effects. Biochemistry. PMID 28700220 DOI: 10.1021/Acs.Biochem.7B00307 |
0.804 |
|
2017 |
Franco TM, Favrot L, Vergnolle O, Blanchard JS. Mechanism-Based Inhibition of the Mycobacterium tuberculosis Branched-chain Aminotransferase by D- and L-cycloserine. Acs Chemical Biology. PMID 28272868 DOI: 10.1021/Acschembio.7B00142 |
0.432 |
|
2016 |
Amorim Franco TM, Hegde SS, Blanchard JS. The chemical mechanism of the branched-chain aminotransferase IlvE from Mycobacterium tuberculosis. Biochemistry. PMID 27780341 DOI: 10.1021/Acs.Biochem.6B00928 |
0.489 |
|
2016 |
Vergnolle O, Xu H, Tufariello JM, Favrot L, Malek AA, Jacobs WR, Blanchard JS. Post-Translational Acetylation of MbtA Modulates Mycobacterial Siderophore Biosynthesis. The Journal of Biological Chemistry. PMID 27566542 DOI: 10.1074/Jbc.M116.744532 |
0.431 |
|
2016 |
Noy T, Vergnolle O, Hartman TE, Rhee KY, Jacobs WR, Berney M, Blanchard JS. Central Role of Pyruvate Kinase in Carbon Co-Catabolism of Mycobacterium tuberculosis. The Journal of Biological Chemistry. PMID 26858255 DOI: 10.1074/Jbc.M115.707430 |
0.33 |
|
2016 |
Favrot L, Blanchard JS, Vergnolle O. Bacterial GCN5-related N-acetyltransferases: From Resistance to Regulation. Biochemistry. PMID 26818562 DOI: 10.1021/Acs.Biochem.5B01269 |
0.372 |
|
2015 |
Kurz SG, Hazra S, Bethel CR, Romagnoli C, Caselli E, Prati F, Blanchard JS, Bonomo RA. Inhibiting the β-Lactamase of Mycobacterium tuberculosis (Mtb) with Novel Boronic Acid Transition-State Inhibitors (BATSIs). Acs Infectious Diseases. 1: 234-42. PMID 27622739 DOI: 10.1021/Acsinfecdis.5B00003 |
0.375 |
|
2015 |
Hazra S, Kurz SG, Wolff K, Nguyen L, Bonomo RA, Blanchard JS. Kinetic and Structural Characterization of the Interaction of the 6-methylidene penem 2 with the β-Lactamase from Mycobacterium tuberculosis. Biochemistry. PMID 26237118 DOI: 10.1021/Acs.Biochem.5B00698 |
0.395 |
|
2014 |
Hazra S, Xu H, Blanchard JS. Tebipenem, a new carbapenem antibiotic, is a slow substrate that inhibits the β-lactamase from Mycobacterium tuberculosis. Biochemistry. 53: 3671-8. PMID 24846409 DOI: 10.1021/Bi500339J |
0.489 |
|
2014 |
Noy T, Xu H, Blanchard JS. Acetylation of acetyl-CoA synthetase from Mycobacterium tuberculosis leads to specific inactivation of the adenylation reaction. Archives of Biochemistry and Biophysics. 550: 42-9. PMID 24751484 DOI: 10.1016/J.Abb.2014.04.004 |
0.497 |
|
2013 |
Quartararo CE, Hadi T, Cahill SM, Blanchard JS. Solvent isotope-induced equilibrium perturbation for isocitrate lyase. Biochemistry. 52: 9286-93. PMID 24261638 DOI: 10.1021/Bi4013319 |
0.792 |
|
2013 |
Hadi T, Hazra S, Tanner ME, Blanchard JS. Structure of MurNAc 6-phosphate hydrolase (MurQ) from Haemophilus influenzae with a bound inhibitor. Biochemistry. 52: 9358-66. PMID 24251551 DOI: 10.1021/Bi4010446 |
0.459 |
|
2013 |
Wolfson-Stofko B, Hadi T, Blanchard JS. Kinetic and mechanistic characterization of the glyceraldehyde 3-phosphate dehydrogenase from Mycobacterium tuberculosis Archives of Biochemistry and Biophysics. 540: 53-61. PMID 24161676 DOI: 10.1016/J.Abb.2013.10.007 |
0.818 |
|
2013 |
Kurz SG, Wolff KA, Hazra S, Bethel CR, Hujer AM, Smith KM, Xu Y, Tremblay LW, Blanchard JS, Nguyen L, Bonomo RA. Can inhibitor-resistant substitutions in the Mycobacterium tuberculosis β-Lactamase BlaC lead to clavulanate resistance?: a biochemical rationale for the use of β-lactam-β-lactamase inhibitor combinations. Antimicrobial Agents and Chemotherapy. 57: 6085-96. PMID 24060876 DOI: 10.1128/Aac.01253-13 |
0.354 |
|
2013 |
Vergnolle O, Xu H, Blanchard JS. Mechanism and regulation of mycobactin fatty acyl-AMP ligase FadD33 Journal of Biological Chemistry. 288: 28116-28125. PMID 23935107 DOI: 10.1074/Jbc.M113.495549 |
0.46 |
|
2013 |
Serrano H, Blanchard JS. Kinetic and isotopic characterization of l -proline dehydrogenase from mycobacterium tuberculosis Biochemistry. 52: 5009-5015. PMID 23834473 DOI: 10.1021/Bi400338F |
0.443 |
|
2013 |
Chow C, Xu H, Blanchard JS. Kinetic characterization of hydrolysis of nitrocefin, cefoxitin, and meropenem by β-lactamase from mycobacterium tuberculosis Biochemistry. 52: 4097-4104. PMID 23672214 DOI: 10.1021/Bi400177Y |
0.798 |
|
2013 |
Quartararo CE, Hazra S, Hadi T, Blanchard JS. Structural, kinetic and chemical mechanism of isocitrate dehydrogenase-1 from Mycobacterium tuberculosis. Biochemistry. 52: 1765-75. PMID 23409873 DOI: 10.1021/Bi400037W |
0.811 |
|
2013 |
Hazra S, Blanchard JS. 178 Targeting “Beta lactamase-C” in development of novel anti-tuberculosis therapeutics Journal of Biomolecular Structure and Dynamics. 31: 115-115. DOI: 10.1080/07391102.2013.786420 |
0.341 |
|
2012 |
Czekster CM, Blanchard JS. One substrate, five products: Reactions catalyzed by the dihydroneopterin aldolase from Mycobacterium tuberculosis Journal of the American Chemical Society. 134: 19758-19771. PMID 23150985 DOI: 10.1021/Ja308350F |
0.786 |
|
2012 |
Xu H, Hazra S, Blanchard JS. NXL104 irreversibly inhibits the β-lactamase from Mycobacterium tuberculosis. Biochemistry. 51: 4551-7. PMID 22587688 DOI: 10.1021/Bi300508R |
0.422 |
|
2011 |
Czekster CM, Vandemeulebroucke A, Blanchard JS. Two parallel pathways in the kinetic sequence of the dihydrofolate reductase from mycobacterium tuberculosis Biochemistry. 50: 7045-7056. PMID 21744813 DOI: 10.1021/Bi200608N |
0.76 |
|
2011 |
Quartararo CE, Blanchard JS. Kinetic and chemical mechanism of malate synthase from mycobacterium tuberculosis Biochemistry. 50: 6879-6887. PMID 21728344 DOI: 10.1021/Bi2007299 |
0.833 |
|
2011 |
Xu H, Hegde SS, Blanchard JS. Reversible acetylation and inactivation of Mycobacterium tuberculosis acetyl-CoA synthetase is dependent on cAMP Biochemistry. 50: 5883-5892. PMID 21627103 DOI: 10.1021/Bi200156T |
0.4 |
|
2011 |
Vetting MW, Hegde SS, Wang M, Jacoby GA, Hooper DC, Blanchard JS. Structure of QnrB1, a plasmid-mediated fluoroquinolone resistance factor Journal of Biological Chemistry. 286: 25265-25273. PMID 21597116 DOI: 10.1074/Jbc.M111.226936 |
0.319 |
|
2011 |
Czekster CM, Vandemeulebroucke A, Blanchard JS. Kinetic and chemical mechanism of the dihydrofolate reductase from Mycobacterium tuberculosis Biochemistry. 50: 367-375. PMID 21138249 DOI: 10.1021/Bi1016843 |
0.771 |
|
2011 |
Hegde SS, Vetting MW, Mitchenall LA, Maxwell A, Blanchard JS. Structural and biochemical analysis of the pentapeptide repeat protein EfsQnr, a potent DNA gyrase inhibitor Antimicrobial Agents and Chemotherapy. 55: 110-117. PMID 20937785 DOI: 10.1128/Aac.01158-10 |
0.348 |
|
2010 |
Tremblay LW, Xu H, Blanchard JS. Structures of the Michaelis complex (1.2 Å) and the covalent acyl intermediate (2.0 Å) of cefamandole bound in the active sites of the mycobacterium tuberculosis β-lactamase K73A and E166A mutants Biochemistry. 49: 9685-9687. PMID 20961112 DOI: 10.1021/Bi1015088 |
0.388 |
|
2010 |
Seiner DR, Hegde SS, Blanchard JS. Kinetics and inhibition of nicotinamidase from mycobacterium tuberculosis Biochemistry. 49: 9613-9619. PMID 20879713 DOI: 10.1021/Bi1011157 |
0.492 |
|
2010 |
Vetting MW, Hegde SS, Blanchard JS. The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase Nature Chemical Biology. 6: 797-799. PMID 20852636 DOI: 10.1038/Nchembio.440 |
0.473 |
|
2010 |
Frantom PA, Coward JK, Blanchard JS. UDP-(5F)-GlcNAc acts as a slow-binding inhibitor of MshA, a retaining glycosyltransferase. Journal of the American Chemical Society. 132: 6626-7. PMID 20411981 DOI: 10.1021/Ja101231A |
0.756 |
|
2010 |
Sikora AL, Wilson DJ, Aldrich CC, Blanchard JS. Kinetic and inhibition studies of dihydroxybenzoate-AMP ligase from Escherichia coli. Biochemistry. 49: 3648-57. PMID 20359185 DOI: 10.1021/Bi100350C |
0.812 |
|
2010 |
Tremblay LW, Fan F, Blanchard JS. Biochemical and structural characterization of mycobacterium tuberculosis β-lactamase with the carbapenems ertapenem and doripenem Biochemistry. 49: 3766-3773. PMID 20353175 DOI: 10.1021/Bi100232Q |
0.47 |
|
2010 |
Frantom PA, Blanchard JS. Bisubstrate analog inhibitors Comprehensive Natural Products Ii: Chemistry and Biology. 8: 689-717. |
0.647 |
|
2009 |
Tremblay LW, Blanchard JS. The 1.9 Å structure of the branched-chain amino-acid transaminase (IlvE) from Mycobacterium tuberculosis Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 65: 1071-1077. PMID 19923721 DOI: 10.1107/S1744309109036690 |
0.429 |
|
2009 |
Stoll VS, Blanchard JS. Buffers: principles and practice. Methods in Enzymology. 463: 43-56. PMID 19892166 DOI: 10.1016/S0076-6879(09)63006-8 |
0.399 |
|
2009 |
Sikora AL, Cahill SM, Blanchard JS. Enterobactin synthetase-catalyzed formation of P(1),P(3)-diadenosine-5'-tetraphosphate. Biochemistry. 48: 10827-9. PMID 19852513 DOI: 10.1021/Bi901680M |
0.764 |
|
2009 |
Fan F, Vetting MW, Frantom PA, Blanchard JS. Structures and mechanisms of the mycothiol biosynthetic enzymes. Current Opinion in Chemical Biology. 13: 451-9. PMID 19699138 DOI: 10.1016/J.Cbpa.2009.07.018 |
0.749 |
|
2009 |
Frantom PA, Zhang HM, Emmett MR, Marshall AG, Blanchard JS. Mapping of the allosteric network in the regulation of alpha-isopropylmalate synthase from Mycobacterium tuberculosis by the feedback inhibitor L-leucine: solution-phase H/D exchange monitored by FT-ICR mass spectrometry. Biochemistry. 48: 7457-64. PMID 19606873 DOI: 10.1021/Bi900851Q |
0.724 |
|
2009 |
Fan F, Blanchard JS. Toward the catalytic mechanism of a cysteine ligase (MshC) from Mycobacterium smegmatis: An enzyme involved in the biosynthetic pathway of mycothiol Biochemistry. 48: 7150-7159. PMID 19505149 DOI: 10.1021/Bi900457X |
0.526 |
|
2009 |
Reich-Slotky R, Kabbash CA, Della-Latta P, Blanchard JS, Feinmark SJ, Freeman S, Kaplan G, Shuman HA, Silverstein SC. Gemfibrozil inhibits Legionella pneumophila and Mycobacterium tuberculosis enoyl coenzyme A reductases and blocks intracellular growth of these bacteria in macrophages. Journal of Bacteriology. 191: 5262-71. PMID 19429621 DOI: 10.1128/Jb.00175-09 |
0.35 |
|
2009 |
Hugonnet JE, Tremblay LW, Boshoff HI, Barry CE, Blanchard JS. Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis Science. 323: 1215-1218. PMID 19251630 DOI: 10.1126/Science.1167498 |
0.332 |
|
2009 |
De Carvalho LPS, Frantom PA, Argyrou A, Blanchard JS. Kinetic evidence for interdomain communication in the allosteric regulation of α-isopropylmalate synthase from Mycobacterium tuberculosis Biochemistry. 48: 1996-2004. PMID 19166329 DOI: 10.1021/Bi801707T |
0.748 |
|
2009 |
Fan F, Vetting MW, Frantom PA, Blanchard JS. Structures and mechanisms of the mycothiol biosynthetic enzymes Current Opinion in Chemical Biology. 13: 444-452. DOI: 10.1016/j.cbpa.2009.07.018 |
0.719 |
|
2008 |
Tremblay LW, Fan F, Vetting MW, Blanchard JS. The 1.6 Å crystal structure of Mycobacterium smegmatis MshC: The penultimate enzyme in the mycothiol biosynthetic pathway Biochemistry. 47: 13326-13335. PMID 19053270 DOI: 10.1021/Bi801708F |
0.479 |
|
2008 |
Vetting MW, Errey JC, Blanchard JS. Rv0802c from Mycobacterium tuberculosis: The first structure of a succinyltransferase with the GNAT fold Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 64: 978-985. PMID 18997321 DOI: 10.1107/S1744309108031679 |
0.72 |
|
2008 |
Khrapunov S, Cheng H, Hegde S, Blanchard J, Brenowitz M. Solution structure and refolding of the Mycobacterium tuberculosis pentapeptide repeat protein MfpA Journal of Biological Chemistry. 283: 36290-36299. PMID 18977756 DOI: 10.1074/Jbc.M804702200 |
0.342 |
|
2008 |
Sikora AL, Frankel BA, Blanchard JS. Kinetic and chemical mechanism of arylamine N-acetyltransferase from Mycobacterium tuberculosis Biochemistry. 47: 10781-10789. PMID 18795795 DOI: 10.1021/Bi800398C |
0.824 |
|
2008 |
Vetting MW, Chi HP, Hegde SS, Jacoby GA, Hooper DC, Blanchard JS. Mechanistic and structural analysis of aminoglycoside N-acetyltransferase AAC(6′)-Ib and its bifunctional, fluoroquinolone-active AAC(6′)-Ib-cr variant Biochemistry. 47: 9825-9835. PMID 18710261 DOI: 10.1021/Bi800664X |
0.324 |
|
2008 |
Vetting MW, Bareich DC, Yu M, Blanchard JS. Crystal structure of RimI from Salmonella typhimurium LT2, the GNAT responsible for Nα-acetylation of ribosomal protein S18 Protein Science. 17: 1781-1790. PMID 18596200 DOI: 10.1110/Ps.035899.108 |
0.606 |
|
2008 |
Frankel BA, Blanchard JS. Mechanistic analysis of Mycobacterium tuberculosis Rv1347c, a lysine Nε-acyltransferase involved in mycobactin biosynthesis Archives of Biochemistry and Biophysics. 477: 259-266. PMID 18539130 DOI: 10.1016/J.Abb.2008.05.013 |
0.478 |
|
2008 |
Magalhães ML, Argyrou A, Cahill SM, Blanchard JS. Kinetic and mechanistic analysis of the Escherichia coli ribD-encoded bifunctional deaminase-reductase involved in riboflavin biosynthesis. Biochemistry. 47: 6499-507. PMID 18500821 DOI: 10.1021/Bi800264G |
0.45 |
|
2008 |
Tremblay LW, Hugonnet JE, Blanchard JS. Structure of the covalent adduct formed between Mycobacterium tuberculosis β-lactamase and clavulanate Biochemistry. 47: 5312-5316. PMID 18422342 DOI: 10.1021/Bi8001055 |
0.354 |
|
2008 |
Vetting MW, Frantom PA, Blanchard JS. Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: Substrate-assisted catalysis Journal of Biological Chemistry. 283: 15834-15844. PMID 18390549 DOI: 10.1074/Jbc.M801017200 |
0.727 |
|
2008 |
Williams L, Fan F, Blanchard JS, Raushel FM. Positional isotope exchange analysis of the Mycobacterium smegmatis cysteine ligase (MshC). Biochemistry. 47: 4843-50. PMID 18373355 DOI: 10.1021/Bi800327U |
0.655 |
|
2008 |
Magalhães MLB, Vetting MW, Gao F, Freiburger L, Auclair K, Blanchard JS. Kinetic and structural analysis of bisubstrate inhibition of the Salmonella enterica aminoglycoside 6′-N-acetyltransferase Biochemistry. 47: 579-584. PMID 18095712 DOI: 10.1021/Bi701957C |
0.368 |
|
2007 |
Hugonnet JE, Blanchard JS. Irreversible inhibition of the Mycobacterium tuberculosis β-lactamase by clavulanate Biochemistry. 46: 11998-12004. PMID 17915954 DOI: 10.1021/Bi701506H |
0.43 |
|
2007 |
Pillai B, Cherney M, Diaper CM, Sutherland A, Blanchard JS, Vederas JC, James MN. Dynamics of catalysis revealed from the crystal structures of mutants of diaminopimelate epimerase. Biochemical and Biophysical Research Communications. 363: 547-53. PMID 17889830 DOI: 10.1016/J.Bbrc.2007.09.012 |
0.469 |
|
2007 |
Fan F, Luxenburger A, Painter GF, Blanchard JS. Steady-state and pre-steady-state kinetic analysis of Mycobacterium smegmatis cysteine ligase (MshC) Biochemistry. 46: 11421-11429. PMID 17848100 DOI: 10.1021/Bi7011492 |
0.39 |
|
2007 |
Argyrou A, Vetting MW, Blanchard JS. New insight into the mechanism of action of and resistance to isoniazid: Interaction of Mycobacterium tuberculosis enoyl-ACP reductase with INH-NADP Journal of the American Chemical Society. 129: 9582-9583. PMID 17636923 DOI: 10.1021/Ja073160K |
0.434 |
|
2007 |
Hegde SS, Chandler J, Vetting MW, Yu M, Blanchard JS. Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase. Biochemistry. 46: 7187-95. PMID 17516632 DOI: 10.1021/Bi700256Z |
0.638 |
|
2006 |
Yu M, Magalhães MLB, Cook PF, Blanchard JS. Bisubstrate inhibition: Theory and application to N-acetyltransferases Biochemistry. 45: 14788-14794. PMID 17144672 DOI: 10.1021/Bi061621T |
0.616 |
|
2006 |
Yu M, De Carvalho LPS, Sun G, Blanchard JS. Activity-based substrate profiling for Gcn5-related N-acetyltransferases: The use of chloroacetyl-coenzyme A to identify protein substrates Journal of the American Chemical Society. 128: 15356-15357. PMID 17131985 DOI: 10.1021/Ja066298W |
0.639 |
|
2006 |
Argyrou A, Jin L, Siconilfi-Baez L, Angeletti RH, Blanchard JS. Proteome-wide profiling of isoniazid targets in Mycobacterium tuberculosis Biochemistry. 45: 13947-13953. PMID 17115689 DOI: 10.1021/bi061874m |
0.359 |
|
2006 |
Silva RG, De Carvalho LPS, Blanchard JS, Santos DS, Basso LA. Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein (ACP) reductase: Kinetic and chemical mechanisms Biochemistry. 45: 13064-13073. PMID 17059223 DOI: 10.1021/Bi0611210 |
0.67 |
|
2006 |
Wing C, Errey JC, Mukhopadhyay B, Blanchard JS, Field RA. Expression and initial characterization of WbbI, a putative d-Galf:α-d-Glc β-1,6-galactofuranosyltransferase from Escherichia coli K-12 Organic and Biomolecular Chemistry. 4: 3945-3950. PMID 17047874 DOI: 10.1039/B609455D |
0.753 |
|
2006 |
De Carvalho LPS, Blanchard JS. Kinetic and chemical mechanism of α-isopropylmalate synthase from Mycobacterium tuberculosis Biochemistry. 45: 8988-8999. PMID 16846242 DOI: 10.1021/Bi0606602 |
0.392 |
|
2006 |
Pillai B, Cherney MM, Diaper CM, Sutherland A, Blanchard JS, Vederas JC, James MN. Structural insights into stereochemical inversion by diaminopimelate epimerase: an antibacterial drug target. Proceedings of the National Academy of Sciences of the United States of America. 103: 8668-73. PMID 16723397 DOI: 10.1073/Pnas.0602537103 |
0.436 |
|
2006 |
de Carvalho LPS, Blanchard JS. Kinetic analysis of the effects of monovalent cations and divalent metals on the activity of Mycobacterium tuberculosis α-isopropylmalate synthase Archives of Biochemistry and Biophysics. 451: 141-148. PMID 16684501 DOI: 10.1016/J.Abb.2006.03.030 |
0.395 |
|
2006 |
Argyrou A, Vetting MW, Aladegbami B, Blanchard JS. Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid Nature Structural and Molecular Biology. 13: 408-413. PMID 16648861 DOI: 10.1038/Nsmb1089 |
0.402 |
|
2006 |
Errey JC, Blanchard JS. Functional annotation and kinetic characterization of PhnO from Salmonella enterica Biochemistry. 45: 3033-3039. PMID 16503658 DOI: 10.1021/bi052297p |
0.689 |
|
2006 |
Vetting MW, Yu M, Rendle PM, Blanchard JS. The substrate-induced conformational change of mycobacterium tuberculosis mycothiol synthase Journal of Biological Chemistry. 281: 2795-2802. PMID 16326705 DOI: 10.1074/Jbc.M510798200 |
0.634 |
|
2005 |
Magalhaes MLB, Blanchard JS. The kinetic mechanism of AAC(3)-IV aminoglycoside acetyltransferase from Escherichia coli Biochemistry. 44: 16275-16283. PMID 16331988 DOI: 10.1021/Bi051777D |
0.496 |
|
2005 |
Diaper CM, Sutherland A, Pillai B, James MN, Semchuk P, Blanchard JS, Vederas JC. The stereoselective synthesis of aziridine analogues of diaminopimelic acid (DAP) and their interaction with dap epimerase. Organic & Biomolecular Chemistry. 3: 4402-11. PMID 16327902 DOI: 10.1039/B513409A |
0.376 |
|
2005 |
De Carvalho LPS, Argyrou A, Blanchard JS. Slow-onset feedback inhibition: Inhibition of Mycobacterium tuberculosis α-isopropylmalate synthase by L-leucine Journal of the American Chemical Society. 127: 10004-10005. PMID 16011356 DOI: 10.1021/Ja052513H |
0.432 |
|
2005 |
Hegde SS, Vetting MW, Roderick SL, Mitchenall LA, Maxwell A, Takiff HE, Blanchard JS. Biochemistry: A fluoroquinolone resistance protein from Mycobacterium tuberculosis that mimics DNA Science. 308: 1480-1483. PMID 15933203 DOI: 10.1126/Science.1110699 |
0.31 |
|
2005 |
Errey JC, Blanchard JS. Functional characterization of a novel ArgA from Mycobacterium tuberculosis Journal of Bacteriology. 187: 3039-3044. PMID 15838030 DOI: 10.1128/Jb.187.9.3039-3044.2005 |
0.716 |
|
2005 |
Vetting MW, De Carvalho LPS, Roderick SL, Blanchard JS. A novel dimeric structure of the RimL Nα-acetyltransferase from Salmonella typhimurium Journal of Biological Chemistry. 280: 22108-22114. PMID 15817456 DOI: 10.1074/Jbc.M502401200 |
0.4 |
|
2005 |
Vetting MW, Luiz LP, Yu M, Hegde SS, Magnet S, Roderick SL, Blanchard JS. Structure and functions of the GNAT superfamily of acetyltransferases Archives of Biochemistry and Biophysics. 433: 212-226. PMID 15581578 DOI: 10.1016/J.Abb.2004.09.003 |
0.597 |
|
2004 |
Argyrou A, Vetting MW, Blanchard JS. Characterization of a new member of the flavoprotein disulfide reductase family of enzymes from Mycobacterium tuberculosis Journal of Biological Chemistry. 279: 52694-52702. PMID 15456792 DOI: 10.1074/Jbc.M410704200 |
0.534 |
|
2004 |
Argyrou A, Blanchard JS. Flavoprotein Disulfide Reductases: Advances in Chemistry and Function Progress in Nucleic Acid Research and Molecular Biology. 78: 89-142. PMID 15210329 DOI: 10.1016/S0079-6603(04)78003-4 |
0.458 |
|
2004 |
Zheng R, Dam TK, Brewer CF, Blanchard JS. Active site residues in Mycobacterium tuberculosis pantothenate synthetase required in the formation and stabilization of the adenylate intermediate Biochemistry. 43: 7171-7178. PMID 15170354 DOI: 10.1021/Bi049676N |
0.67 |
|
2004 |
Vetting MW, Magnet S, Nieves E, Roderick SL, Blanchard JS. A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones Chemistry and Biology. 11: 565-573. PMID 15123251 DOI: 10.1016/J.Chembiol.2004.03.017 |
0.384 |
|
2004 |
Argyrou A, Blanchard JS. Kinetic and Chemical Mechanism of Mycobacterium tuberculosis 1-Deoxy-D-xylulose-5-phosphate Isomeroreductase Biochemistry. 43: 4375-4384. PMID 15065882 DOI: 10.1021/Bi049974K |
0.469 |
|
2004 |
Magnet S, Blanchard JS. Mechanistic and Kinetic Study of the ATP-Dependent DNA Ligase of Neisseria meningitidis Biochemistry. 43: 710-717. PMID 14730975 DOI: 10.1021/Bi0355387 |
0.402 |
|
2003 |
Zheng R, Blanchard JS. Substrate specificity and kinetic isotope effect analysis of the Eschericia coli ketopantoate reductase Biochemistry. 42: 11289-11296. PMID 14503879 DOI: 10.1021/Bi030101K |
0.629 |
|
2003 |
Cirilli M, Zheng R, Scapin G, Blanchard JS. The three-dimensional structures of the Mycobacterium tuberculosis dihydrodipicolinate reductase-NADH-2,6-PDC and -NADPH-2,6-PDC complexes. Structural and mutagenic analysis of relaxed nucleotide specificity Biochemistry. 42: 10644-10650. PMID 12962488 DOI: 10.1021/Bi030044V |
0.675 |
|
2003 |
Vetting MW, Roderick SL, Yu M, Blanchard JS. Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases Protein Science. 12: 1954-1959. PMID 12930994 DOI: 10.1110/Ps.03153703 |
0.643 |
|
2003 |
Vogt RN, Steenkamp DJ, Zheng R, Blanchard JS. The metabolism of nitrosothiols in the mycobacteria: Identification and characterization of S-nitrosomycothiol reductase Biochemical Journal. 374: 657-665. PMID 12809551 DOI: 10.1042/Bj20030642 |
0.653 |
|
2003 |
Vetting M, Roderick SL, Hegde S, Magnet S, Blanchard JS. What can structure tell us about in vivo function? The case of aminoglycoside-resistance genes. Biochemical Society Transactions. 31: 520-2. PMID 12773148 DOI: 10.1042/Bst0310520 |
0.391 |
|
2003 |
Williams L, Zheng R, Blanchard JS, Raushel FM. Positional isotope exchange analysis of the pantothenate synthetase reaction. Biochemistry. 42: 5108-13. PMID 12718554 DOI: 10.1021/Bi0340853 |
0.709 |
|
2003 |
Magnet S, Smith TA, Zheng R, Nordmann P, Blanchard JS. Aminoglycoside resistance resulting from tight drug binding to an altered aminoglycoside acetyltransferase. Antimicrobial Agents and Chemotherapy. 47: 1577-83. PMID 12709325 DOI: 10.1128/Aac.47.5.1577-1583.2003 |
0.586 |
|
2003 |
Hegde SS, Blanchard JS. Kinetic and mechanistic characterization of recombinant Lactobacillus viridescens FemX (UDP-N-acetylmuramoyl pentapeptide-lysine N6-alanyltransferase). The Journal of Biological Chemistry. 278: 22861-7. PMID 12679335 DOI: 10.1074/Jbc.M301565200 |
0.515 |
|
2003 |
Blanchard JS. Resisting bacterial drug resistance. Chemistry & Biology. 10: 104-6. PMID 12618181 DOI: 10.1016/S1074-5521(03)00033-4 |
0.317 |
|
2003 |
Argyrou A, Sun G, Palfey BA, Blanchard JS. Catalysis of diaphorase reactions by Mycobacterium tuberculosis lipoamide dehydrogenase occurs at the EH4 level. Biochemistry. 42: 2218-28. PMID 12590611 DOI: 10.1021/Bi020654F |
0.395 |
|
2003 |
Sugantino M, Zheng R, Yu M, Blanchard JS. Mycobacterium tuberculosis ketopantoate hydroxymethyltransferase: tetrahydrofolate-independent hydroxymethyltransferase and enolization reactions with alpha-keto acids. Biochemistry. 42: 191-9. PMID 12515554 DOI: 10.1021/Bi020516Q |
0.698 |
|
2002 |
Schroeder EK, de Souza N, Santos DS, Blanchard JS, Basso LA. Drugs that inhibit mycolic acid biosynthesis in Mycobacterium tuberculosis. Current Pharmaceutical Biotechnology. 3: 197-225. PMID 12164478 DOI: 10.2174/1389201023378328 |
0.537 |
|
2002 |
Vetting MW, Hegde SS, Javid-Majd F, Blanchard JS, Roderick SL. Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates. Nature Structural Biology. 9: 653-8. PMID 12161746 DOI: 10.1038/Nsb830 |
0.428 |
|
2002 |
Hegde SS, Dam TK, Brewer CF, Blanchard JS. Thermodynamics of aminoglycoside and acyl-coenzyme A binding to the Salmonella enterica AAC(6')-Iy aminoglycoside N-acetyltransferase. Biochemistry. 41: 7519-27. PMID 12044186 DOI: 10.1021/Bi020190L |
0.398 |
|
2002 |
Beaman TW, Vogel KW, Drueckhammer DG, Blanchard JS, Roderick SL. Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase. Protein Science : a Publication of the Protein Society. 11: 974-9. PMID 11910040 DOI: 10.1110/Ps.4310102 |
0.424 |
|
2001 |
Zheng R, Blanchard JS. Steady-state and pre-steady-state kinetic analysis of Mycobacterium tuberculosis pantothenate synthetase. Biochemistry. 40: 12904-12. PMID 11669627 DOI: 10.1021/Bi011522+ |
0.638 |
|
2001 |
Hegde SS, Javid-Majd F, Blanchard JS. Overexpression and mechanistic analysis of chromosomally encoded aminoglycoside 2'-N-acetyltransferase (AAC(2')-Ic) from Mycobacterium tuberculosis. The Journal of Biological Chemistry. 276: 45876-81. PMID 11590162 DOI: 10.1074/Jbc.M108810200 |
0.447 |
|
2001 |
Argyrou A, Blanchard JS. Mycobacterium tuberculosis lipoamide dehydrogenase is encoded by Rv0462 and not by the lpdA or lpdB genes. Biochemistry. 40: 11353-63. PMID 11560483 DOI: 10.1021/Bi010575O |
0.421 |
|
2001 |
Shi W, Basso LA, Santos DS, Tyler PC, Furneaux RH, Blanchard JS, Almo SC, Schramm VL. Structures of purine nucleoside phosphorylase from Mycobacterium tuberculosis in complexes with immucillin-H and its pieces. Biochemistry. 40: 8204-15. PMID 11444966 DOI: 10.1021/Bi010585P |
0.611 |
|
2001 |
Basso LA, Santos DS, Shi W, Furneaux RH, Tyler PC, Schramm VL, Blanchard JS. Purine nucleoside phosphorylase from Mycobacterium tuberculosis. Analysis of inhibition by a transition-state analogue and dissection by parts. Biochemistry. 40: 8196-203. PMID 11444965 DOI: 10.1021/Bi010584X |
0.593 |
|
2001 |
Paiva AM, Vanderwall DE, Blanchard JS, Kozarich JW, Williamson JM, Kelly TM. Inhibitors of dihydrodipicolinate reductase, a key enzyme of the diaminopimelate pathway of Mycobacterium tuberculosis. Biochimica Et Biophysica Acta. 1545: 67-77. PMID 11342032 DOI: 10.1016/S0167-4838(00)00262-4 |
0.42 |
|
2001 |
Patel MP, Blanchard JS. Mycobacterium tuberculosis mycothione reductase: pH dependence of the kinetic parameters and kinetic isotope effects. Biochemistry. 40: 5119-26. PMID 11318633 DOI: 10.1021/Bi0029144 |
0.489 |
|
2001 |
Magnet S, Lambert T, Courvalin P, Blanchard JS. Kinetic and mutagenic characterization of the chromosomally encoded Salmonella enterica AAC(6')-Iy aminoglycoside N-acetyltransferase. Biochemistry. 40: 3700-9. PMID 11297438 DOI: 10.1021/Bi002736E |
0.508 |
|
2000 |
Zheng R, Blanchard JS. Identification of active site residues in E. coli ketopantoate reductase by mutagenesis and chemical rescue. Biochemistry. 39: 16244-51. PMID 11123955 DOI: 10.1021/Bi002134V |
0.651 |
|
2000 |
Cirilli M, Scapin G, Sutherland A, Vederas JC, Blanchard JS. The three-dimensional structure of the ternary complex of Corynebacterium glutamicum diaminopimelate dehydrogenase-NADPH-L-2-amino-6-methylene-pimelate. Protein Science : a Publication of the Protein Society. 9: 2034-7. PMID 11106178 DOI: 10.1110/Ps.9.10.2034 |
0.437 |
|
2000 |
Caplan JF, Zheng R, Blanchard JS, Vederas JC. Vinylogous amide analogues of diaminopimelic acid (DAP) as inhibitors of enzymes involved in bacterial lysine biosynthesis. Organic Letters. 2: 3857-60. PMID 11101437 DOI: 10.1021/Ol000271E |
0.635 |
|
2000 |
Barlow JN, Blanchard JS. Enzymatic synthesis of UDP-(3-deoxy-3-fluoro)-D-galactose and UDP-(2-deoxy-2-fluoro)-D-galactose and substrate activity with UDP-galactopyranose mutase. Carbohydrate Research. 328: 473-80. PMID 11093703 DOI: 10.1016/S0008-6215(00)00135-X |
0.391 |
|
2000 |
Brunhuber NM, Thoden JB, Blanchard JS, Vanhooke JL. Rhodococcus L-phenylalanine dehydrogenase: kinetics, mechanism, and structural basis for catalytic specificity. Biochemistry. 39: 9174-87. PMID 10924111 DOI: 10.1021/Bi000494C |
0.493 |
|
2000 |
Born TL, Franklin M, Blanchard JS. Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase. Biochemistry. 39: 8556-64. PMID 10913262 DOI: 10.1021/Bi000462P |
0.5 |
|
2000 |
Zheng R, Blanchard JS. Kinetic and mechanistic analysis of the E. coli panE-encoded ketopantoate reductase. Biochemistry. 39: 3708-17. PMID 10736170 DOI: 10.1021/Bi992676G |
0.652 |
|
2000 |
Javid-Majd F, Blanchard JS. Mechanistic analysis of the argE-encoded N-acetylornithine deacetylase. Biochemistry. 39: 1285-93. PMID 10684608 DOI: 10.1021/Bi992177F |
0.478 |
|
1999 |
Born TL, Blanchard JS. Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Escherichia coli metA-encoded homoserine transsuccinylase. Biochemistry. 38: 14416-23. PMID 10572016 DOI: 10.1021/Bi991710O |
0.525 |
|
1999 |
Patel MP, Blanchard JS. Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase. Biochemistry. 38: 11827-33. PMID 10512639 DOI: 10.1021/Bi991025H |
0.533 |
|
1999 |
Born TL, Blanchard JS. Structure/function studies on enzymes in the diaminopimelate pathway of bacterial cell wall biosynthesis. Current Opinion in Chemical Biology. 3: 607-13. PMID 10508663 DOI: 10.1016/S1367-5931(99)00016-2 |
0.459 |
|
1999 |
Koo CW, Blanchard JS. Chemical mechanism of Haemophilus influenzae diaminopimelate epimerase. Biochemistry. 38: 4416-22. PMID 10194362 DOI: 10.1021/Bi982911F |
0.399 |
|
1999 |
Ledwidge R, Blanchard JS. The dual biosynthetic capability of N-acetylornithine aminotransferase in arginine and lysine biosynthesis. Biochemistry. 38: 3019-24. PMID 10074354 DOI: 10.1021/Bi982574A |
0.417 |
|
1999 |
Vanhooke JL, Thoden JB, Brunhuber NM, Blanchard JS, Holden HM. Phenylalanine dehydrogenase from Rhodococcus sp. M4: high-resolution X-ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism. Biochemistry. 38: 2326-39. PMID 10029526 DOI: 10.1021/Bi982244Q |
0.454 |
|
1998 |
Basso LA, Blanchard JS. Resistance to antitubercular drugs. Advances in Experimental Medicine and Biology. 456: 115-44. PMID 10549366 DOI: 10.1007/978-1-4615-4897-3_7 |
0.552 |
|
1998 |
Cirilli M, Zheng R, Scapin G, Blanchard JS. Structural symmetry: the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase. Biochemistry. 37: 16452-8. PMID 9843410 DOI: 10.1021/Bi982138O |
0.598 |
|
1998 |
Wang PF, Marcinkeviciene J, Williams CH, Blanchard JS. Thioredoxin reductase-thioredoxin fusion enzyme from Mycobacterium leprae: comparison with the separately expressed thioredoxin reductase. Biochemistry. 37: 16378-89. PMID 9819230 DOI: 10.1021/Bi980754E |
0.475 |
|
1998 |
Patel MP, Marcinkeviciene J, Blanchard JS. Enterococcus faecalis glutathione reductase: purification, characterization and expression under normal and hyperbaric O2 conditions. Fems Microbiology Letters. 166: 155-63. PMID 9741094 DOI: 10.1111/J.1574-6968.1998.Tb13197.X |
0.458 |
|
1998 |
Basso LA, Zheng R, Musser JM, Jacobs WR, Blanchard JS. Mechanisms of isoniazid resistance in Mycobacterium tuberculosis: enzymatic characterization of enoyl reductase mutants identified in isoniazid-resistant clinical isolates. The Journal of Infectious Diseases. 178: 769-75. PMID 9728546 DOI: 10.1086/515362 |
0.724 |
|
1998 |
Born TL, Zheng R, Blanchard JS. Hydrolysis of N-succinyl-L,L-diaminopimelic acid by the Haemophilus influenzae dapE-encoded desuccinylase: metal activation, solvent isotope effects, and kinetic mechanism. Biochemistry. 37: 10478-87. PMID 9671518 DOI: 10.1021/Bi9806807 |
0.612 |
|
1998 |
Beaman TW, Blanchard JS, Roderick SL. The conformational change and active site structure of tetrahydrodipicolinate N-succinyltransferase. Biochemistry. 37: 10363-9. PMID 9671504 DOI: 10.1021/Bi980759B |
0.46 |
|
1998 |
Scapin G, Blanchard JS. Enzymology of bacterial lysine biosynthesis. Advances in Enzymology and Related Areas of Molecular Biology. 72: 279-324. PMID 9559056 DOI: 10.1002/9780470123188.Ch8 |
0.362 |
|
1998 |
Scapin G, Cirilli M, Reddy SG, Gao Y, Vederas JC, Blanchard JS. Substrate and inhibitor binding sites in Corynebacterium glutamicum diaminopimelate dehydrogenase. Biochemistry. 37: 3278-85. PMID 9521647 DOI: 10.1021/Bi9727949 |
0.497 |
|
1998 |
Wang F, Scapin G, Blanchard JS, Angeletti RH. Substrate binding and conformational changes of Clostridium glutamicum diaminopimelate dehydrogenase revealed by hydrogen/deuterium exchange and electrospray mass spectrometry Protein Science. 7: 293-299. PMID 9521104 DOI: 10.1002/Pro.5560070208 |
0.421 |
|
1997 |
Scapin G, Reddy SG, Zheng R, Blanchard JS. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate. Biochemistry. 36: 15081-8. PMID 9398235 DOI: 10.1021/Bi9719915 |
0.653 |
|
1997 |
Marcinkeviciene J, Blanchard JS. Catalytic properties of lipoamide dehydrogenase from Mycobacterium smegmatis Archives of Biochemistry and Biophysics. 340: 168-176. PMID 9143318 DOI: 10.1006/Abbi.1997.9926 |
0.503 |
|
1997 |
Wang F, Blanchard JS, Tang XJ. Hydrogen exchange/electrospray ionization mass spectrometry studies of substrate and inhibitor binding and conformational changes of Escherichia coli dihydrodipicolinate reductase Biochemistry. 36: 3755-3759. PMID 9092803 DOI: 10.1021/Bi963065G |
0.45 |
|
1997 |
Beaman TW, Binder DA, Blanchard JS, Roderick SL. Three-dimensional structure of tetrahydrodipicolinate N- succinyltransferase Biochemistry. 36: 489-494. PMID 9012664 DOI: 10.1021/Bi962522Q |
0.388 |
|
1997 |
Zabinski RF, Blanchard JS. The requirement for manganese and oxygen in the isoniazid-dependent inactivation of Mycobacterium tuberculosis enoyl reductase Journal of the American Chemical Society. 119: 2331-2332. DOI: 10.1021/Ja9639731 |
0.323 |
|
1997 |
Basso LA, Zheng R, Musser JM, Blanchard JS. Nadh binding to wild-type and mutant forms of inha from isoniazid-resistant clinical isolates of mycobacterium tuberculosis Faseb Journal. 11: A1441. |
0.492 |
|
1997 |
Ledwidge R, Zheng R, Blanchard JS. Identification of the argD-encoded n-acetylornithine aminotransferase as n-succinyldiaminopimelate transaminase Faseb Journal. 11: A1320. |
0.425 |
|
1996 |
Scapin G, Reddy SG, Blanchard JS. Three-dimensional structure of meso-diaminopimelic acid dehydrogenase from Corynebacterium glutamicum Biochemistry. 35: 13540-13551. PMID 8885833 DOI: 10.1021/Bi961628I |
0.449 |
|
1996 |
Reddy SG, Scapin G, Blanchard JS. Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: Thermodynamic and structural analysis of binary complexes Biochemistry. 35: 13294-13302. PMID 8873595 DOI: 10.1021/Bi9615809 |
0.413 |
|
1996 |
Blanchard JS. Molecular mechanisms of drug resistance in Mycobacterium tuberculosis Annual Review of Biochemistry. 65: 215-239. PMID 8811179 DOI: 10.1146/Annurev.Bi.65.070196.001243 |
0.357 |
|
1996 |
Kliukiené R, Maroziené A, Cénas N, Becker K, Blanchard JS. Photoinactivation of trypanothione reductase and glutathione reductase by A1-phthalocyanine tetrasulfonate and hematoporphyrin Biochemical and Biophysical Research Communications. 218: 629-632. PMID 8561807 DOI: 10.1006/Bbrc.1996.0111 |
0.447 |
|
1996 |
Tao W, Grubmeyer C, Blanchard JS. Transition state structure of Salmonella typhimurium orotate phosphoribosyltransferase Biochemistry. 35: 14-21. PMID 8555167 DOI: 10.1021/Bi951898L |
0.346 |
|
1996 |
Basso LA, Zheng R, Blanchard JS. Kinetics of inactivation of WT and C243S mutant of Mycobacterium tuberculosis enoyl reductase by activated isoniazid Journal of the American Chemical Society. 118: 11301-11302. DOI: 10.1021/Ja962035Y |
0.687 |
|
1996 |
Quernard A, Dessen A, Sugantino M, Jacobs WR, Sacchettini JC, Blanchard JS. Binding of catalase-peroxidase-activated isoniazid to wild-type and mutant Mycobacterium tuberculosis enoyl-ACP reductases Journal of the American Chemical Society. 118: 1561-1562. DOI: 10.1021/Ja950998B |
0.359 |
|
1995 |
Scapin G, Blanchard JS, Sacchettini JC. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. Biochemistry. 34: 3502-12. PMID 7893645 DOI: 10.1021/Bi00011A003 |
0.452 |
|
1995 |
Blanchard JS. Expression, purification, and characterization of escherichia coli dihydrodipicolinate reductase Biochemistry®. 34: 3492-3501. PMID 7893644 DOI: 10.1021/Bi00011A002 |
0.474 |
|
1995 |
Dessen A, Quémard A, Blanchard JS, Jacobs WR, Sacchettini JC. Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis Science. 267: 1638-1641. PMID 7886450 DOI: 10.1126/Science.7886450 |
0.385 |
|
1995 |
Blanchard JS. Quinone reductase reaction catalyzed by streptococcus faecalis NADH peroxidase Biochemistry®. 34: 6621-6627. PMID 7756294 DOI: 10.1021/Bi00020A007 |
0.444 |
|
1995 |
Marcinkeviciene JA, Magliozzo RS, Blanchard JS. Purification and characterization of the Mycobacterium smegmatis catalase-peroxidase involved in isoniazid activation Journal of Biological Chemistry. 270: 22290-22295. PMID 7673210 DOI: 10.1074/Jbc.270.38.22290 |
0.456 |
|
1995 |
Blanchard JS. Enzymatic Characterization of the Target for Isoniazid in Mycobacterium tuberculosis Biochemistry®. 34: 8235-8241. PMID 7599116 DOI: 10.1021/Bi00026A004 |
0.519 |
|
1995 |
Zheng R, Cenas N, Blanchard JS. Catalytic and potentiometric characterization of E201D and E201Q mutants of Trypanosoma congolense trypanothione reductase. Biochemistry. 34: 12697-703. PMID 7548022 DOI: 10.1021/Bi00039A028 |
0.654 |
|
1995 |
Tanaka Y, Tao W, Blanchard JS, Hehre EJ. Transition state structures for the hydrolysis of alpha-D-glucopyranosyl fluoride by retaining and inverting reactions of glycosylases. Journal of Biological Chemistry. 269: 32306-32312. DOI: 10.1074/Jbc.270.10.5686 |
0.384 |
|
1994 |
Brunhuber NMW, Banerjee A, Jacobs WR, Blanchard JS. Cloning, sequencing, and expression of rhodococcus L-Phenylalanine dehydrogenase: Sequence comparisons to amino-acid dehydrogenases Journal of Biological Chemistry. 269: 16203-16211. PMID 8206922 |
0.308 |
|
1994 |
Cenas NK, Arscott D, Williams CH, Blanchard JS. Mechanism of reduction of quinones by Trypanosoma congolense trypanothione reductase. Biochemistry. 33: 2509-15. PMID 8117712 DOI: 10.1021/Bi00175A021 |
0.431 |
|
1994 |
Leichus BN, Blanchard JS. Isotopic analysis of the reaction catalyzed by glycerol dehydrogenase Biochemistry®. 33: 14642-14649. PMID 7981227 DOI: 10.1021/Bi00252A033 |
0.351 |
|
1994 |
Cenas N, Bironaite D, Dickancaite E, Anusevicius Z, Sarlauskas J, Blanchard JS. Chinifur, a Selective Inhibitor and "Subversive Substrate" for Trypanosoma congolense Trypanothione Reductase Biochemical and Biophysical Research Communications. 204: 224-229. PMID 7945363 DOI: 10.1006/Bbrc.1994.2448 |
0.382 |
|
1994 |
Brunhuber NMW, Blanchard JS. The biochemistry and enzymology of amino acid dehydrogenases Critical Reviews in Biochemistry and Molecular Biology. 29: 415-467. PMID 7705101 DOI: 10.3109/10409239409083486 |
0.422 |
|
1993 |
Matsui H, Tanaka Y, Brewer CF, Blanchard JS, Hehre EJ. Hydrolysis of α- and β-d-glucosyl fluoride by individual glucosidases: new evidence for separately controlled "plastic" and "conserved" phases in glycosylase catalysis Carbohydrate Research. 250: 45-56. DOI: 10.1016/0008-6215(93)84153-W |
0.347 |
|
1992 |
Leichus BN, Bradley M, Nadeau K, Walsh CT, Blanchard JS. Kinetic isotope effect analysis of the reaction catalyzed by Trypanosoma congolense trypanothione reductase Biochemistry. 31: 6414-6420. PMID 1633154 DOI: 10.1021/Bi00143A008 |
0.4 |
|
1992 |
Leichus BN, Blanchard JS. Pig heart lipoamide dehydrogenase: Solvent equilibrium and kinetic isotope effects Biochemistry. 31: 3065-3072. PMID 1554695 DOI: 10.1021/Bi00127A006 |
0.439 |
|
1991 |
Stoll VS, Blanchard JS. Chemical mechanism and rate-limiting steps in the reaction catalyzed by streptococcus faecalis NADH Peroxidase Biochemistry. 30: 942-948. PMID 1899199 DOI: 10.1021/Bi00218A009 |
0.368 |
|
1991 |
Sweet WL, Blanchard JS. Human erythrocyte glutathione reductase: chemical mechanism and structure of the transition state for hydride transfer. Biochemistry. 30: 8702-9. PMID 1888731 DOI: 10.1021/Bi00099A031 |
0.422 |
|
1990 |
Stoll VS, Blanchard JS. Buffers: principles and practice. Methods in Enzymology. 182: 24-38. PMID 2314240 DOI: 10.1016/0076-6879(90)82006-N |
0.427 |
|
1990 |
Sweet WL, Blanchard JS. Fumarase: viscosity dependence of the kinetic parameters. Archives of Biochemistry and Biophysics. 277: 196-202. PMID 2306120 DOI: 10.1016/0003-9861(90)90569-K |
0.355 |
|
1990 |
Vanoni MA, Wong KK, Ballou DP, Blanchard JS. Glutathione reductase: comparison of steady-state and rapid reaction primary kinetic isotope effects exhibited by the yeast, spinach, and Escherichia coli enzymes. Biochemistry. 29: 5790-6. PMID 2200516 DOI: 10.1021/Bi00476A021 |
0.481 |
|
1989 |
Wong KK, Blanchard JS. Human erythrocyte glutathione reductase: pH dependence of kinetic parameters Biochemistry. 28: 3586-3590. PMID 2742856 DOI: 10.1021/Bi00434A065 |
0.356 |
|
1988 |
Stoll VS, Blanchard JS. Kinetic mechanism and nucleotide specificity of NADH peroxidase. Archives of Biochemistry and Biophysics. 260: 752-62. PMID 3124762 DOI: 10.1016/0003-9861(88)90505-X |
0.457 |
|
1988 |
Wong KK, Vanoni MA, Blanchard JS. Glutathione reductase: Solvent equilibrium and kinetic isotope effects Biochemistry. 27: 7091-7096. PMID 2848577 DOI: 10.1021/Bi00418A063 |
0.444 |
|
1986 |
Englard S, Blanchard JS, Midelfort CF. Gamma-butyrobetaine hydroxylase: stereochemical course of the hydroxylation reaction. Biochemistry. 24: 1110-6. PMID 4096892 DOI: 10.1021/Bi00326A007 |
0.372 |
|
1986 |
Butera L, Englard S, Blanchard JS, Avigad G. Structures of D-threo-2,5-hexodiulose 1-phosphate and D-threo-2,5-hexodiulose 1,6-bisphosphate (5-keto-D-fructose mono- and bis-phosphate) in solution by 13C-N.M.R. spectroscopy. Carbohydrate Research. 148: 179-88. PMID 3708629 DOI: 10.1016/S0008-6215(00)90386-0 |
0.301 |
|
1984 |
Blanchard JS, Englard S. gamma-butyrobetaine hydroxylase: primary and secondary tritium kinetic isotope effects. Biochemistry. 22: 5922-9. PMID 6661416 DOI: 10.1021/Bi00294A036 |
0.371 |
|
1984 |
Englard S, Blanchard JS, Miura-Fraboni J. Production of trimethylamine from structurally related trimethylammonium compounds by resting cell suspensions of ?-butyrobetaine-and d, l-carnitine-grown Acinetobacter calcoaceticus and Pseudomonas putida Archives of Microbiology. 137: 88-88. DOI: 10.1007/Bf00413486 |
0.344 |
|
1983 |
Blanchard JS, Englard S, Kondo A. gamma-Butyrobetaine hydroxylase: a unique protective effect of catalase. Archives of Biochemistry and Biophysics. 219: 327-34. PMID 7165306 DOI: 10.1016/0003-9861(82)90163-1 |
0.376 |
|
1983 |
Blanchard JS. Buffers for enzymes Methods in Enzymology. 404-414. PMID 6717292 DOI: 10.1016/S0076-6879(84)04107-0 |
0.314 |
|
1982 |
Blanchard JS, Brewer CF, Englard S, Avigad G. Solution structure of 5-keto-D-fructose: relevance to the specificity of hexose kinases. Biochemistry. 21: 75-81. PMID 7059583 DOI: 10.1021/Bi00530A014 |
0.33 |
|
1982 |
Kondo A, Blanchard JS, Englard S. Purification and properties of calf liver gamma-butyrobetaine hydroxylase. Archives of Biochemistry and Biophysics. 212: 338-46. PMID 6798936 DOI: 10.1016/0003-9861(81)90374-X |
0.414 |
|
1980 |
Blanchard JS, Cleland WW. Use of isotope effects to deduce the chemical mechanism of fumarase. Biochemistry. 19: 4506-13. PMID 7407088 |
0.519 |
|
1980 |
Cook PF, Blanchard JS, Cleland WW. Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactions. Biochemistry. 19: 4853-8. PMID 7000186 DOI: 10.1021/Bi00562A023 |
0.492 |
|
1980 |
Blanchard JS, Cleland WW. Kinetic and chemical mechanisms of yeast formate dehydrogenase. Biochemistry. 19: 3543-50. PMID 6996706 |
0.533 |
|
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