| Year |
Citation |
Score |
| 2020 |
Jones BJ, Evans RL, Mylrea NJ, Chaudhury D, Luo C, Guan B, Pierce CT, Gordon WR, Wilmot CM, Kazlauskas RJ. Larger active site in an ancestral hydroxynitrile lyase increases catalytically promiscuous esterase activity. Plos One. 15: e0235341. PMID 32603354 DOI: 10.1371/Journal.Pone.0235341 |
0.417 |
|
| 2020 |
Li C, Vavra JW, Carr CE, Huang HT, Maroney MJ, Wilmot CM. Complexation of the nickel and cobalt transcriptional regulator RcnR with DNA. Acta Crystallographica. Section F, Structural Biology Communications. 76: 25-30. PMID 31929183 DOI: 10.1107/S2053230X19017084 |
0.346 |
|
| 2019 |
Koehn EM, Latham JA, Armand T, Evans RL, Tu X, Wilmot CM, Iavarone AT, Klinman JP. Discovery of Hydroxylase Activity for PqqB Provides a Missing Link in the Pyrroloquinoline Quinone Biosynthetic Pathway. Journal of the American Chemical Society. PMID 30811189 DOI: 10.1021/Jacs.8B13453 |
0.387 |
|
| 2018 |
Jensen MR, Goblirsch BR, Esler MA, Christenson JK, Mohamed FA, Wackett LP, Wilmot CM. The role of OleA His285 in orchestration of long-chain acyl-coenzyme A substrates. Febs Letters. PMID 29430657 DOI: 10.1002/1873-3468.13004 |
0.795 |
|
| 2018 |
Barr I, Stich TA, Gizzi AS, Grove TL, Bonanno JB, Latham JA, Chung T, Wilmot CM, Britt RD, Almo SC, Klinman JP. X-ray and EPR Characterization of the Auxiliary Fe-S Clusters in the Radical SAM Enzyme PqqE. Biochemistry. PMID 29405700 DOI: 10.1021/Acs.Biochem.7B01097 |
0.347 |
|
| 2017 |
Jensen MR, Goblirsch BR, Christenson JK, Esler MA, Mohamed FA, Wackett LP, Wilmot CM. OleA Glu117 is key to condensation of two fatty-acyl coenzyme A substrates in long-chain olefin biosynthesis. The Biochemical Journal. PMID 29025976 DOI: 10.1042/Bcj20170642 |
0.812 |
|
| 2017 |
Tu X, Latham JA, Klema VJ, Evans RL, Li C, Klinman JP, Wilmot CM. Crystal structures reveal metal-binding plasticity at the metallo-β-lactamase active site of PqqB from Pseudomonas putida. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 28825148 DOI: 10.1007/S00775-017-1486-8 |
0.786 |
|
| 2017 |
Evans RL, Latham JA, Xia Y, Klinman JP, Wilmot CM. NMR structure and binding studies of PqqD, a chaperone required in the biosynthesis of the bacterial dehydrogenase cofactor pyrroloquinoline quinone. Biochemistry. PMID 28481092 DOI: 10.1021/Acs.Biochem.7B00247 |
0.358 |
|
| 2017 |
Christenson JK, Jensen MR, Goblirsch BR, Mohamed F, Zhang W, Wilmot CM, Wackett LP. Active Multi-Enzyme Assemblies for Long-Chain Olefinic Hydrocarbon Biosynthesis. Journal of Bacteriology. PMID 28223313 DOI: 10.1128/Jb.00890-16 |
0.803 |
|
| 2016 |
Christenson JK, Richman JE, Jensen MR, Neufeld JY, Wilmot CM, Wackett LP. β-Lactone Synthetase Found in Olefin Biosynthesis Pathway. Biochemistry. PMID 28029240 DOI: 10.1021/Acs.Biochem.6B01199 |
0.348 |
|
| 2016 |
Goblirsch BR, Jensen MR, Mohamed F, Wackett LP, Wilmot CM. Substrate Trapping in Crystals of the Thiolase OleA Identifies Three Channels that Enable Long-Chain Olefin Biosynthesis. The Journal of Biological Chemistry. PMID 27815501 DOI: 10.1074/Jbc.M116.760892 |
0.817 |
|
| 2016 |
Evans RL, Latham JA, Klinman JP, Wilmot CM, Xia Y. (1)H, (13)C, and (15)N resonance assignments and secondary structure information for Methylobacterium extorquens PqqD and the complex of PqqD with PqqA. Biomolecular Nmr Assignments. PMID 27638737 DOI: 10.1007/S12104-016-9705-8 |
0.418 |
|
| 2016 |
Roessler CG, Agarwal R, Allaire M, Alonso-Mori R, Andi B, Bachega JF, Bommer M, Brewster AS, Browne MC, Chatterjee R, Cho E, Cohen AE, Cowan M, Datwani S, Davidson VL, ... ... Wilmot CM, et al. Acoustic Injectors for Drop-On-Demand Serial Femtosecond Crystallography. Structure (London, England : 1993). PMID 26996959 DOI: 10.1016/J.Str.2016.02.007 |
0.326 |
|
| 2015 |
Shin S, Feng M, Li C, Williamson HR, Choi M, Wilmot CM, Davidson VL. A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent Fe(II)/Fe(III) state and enhances charge resonance stabilization of the bis-Fe(IV) state. Biochimica Et Biophysica Acta. 1847: 709-16. PMID 25896561 DOI: 10.1016/J.Bbabio.2015.04.008 |
0.319 |
|
| 2014 |
Cheng Z, Cheung P, Kuo AJ, Yukl ET, Wilmot CM, Gozani O, Patel DJ. A molecular threading mechanism underlies Jumonji lysine demethylase KDM2A regulation of methylated H3K36. Genes & Development. 28: 1758-71. PMID 25128496 DOI: 10.1101/Gad.246561.114 |
0.37 |
|
| 2014 |
Shin S, Yukl ET, Sehanobish E, Wilmot CM, Davidson VL. Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG. Biochemistry. 53: 1342-9. PMID 24517455 DOI: 10.1021/Bi5000349 |
0.404 |
|
| 2014 |
Ou L, Herzog TL, Wilmot CM, Whitley CB. Standardization of α-L-iduronidase enzyme assay with Michaelis-Menten kinetics. Molecular Genetics and Metabolism. 111: 113-5. PMID 24332804 DOI: 10.1016/J.Ymgme.2013.11.009 |
0.338 |
|
| 2014 |
Wilmot C, Yukl E, Jensen L, Davidson V. MauG catalysis: a tale of ferryl iron, radicals and long distance hopping Acta Crystallographica Section a Foundations and Advances. 70: C312-C312. DOI: 10.1107/S2053273314096879 |
0.462 |
|
| 2013 |
Yukl ET, Williamson HR, Higgins L, Davidson VL, Wilmot CM. Oxidative damage in MauG: implications for the control of high-valent iron species and radical propagation pathways. Biochemistry. 52: 9447-55. PMID 24320950 DOI: 10.1021/Bi401441H |
0.411 |
|
| 2013 |
Makris TM, Knoot CJ, Wilmot CM, Lipscomb JD. Structure of a dinuclear iron cluster-containing β-hydroxylase active in antibiotic biosynthesis. Biochemistry. 52: 6662-71. PMID 23980641 DOI: 10.1021/Bi400845B |
0.437 |
|
| 2013 |
Cedervall P, Hooper AB, Wilmot CM. Structural studies of hydroxylamine oxidoreductase reveal a unique heme cofactor and a previously unidentified interaction partner. Biochemistry. 52: 6211-8. PMID 23952581 DOI: 10.1021/Bi400960W |
0.821 |
|
| 2013 |
Abu Tarboush N, Yukl ET, Shin S, Feng M, Wilmot CM, Davidson VL. Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG. Biochemistry. 52: 6358-67. PMID 23952537 DOI: 10.1021/Bi400905S |
0.345 |
|
| 2013 |
Johnson BJ, Yukl ET, Klema VJ, Klinman JP, Wilmot CM. Structural snapshots from the oxidative half-reaction of a copper amine oxidase: Implications for O2 activation Journal of Biological Chemistry. 288: 28409-28417. PMID 23940035 DOI: 10.1074/Jbc.M113.501791 |
0.801 |
|
| 2013 |
Yukl ET, Jensen LM, Davidson VL, Wilmot CM. Structures of MauG in complex with quinol and quinone MADH. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 69: 738-43. PMID 23832199 DOI: 10.1107/S1744309113016539 |
0.42 |
|
| 2013 |
Davidson VL, Wilmot CM. Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone. Annual Review of Biochemistry. 82: 531-50. PMID 23746262 DOI: 10.1146/Annurev-Biochem-051110-133601 |
0.459 |
|
| 2013 |
Abu Tarboush N, Jensen LM, Wilmot CM, Davidson VL. A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis. Febs Letters. 587: 1736-41. PMID 23669364 DOI: 10.1016/J.Febslet.2013.04.047 |
0.415 |
|
| 2013 |
Yukl ET, Liu F, Krzystek J, Shin S, Jensen LM, Davidson VL, Wilmot CM, Liu A. Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. 110: 4569-73. PMID 23487750 DOI: 10.1073/Pnas.1215011110 |
0.421 |
|
| 2013 |
Klema VJ, Solheid CJ, Klinman JP, Wilmot CM. Structural analysis of aliphatic versus aromatic substrate specificity in a copper amine oxidase from hansenula polymorpha Biochemistry. 52: 2291-2301. PMID 23452079 DOI: 10.1021/Bi3016845 |
0.824 |
|
| 2013 |
Wilmot CM, Yukl ET. MauG: a di-heme enzyme required for methylamine dehydrogenase maturation. Dalton Transactions (Cambridge, England : 2003). 42: 3127-35. PMID 23086017 DOI: 10.1039/C2Dt32059B |
0.386 |
|
| 2013 |
Johnson BJ, Yukl ET, Klema VJ, Klinman JP, Wilmot CM. Structural evidence for the semiquinone in a copper amine oxidase from Hansenula polymorpha: implications for the catalytic mechanism Journal of Biological Chemistry. DOI: 10.2210/Pdb4Kfd/Pdb |
0.792 |
|
| 2012 |
Jensen LM, Meharenna YT, Davidson VL, Poulos TL, Hedman B, Wilmot CM, Sarangi R. Geometric and electronic structures of the His-Fe(IV)=O and His-Fe(IV)-Tyr hemes of MauG. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 17: 1241-55. PMID 23053529 DOI: 10.1007/S00775-012-0939-3 |
0.345 |
|
| 2012 |
Klema VJ, Wilmot CM. The role of protein crystallography in defining the mechanisms of biogenesis and catalysis in copper amine oxidase. International Journal of Molecular Sciences. 13: 5375-405. PMID 22754303 DOI: 10.3390/Ijms13055375 |
0.82 |
|
| 2012 |
Klema VJ, Johnson BJ, Klinman JP, Wilmot CM. The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with Cu I and Co II Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 68: 501-510. PMID 22691777 DOI: 10.1107/S1744309112012857 |
0.796 |
|
| 2012 |
Wilmot CM. Polysaccharide monoxygenases: giving a boost to biofuel production. Structure (London, England : 1993). 20: 938-40. PMID 22681899 DOI: 10.1016/J.Str.2012.05.006 |
0.429 |
|
| 2012 |
Goblirsch BR, Frias JA, Wackett LP, Wilmot CM. Crystal structures of Xanthomonas campestris OleA reveal features that promote head-to-head condensation of two long-chain fatty acids. Biochemistry. 51: 4138-46. PMID 22524624 DOI: 10.1021/Bi300386M |
0.818 |
|
| 2012 |
Yukl ET, Wilmot CM. Cofactor biosynthesis through protein post-translational modification. Current Opinion in Chemical Biology. 16: 54-9. PMID 22387133 DOI: 10.1016/J.Cbpa.2012.02.010 |
0.381 |
|
| 2012 |
Feng M, Jensen LM, Yukl ET, Wei X, Liu A, Wilmot CM, Davidson VL. Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauG. Biochemistry. 51: 1598-606. PMID 22299652 DOI: 10.1021/Bi201882E |
0.457 |
|
| 2011 |
Tarboush NA, Jensen LM, Yukl ET, Geng J, Liu A, Wilmot CM, Davidson VL. Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. 108: 16956-61. PMID 21969534 DOI: 10.1073/Pnas.1109423108 |
0.378 |
|
| 2011 |
Cedervall PE, Dey M, Li X, Sarangi R, Hedman B, Ragsdale SW, Wilmot CM. Structural analysis of a Ni-methyl species in methyl-coenzyme M reductase from Methanothermobacter marburgensis. Journal of the American Chemical Society. 133: 5626-8. PMID 21438550 DOI: 10.1021/Ja110492P |
0.784 |
|
| 2011 |
Yukl ET, Goblirsch BR, Davidson VL, Wilmot CM. Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: implications for the mechanism of dioxygen activation. Biochemistry. 50: 2931-8. PMID 21355604 DOI: 10.1021/Bi200023N |
0.802 |
|
| 2011 |
Goblirsch B, Kurker RC, Streit BR, Wilmot CM, DuBois JL. Chlorite dismutases, DyPs, and EfeB: 3 microbial heme enzyme families comprise the CDE structural superfamily. Journal of Molecular Biology. 408: 379-98. PMID 21354424 DOI: 10.1016/J.Jmb.2011.02.047 |
0.76 |
|
| 2011 |
Shin S, Feng M, Chen Y, Jensen LM, Tachikawa H, Wilmot CM, Liu A, Davidson VL. The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis. Biochemistry. 50: 144-50. PMID 21128656 DOI: 10.1021/Bi101819M |
0.308 |
|
| 2011 |
Jensen L, Sanishvili R, Tarboush NA, Davidson V, Wilmot C. Protein complex structures inform about the reactivity of the hemoprotein MauG Acta Crystallographica Section a Foundations of Crystallography. 67: C218-C218. DOI: 10.1107/S0108767311094591 |
0.308 |
|
| 2010 |
Abu Tarboush N, Jensen LM, Feng M, Tachikawa H, Wilmot CM, Davidson VL. Functional importance of tyrosine 294 and the catalytic selectivity for the bis-Fe(IV) state of MauG revealed by replacement of this axial heme ligand with histidine . Biochemistry. 49: 9783-91. PMID 20929212 DOI: 10.1021/Bi101254P |
0.364 |
|
| 2010 |
Frias JA, Goblirsch BR, Wackett LP, Wilmot CM. Cloning, purification, crystallization and preliminary X-ray diffraction of the OleC protein from Stenotrophomonas maltophilia involved in head-to-head hydrocarbon biosynthesis. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 66: 1108-10. PMID 20823539 DOI: 10.1107/S1744309110031751 |
0.792 |
|
| 2010 |
Cedervall PE, Dey M, Pearson AR, Ragsdale SW, Wilmot CM. Structural insight into methyl-coenzyme M reductase chemistry using coenzyme B analogues . Biochemistry. 49: 7683-93. PMID 20707311 DOI: 10.1021/Bi100458D |
0.784 |
|
| 2010 |
Goblirsch BR, Streit BR, Dubois JL, Wilmot CM. Structural features promoting dioxygen production by Dechloromonas aromatica chlorite dismutase. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 15: 879-88. PMID 20386942 DOI: 10.1007/S00775-010-0651-0 |
0.827 |
|
| 2010 |
Jensen LM, Sanishvili R, Davidson VL, Wilmot CM. In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex. Science (New York, N.Y.). 327: 1392-4. PMID 20223990 DOI: 10.1126/Science.1182492 |
0.508 |
|
| 2010 |
Chang CM, Klema VJ, Johnson BJ, Mure M, Klinman JP, Wilmot CM. Kinetic and structural analysis of substrate specificity in two copper amine oxidases from Hansenula polymorpha Biochemistry. 49: 2540-2550. PMID 20155950 DOI: 10.1021/Bi901933D |
0.797 |
|
| 2009 |
Cedervall PE, Hooper AB, Wilmot CM. Crystallization and preliminary X-ray crystallographic analysis of a new crystal form of hydroxylamine oxidoreductase from Nitrosomonas europaea. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 65: 1296-8. PMID 20054133 DOI: 10.1107/S1744309109046119 |
0.796 |
|
| 2009 |
Goblirsch BR, Streit BR, DuBois JL, Wilmot CM. Crystallization and preliminary X-ray diffraction of chlorite dismutase from Dechloromonas aromatica RCB. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 65: 818-21. PMID 19652348 DOI: 10.1107/S1744309109026785 |
0.786 |
|
| 2009 |
Wilmot CM, Davidson VL. Uncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis. Current Opinion in Chemical Biology. 13: 469-74. PMID 19648051 DOI: 10.1016/J.Cbpa.2009.06.026 |
0.42 |
|
| 2007 |
De la Mora-Rey T, Wilmot CM. Synergy within structural biology of single crystal optical spectroscopy and X-ray crystallography. Current Opinion in Structural Biology. 17: 580-6. PMID 17959373 DOI: 10.1016/J.Sbi.2007.09.005 |
0.791 |
|
| 2007 |
Pearson AR, Elmore BO, Yang C, Ferrara JD, Hooper AB, Wilmot CM. The crystal structure of cytochrome P460 of Nitrosomonas europaea reveals a novel cytochrome fold and heme-protein cross-link. Biochemistry. 46: 8340-9. PMID 17583915 DOI: 10.1021/Bi700086R |
0.698 |
|
| 2007 |
Wilmot CM. Biochemistry. An ancient and intimate partnership. Science (New York, N.Y.). 316: 379-80. PMID 17446378 DOI: 10.1126/Science.1141629 |
0.352 |
|
| 2007 |
Johnson BJ, Cohen J, Welford RW, Pearson AR, Schulten K, Klinman JP, Wilmot CM. Exploring molecular oxygen pathways in Hansenula polymorpha copper-containing amine oxidase Journal of Biological Chemistry. 282: 17767-17776. PMID 17409383 DOI: 10.1074/Jbc.M701308200 |
0.695 |
|
| 2007 |
Knowles P, Kurtis C, Murray J, Saysell C, Tambyrajah W, Wilmot C, McPherson M, Phillips S, Dooley D, Brown D, Rogers M, Mure M. Hydrazine and amphetamine binding to amine oxidases: Old drugs with new prospects Journal of Neural Transmission. 114: 743-746. PMID 17406963 DOI: 10.1007/S00702-007-0681-0 |
0.345 |
|
| 2007 |
Pearson AR, Pahl R, Kovaleva EG, Davidson VL, Wilmot CM. Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry. Journal of Synchrotron Radiation. 14: 92-8. PMID 17211075 DOI: 10.1107/S0909049506051259 |
0.665 |
|
| 2006 |
Li X, Jones LH, Pearson AR, Wilmot CM, Davidson VL. Mechanistic possibilities in MauG-dependent tryptophan tryptophylquinone biosynthesis. Biochemistry. 45: 13276-83. PMID 17073448 DOI: 10.1021/Bi061497D |
0.67 |
|
| 2006 |
Pearson AR, Marimanikkuppam S, Li X, Davidson VL, Wilmot CM. Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase. Journal of the American Chemical Society. 128: 12416-7. PMID 16984182 DOI: 10.1021/Ja064466E |
0.636 |
|
| 2006 |
Elmore BO, Pearson AR, Wilmot CM, Hooper AB. Expression, purification, crystallization and preliminary X-ray diffraction of a novel Nitrosomonas europaea cytochrome, cytochrome P460. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 62: 395-8. PMID 16582494 DOI: 10.1107/S1744309106008785 |
0.666 |
|
| 2005 |
Wang Y, Li X, Jones LH, Pearson AR, Wilmot CM, Davidson VL. MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase. Journal of the American Chemical Society. 127: 8258-9. PMID 15941239 DOI: 10.1021/Ja051734K |
0.676 |
|
| 2005 |
Jones LH, Pearson AR, Tang Y, Wilmot CM, Davidson VL. Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase. The Journal of Biological Chemistry. 280: 17392-6. PMID 15734739 DOI: 10.1074/Jbc.M500943200 |
0.675 |
|
| 2005 |
Mure M, Kurtis CR, Brown DE, Rogers MS, Tambyrajah WS, Saysell C, Wilmot CM, Phillips SE, Knowles PF, Dooley DM, McPherson MJ. Active site rearrangement of the 2-hydrazinopyridine adduct in Escherichia coli amine oxidase to an azo copper(II) chelate form: a key role for tyrosine 369 in controlling the mobility of the TPQ-2HP adduct. Biochemistry. 44: 1583-94. PMID 15683242 DOI: 10.1021/Bi0479860 |
0.416 |
|
| 2005 |
Mure M, Brown DE, Saysell C, Rogers MS, Wilmot CM, Kurtis CR, McPherson MJ, Phillips SE, Knowles PF, Dooley DM. Role of the interactions between the active site base and the substrate Schiff base in amine oxidase catalysis. Evidence from structural and spectroscopic studies of the 2-hydrazinopyridine adduct of Escherichia coli amine oxidase. Biochemistry. 44: 1568-82. PMID 15683241 DOI: 10.1021/Bi047988K |
0.435 |
|
| 2005 |
De la Mora-Rey T, Pearson AR, Watts KT, Hoeffner E, Wilmot C. X-ray structures of methylamine dehydrogenase reaction intermediates Acta Crystallographica Section a Foundations of Crystallography. 61: c182-c182. DOI: 10.1107/S0108767305092251 |
0.642 |
|
| 2005 |
Pearson AR, De la Mora Rey T, Watts KT, Hoeffner E, Wilmot CM. Tracking X-ray derived redox changes using single crystal microspectrophotometry Acta Crystallographica Section a Foundations of Crystallography. 61: c195-c195. DOI: 10.1107/S0108767305091683 |
0.629 |
|
| 2005 |
Johnson B, Pearson A, Samuels N, Klinman J, Wilmot C. Dioxygen activation inHansenula polymorphaamine oxidase Acta Crystallographica Section a Foundations of Crystallography. 61: c209-c210. DOI: 10.1107/S0108767305091087 |
0.592 |
|
| 2004 |
Wilmot CM, Saysell CG, Blessington A, Conn DA, Kurtis CR, McPherson MJ, Knowles PF, Phillips SE. Medical implications from the crystal structure of a copper-containing amine oxidase complexed with the antidepressant drug tranylcypromine. Febs Letters. 576: 301-5. PMID 15498552 DOI: 10.1016/J.Febslet.2004.09.031 |
0.433 |
|
| 2004 |
Brazeau BJ, Johnson BJ, Wilmot CM. Copper-containing amine oxidases. Biogenesis and catalysis; a structural perspective. Archives of Biochemistry and Biophysics. 428: 22-31. PMID 15234266 DOI: 10.1016/J.Abb.2004.03.034 |
0.487 |
|
| 2004 |
Pearson AR, De La Mora-Rey T, Graichen ME, Wang Y, Jones LH, Marimanikkupam S, Agger SA, Grimsrud PA, Davidson VL, Wilmot CM. Further insights into quinone cofactor biogenesis: probing the role of mauG in methylamine dehydrogenase tryptophan tryptophylquinone formation. Biochemistry. 43: 5494-502. PMID 15122915 DOI: 10.1021/Bi049863L |
0.78 |
|
| 2004 |
Wilmot CM. Oxygen activation in a copper-containing amine oxidase. Biochemical Society Transactions. 31: 493-6. PMID 12773142 DOI: 10.1042/Bst0310493 |
0.501 |
|
| 2003 |
Wang Y, Graichen ME, Liu A, Pearson AR, Wilmot CM, Davidson VL. MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis. Biochemistry. 42: 7318-25. PMID 12809487 DOI: 10.1021/Bi034243Q |
0.629 |
|
| 2003 |
Pearson AR, Wilmot CM. Catching catalysis in the act: using single crystal kinetics to trap methylamine dehydrogenase reaction intermediates. Biochimica Et Biophysica Acta. 1647: 381-9. PMID 12686162 DOI: 10.1016/S1570-9639(03)00099-2 |
0.691 |
|
| 2003 |
Pearson AR, Jones LH, Higgins L, Ashcroft AE, Wilmot CM, Davidson VL. Understanding quinone cofactor biogenesis in methylamine dehydrogenase through novel cofactor generation. Biochemistry. 42: 3224-30. PMID 12641453 DOI: 10.1021/Bi027073A |
0.636 |
|
| 2002 |
Wilmot CM, Sjögren T, Carlsson GH, Berglund GI, Hajdu J. Defining redox state of X-ray crystal structures by single-crystal ultraviolet-visible microspectrophotometry. Methods in Enzymology. 353: 301-18. PMID 12078505 DOI: 10.1016/S0076-6879(02)53057-3 |
0.448 |
|
| 2002 |
Wilmot CM, Pearson AR. Cryocrystallography of metalloprotein reaction intermediates. Current Opinion in Chemical Biology. 6: 202-7. PMID 12039005 DOI: 10.1016/S1367-5931(02)00300-9 |
0.662 |
|
| 2002 |
Saysell CG, Tambyrajah WS, Murray JM, Wilmot CM, Phillips SEV, McPherson MJ, Knowles PF. Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue Biochemical Journal. 365: 809-816. PMID 11985492 DOI: 10.1042/Bj20011435 |
0.439 |
|
| 2002 |
Sheridan L, Wilmot CM, Cromie KD, van der Logt P, Phillips SE. Crystallization and preliminary X-ray structure determination of jack bean urease with a bound antibody fragment. Acta Crystallographica. Section D, Biological Crystallography. 58: 374-6. PMID 11807281 DOI: 10.1107/S0907444901021503 |
0.473 |
|
| 2001 |
Firbank SJ, Rogers MS, Wilmot CM, Dooley DM, Halcrow MA, Knowles PF, McPherson MJ, Phillips SE. Crystal structure of the precursor of galactose oxidase: an unusual self-processing enzyme. Proceedings of the National Academy of Sciences of the United States of America. 98: 12932-7. PMID 11698678 DOI: 10.1073/Pnas.231463798 |
0.501 |
|
| 2001 |
Murray JM, Kurtis CR, Tambyrajah W, Saysell CG, Wilmot CM, Parsons MR, Phillips SEV, Knowles PF, McPherson MJ. Conserved Tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential Biochemistry. 40: 12808-12818. PMID 11669617 DOI: 10.1021/Bi011187P |
0.499 |
|
| 2000 |
Hajdu J, Neutze R, Sjögren T, Edman K, Szöke A, Wilmouth RC, Wilmot CM. Analyzing protein functions in four dimensions. Nature Structural Biology. 7: 1006-12. PMID 11062553 DOI: 10.1038/80911 |
0.39 |
|
| 2000 |
Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE. Oxygen activation in the copper-containing quinoprotein amine oxidase Biochemical Society Transactions. 28: A77-A77. DOI: 10.1042/Bst028A077 |
0.338 |
|
| 2000 |
Kurtis C, Tambyrajah W, Murray J, Saysell C, Wilmot C, Phillips S, Knowles P, McPherson M. Role of a conserved tyrosine residue in E. coli copper amine oxidase Biochemical Society Transactions. 28: A72-A72. DOI: 10.1042/Bst028A072A |
0.316 |
|
| 2000 |
Saysell CG, Murray JM, Wilmot CM, Brown DE, Dooley DM, Phillips SEV, McPherson MJ, Knowles PF. Investigation into the mechanism of λ(max) shifts and their dependence on pH for the 2-hydrazinopyridine derivatives of two copper amine oxidases Journal of Molecular Catalysis - B Enzymatic. 8: 17-25. DOI: 10.1016/S1381-1177(99)00068-5 |
0.314 |
|
| 1999 |
Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE. Visualization of dioxygen bound to copper during enzyme catalysis. Science (New York, N.Y.). 286: 1724-8. PMID 10576737 DOI: 10.1126/Science.286.5445.1724 |
0.512 |
|
| 1999 |
Murray JM, Saysell CG, Wilmot CM, Tambyrajah WS, Jaeger J, Knowles PF, Phillips SEV, McPherson MJ. The active site base controls cofactor reactivity in Escherichia coli amine oxidase: X-ray crystallographic studies with mutational variants Biochemistry. 38: 8217-8227. PMID 10387067 DOI: 10.1021/Bi9900469 |
0.49 |
|
| 1997 |
Wilmot CM, Murray JM, Alton G, Parsons MR, Convery MA, Blakeley V, Corner AS, Palcic MM, Knowles PF, McPherson MJ, Phillips SEV. Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: Exploring the reductive half-reaction Biochemistry. 36: 1608-1620. PMID 9048544 DOI: 10.1021/Bi962205J |
0.486 |
|
| 1997 |
Reynolds MP, Baron AJ, Wilmot CM, Vinecombe E, Stevens C, Phillips SEV, Knowles PF, McPherson MJ. Structure and mechanism of galactose oxidase: catalytic role of tyrosine 495 Jbic Journal of Biological Inorganic Chemistry. 2: 327-335. DOI: 10.1007/S007750050139 |
0.431 |
|
| 1996 |
Wilmot CM, Parsons MR, Convery MA, Blakeley V, Corner AS, Yadav KDS, McPherson MJ, Knowles PF, Phillips SEV. Crystal structure of an inhibitor complex with the quinoenzyme amine oxidase identifies the active site base Acta Crystallographica Section a Foundations of Crystallography. 52: C139-C139. DOI: 10.1107/S010876739609366X |
0.412 |
|
| 1995 |
Reynolds MP, Baron AJ, Wilmot CM, Phillips SE, Knowles PF, McPherson MJ. Tyrosine 495 is a key residue in the active site of galactose oxidase. Biochemical Society Transactions. 23: 510S. PMID 8654695 DOI: 10.1042/Bst023510S |
0.479 |
|
| 1995 |
Parsons MR, Convery MA, Wilmot CM, Yadav KD, Blakeley V, Corner AS, Phillips SE, McPherson MJ, Knowles PF. Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution. Structure (London, England : 1993). 3: 1171-84. PMID 8591028 DOI: 10.1016/S0969-2126(01)00253-2 |
0.487 |
|
| 1995 |
Convery M, Knowles P, McPherson M, Parsons M, Phillips S, Yadav K, Wilmot C. The structure of amine oxidase from E. coli: Implications for the catalytic mechanism Journal of Inorganic Biochemistry. 59: 658. DOI: 10.1016/0162-0134(95)97746-D |
0.335 |
|
| 1993 |
Baron AJ, Stevens C, Wilmot CM, Knowles PF, Phillips SE, McPherson MJ. Preliminary studies of two active site mutants of galactose oxidase. Biochemical Society Transactions. 21: 319S. PMID 8224464 DOI: 10.1042/Bst021319S |
0.314 |
|
| 1992 |
Stura EA, Chen P, Wilmot CM, Arevalo JH, Wilson IA. Crystallization studies of glycosylated and unglycosylated human recombinant interleukin-2. Proteins. 12: 24-30. PMID 1553380 DOI: 10.1002/Prot.340120104 |
0.468 |
|
| 1990 |
Wilmot CM, Thornton JM. Beta-turns and their distortions: a proposed new nomenclature. Protein Engineering. 3: 479-93. PMID 2371257 DOI: 10.1093/Protein/3.6.479 |
0.473 |
|
| 1988 |
Wilmot CM, Thornton JM. Analysis and prediction of the different types of beta-turn in proteins. Journal of Molecular Biology. 203: 221-32. PMID 3184187 DOI: 10.1016/0022-2836(88)90103-9 |
0.454 |
|
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