C. Wilmot

发表

Beta-turns and their distortions: a proposed new nomenclature.

J. Thornton, C. Wilmot, 1990, Protein engineering.

Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.

M. R. Parsons, M. McPherson, C. Wilmot, 1995, Structure.

Analysis and prediction of the different types of β-turn in proteins

J. Thornton, C. Wilmot, 1988 .

Analysis and prediction of the different types of beta-turn in proteins.

J. Thornton, C. Wilmot, 1988, Journal of molecular biology.

Active Multienzyme Assemblies for Long-Chain Olefinic Hydrocarbon Biosynthesis

L. Wackett, C. Wilmot, Wei Zhang, 2017, Journal of bacteriology.

β-Lactone Synthetase Found in the Olefin Biosynthesis Pathway.

L. Wackett, C. Wilmot, J. Richman, 2017, Biochemistry.

Structural insight into methyl-coenzyme M reductase chemistry using coenzyme B analogues .

C. Wilmot, S. Ragsdale, A. Pearson, 2010, Biochemistry.

Larger active site in an ancestral hydroxynitrile lyase increases catalytically promiscuous esterase activity

C. Wilmot, R. Kazlauskas, W. Gordon, 2020, bioRxiv.

The crystal structure of cytochrome P460 of Nitrosomonas europaea reveals a novel cytochrome fold and heme-protein cross-link.

Cheng Yang, C. Wilmot, A. Hooper, 2007, Biochemistry.

Discovery of Hydroxylase Activity for PqqB Provides a Missing Link in the Pyrroloquinoline Quinone Biosynthetic Pathway.

J. Klinman, C. Wilmot, J. Latham, 2019, Journal of the American Chemical Society.

Structural analysis of aliphatic versus aromatic substrate specificity in a copper amine oxidase from Hansenula polymorpha.

J. Klinman, C. Wilmot, V. J. Klema, 2013, Biochemistry.

Crystallization and preliminary X-ray diffraction of chlorite dismutase from Dechloromonas aromatica RCB.

C. Wilmot, J. DuBois, B. Goblirsch, 2009, Acta crystallographica. Section F, Structural biology and crystallization communications.

Active Site Aspartate Residues Are Critical for Tryptophan Tryptophylquinone Biogenesis in Methylamine Dehydrogenase*

C. Wilmot, V. Davidson, L. Jones, 2005, Journal of Biological Chemistry.

An elastin gene mutation producing abnormal tropoelastin and abnormal elastic fibres in a patient with autosomal dominant cutis laxa.

M. Tassabehji, G. Ashcroft, C. Wilmot, 1998, Human molecular genetics.

Crystallization and preliminary X-ray crystallographic analysis of a new crystal form of hydroxylamine oxidoreductase from Nitrosomonas europaea.

C. Wilmot, A. Hooper, P. Cedervall, 2009, Acta crystallographica. Section F, Structural biology and crystallization communications.

Copper-containing amine oxidases. Biogenesis and catalysis; a structural perspective.

C. Wilmot, B. J. Johnson, B. Brazeau, 2004, Archives of biochemistry and biophysics.

Structures of MauG in complex with quinol and quinone MADH.

C. Wilmot, V. Davidson, E. Yukl, 2013, Acta crystallographica. Section F, Structural biology and crystallization communications.

Cloning, purification, crystallization and preliminary X-ray diffraction of the OleC protein from Stenotrophomonas maltophilia involved in head-to-head hydrocarbon biosynthesis.

L. Wackett, C. Wilmot, Janice A. Frias, 2010, Acta crystallographica. Section F, Structural biology and crystallization communications.

A molecular threading mechanism underlies Jumonji lysine demethylase KDM2A regulation of methylated H3K36

D. Patel, C. Wilmot, O. Gozani, 2014, Genes & development.

Complexation of the nickel and cobalt transcriptional regulator RcnR with DNA.

C. Wilmot, M. Maroney, Carolyn E Carr, 2020, Acta crystallographica. Section F, Structural biology communications.

Standardization of α-L-iduronidase enzyme assay with Michaelis-Menten kinetics.

C. Wilmot, C. Whitley, Li Ou, 2014, Molecular genetics and metabolism.

An Ancient and Intimate Partnership

C. Wilmot, 2007, Science.

Geometric and electronic structures of the His–Fe(IV)=O and His–Fe(IV)–Tyr hemes of MauG

T. Poulos, C. Wilmot, V. Davidson, 2012, JBIC Journal of Biological Inorganic Chemistry.

Structural analysis of a Ni-methyl species in methyl-coenzyme M reductase from Methanothermobacter marburgensis.

C. Wilmot, S. Ragsdale, B. Hedman, 2011, Journal of the American Chemical Society.

Acoustic Injectors for Drop-On-Demand Serial Femtosecond Crystallography.

A. Kuczewski, Diling Zhu, A. Cohen, 2016, Structure.

Structural Snapshots from the Oxidative Half-reaction of a Copper Amine Oxidase

J. Klinman, C. Wilmot, B. J. Johnson, 2013, The Journal of Biological Chemistry.

The Role of Protein Crystallography in Defining the Mechanisms of Biogenesis and Catalysis in Copper Amine Oxidase

C. Wilmot, V. J. Klema, 2012, International journal of molecular sciences.

Kinetic and structural analysis of substrate specificity in two copper amine oxidases from Hansenula polymorpha.

J. Klinman, C. Wilmot, B. J. Johnson, 2010, Biochemistry.

Visualization of dioxygen bound to copper during enzyme catalysis.

J. Hajdu, M. McPherson, C. Wilmot, 1999, Science.

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.

M. McPherson, C. Wilmot, S. Phillips, 2005, Biochemistry.

Oxygen activation in a copper-containing amine oxidase.

C. Wilmot, 2003, Biochemical Society transactions.

Exploring Molecular Oxygen Pathways in Hansenula polymorpha Copper-containing Amine Oxidase*

Klaus Schulten, Judith P Klinman, Arwen R Pearson, 2007, Journal of Biological Chemistry.

Prokaryotic Copper Amine Oxidases

M. R. Parsons, M. McPherson, C. Wilmot, 2006 .

Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction.

M. R. Parsons, M. McPherson, C. Wilmot, 1997, Biochemistry.

Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis

C. Wilmot, V. Davidson, J. Krzystek, 2013, Proceedings of the National Academy of Sciences.

The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with CuI and CoII.

J. Klinman, C. Wilmot, B. J. Johnson, 2012, Acta crystallographica. Section F, Structural biology and crystallization communications.

Crystal structure of the precursor of galactose oxidase: An unusual self-processing enzyme

M. McPherson, C. Wilmot, S. Phillips, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone.

C. Wilmot, V. Davidson, 2013, Annual review of biochemistry.

MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.

C. Wilmot, E. Yukl, 2013, Dalton transactions.

Investigation into the mechanism of λmax shifts and their dependence on pH for the 2-hydrazinopyridine derivatives of two copper amine oxidases

M. McPherson, C. Wilmot, S. Phillips, 2000 .

Catching catalysis in the act: using single crystal kinetics to trap methylamine dehydrogenase reaction intermediates.

C. Wilmot, A. Pearson, 2003, Biochimica et biophysica acta.

Cofactor biosynthesis through protein post-translational modification.

C. Wilmot, E. Yukl, Carrie M Wilmot, 2012, Current opinion in chemical biology.

X-ray and EPR Characterization of the Auxiliary Fe-S Clusters in the Radical SAM Enzyme PqqE.

J. Klinman, S. Almo, J. Bonanno, 2018, Biochemistry.

Structural features promoting dioxygen production by Dechloromonas aromatica chlorite dismutase

C. Wilmot, J. DuBois, B. Goblirsch, 2010, JBIC Journal of Biological Inorganic Chemistry.

A transcription factor involved in skeletal muscle gene expression is deleted in patients with Williams syndrome

M. Tassabehji, C. Wilmot, A. Read, 1999, European Journal of Human Genetics.

Crystal structures of Xanthomonas campestris OleA reveal features that promote head-to-head condensation of two long-chain fatty acids.

L. Wackett, C. Wilmot, Janice A. Frias, 2012, Biochemistry.

Chlorite dismutases, DyPs, and EfeB: 3 microbial heme enzyme families comprise the CDE structural superfamily.

C. Wilmot, J. DuBois, R. Kurker, 2011, Journal of molecular biology.

1H, 13C, and 15N resonance assignments and secondary structure information for Methylobacterium extorquens PqqD and the complex of PqqD with PqqA

J. Klinman, C. Wilmot, J. Latham, 2016, Biomolecular NMR Assignments.

1H, 13C, and 15N resonance assignments and secondary structure information for Methylobacterium extorquens PqqD and the complex of PqqD with PqqA

J. Klinman, C. Wilmot, J. Latham, 2016, Biomolecular NMR assignments.

Nuclear Magnetic Resonance Structure and Binding Studies of PqqD, a Chaperone Required in the Biosynthesis of the Bacterial Dehydrogenase Cofactor Pyrroloquinoline Quinone.

J. Klinman, C. Wilmot, J. Latham, 2017, Biochemistry.

Structures in the AKH Family of Neuropeptides

J. Thornton, C. Wilmot, A. Drake, 1990 .

Structural studies of hydroxylamine oxidoreductase reveal a unique heme cofactor and a previously unidentified interaction partner.

C. Wilmot, A. Hooper, P. Cedervall, 2013, Biochemistry.

demethylase KDM 2 A regulation of methylated H 3 K 36 A molecular threading mechanism underlies Jumonji lysine Material

D. Patel, C. Wilmot, O. Gozani, 2014 .

Standardization of α-L-iduronidase enzyme assay with Michaelis-Menten kinetics.

C. Wilmot, C. Whitley, Li Ou, 2014, Molecular genetics and metabolism.

Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration.

K. Zahs, K. Ashe, J. Cleary, 2015, Cell reports.

Secondary and Supersecondary Motifs in Protein Structures

Janet M. Thornton, B. L. Sibanda, Bancinyane L. Sibanda, 1992 .

Crystallization and preliminary X-ray structure determination of jack bean urease with a bound antibody fragment.

C. Wilmot, S. Phillips, L. Sheridan, 2002, Acta crystallographica. Section D, Biological crystallography.

Analyzing protein functions in four dimensions

Karl Edman, Carrie M. Wilmot, Abraham Szöke, 2000, Nature Structural Biology.

OleA Glu117 is key to condensation of two fatty-acyl coenzyme A substrates in long-chain olefin biosynthesis.

L. Wackett, C. Wilmot, M. Jensen, 2017, The Biochemical journal.

Substrate Trapping in Crystals of the Thiolase OleA Identifies Three Channels That Enable Long Chain Olefin Biosynthesis*

L. Wackett, C. Wilmot, M. Jensen, 2016, The Journal of Biological Chemistry.

Quaternary Structure Defi nes a Large Class of Amyloid-b Oligomers Neutralized by Sequestration Graphical

K. Zahs, K. Ashe, J. Cleary, 2015 .

Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis

C. Wilmot, V. Davidson, J. Geng, 2011, Proceedings of the National Academy of Sciences.

Structure-Based Design and Biological Evaluation of Novel Caspase2 Inhibitors Based on the Peptide AcVDVAD-CHO and the Caspase-2-Mediated Tau Cleavage Sequence YKPVD314

K. Ashe, M. Walters, B. Finzel, 2022, ACS Pharmacology & Translational Science.

Tyrosine 495 is a key residue in the active site of galactose oxidase.

M. McPherson, C. Wilmot, S. Phillips, 1995, Biochemical Society transactions.

Crystal structures reveal metal-binding plasticity at the metallo-β-lactamase active site of PqqB from Pseudomonas putida

J. Klinman, C. Wilmot, J. Latham, 2017, JBIC Journal of Biological Inorganic Chemistry.

Uncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis.

C. Wilmot, V. Davidson, 2009, Current opinion in chemical biology.

MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis.

C. Wilmot, V. Davidson, M. Graichen, 2003, Biochemistry.

Structure of a dinuclear iron cluster-containing β-hydroxylase active in antibiotic biosynthesis.

C. Wilmot, J. Lipscomb, C. J. Knoot, 2013, Biochemistry.

Expression, purification, crystallization and preliminary X-ray diffraction of a novel Nitrosomonas europaea cytochrome, cytochrome P460.

C. Wilmot, A. Hooper, Bradley O. Elmore, 2006, Acta crystallographica. Section F, Structural biology and crystallization communications.

Influence of socio-economic status on people’s perception of the health condition of the Elsieskraal River, Cape Town, South Africa

C. Wilmot, 2015 .

Structure-Based Design and Biological Evaluation of Novel Caspase-2 Inhibitors Based on the Peptide AcVDVAD-CHO and the Caspase-2-Mediated Tau Cleavage Sequence YKPVD314.

K. Ashe, M. Walters, B. Finzel, 2022, ACS pharmacology & translational science.

Synergy within structural biology of single crystal optical spectroscopy and X-ray crystallography.

C. Wilmot, Carrie M Wilmot, Teresa De la Mora-Rey, 2007, Current opinion in structural biology.

Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry.

R. Pahl, C. Wilmot, V. Davidson, 2007, Journal of synchrotron radiation.

Crystal structures reveal metal-binding plasticity at the metallo-β-lactamase active site of PqqB from Pseudomonas putida

J. Klinman, C. Wilmot, J. Latham, 2017, JBIC Journal of Biological Inorganic Chemistry.

Structural Analysis of Substrate Specificity in a Copper Amine Oxidase from Hansenula polymorpha

J. Klinman, C. Wilmot, V. J. Klema, 2012 .

Medical implications from the crystal structure of a copper‐containing amine oxidase complexed with the antidepressant drug tranylcypromine

M. McPherson, C. Wilmot, S. Phillips, 2004, FEBS letters.

Hydrocarbon Biosynthesis in Microorganisms

L. Wackett, C. Wilmot, 2015 .

Site-Directed Mutagenesis of Gln103 Reveals the Influence of This Residue on the Redox Properties and Stability of MauG

C. Wilmot, V. Davidson, E. Yukl, 2014, Biochemistry.

Mechanistic possibilities in MauG-dependent tryptophan tryptophylquinone biosynthesis.

C. Wilmot, V. Davidson, L. Jones, 2006, Biochemistry.

Cryocrystallography of metalloprotein reaction intermediates.

C. Wilmot, A. Pearson, 2002, Current opinion in chemical biology.

Defining redox state of X-ray crystal structures by single-crystal ultraviolet-visible microspectrophotometry.

J. Hajdu, C. Wilmot, G. Berglund, 2002, Methods in enzymology.

Crystal structure of the precursor of galactose oxidase: an unusual self-processing enzyme.

M. McPherson, C. Wilmot, S. Phillips, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue.

M. McPherson, C. Wilmot, S. Phillips, 2002, The Biochemical journal.

Structure and mechanism of galactose oxidase. The free radical site.

M. McPherson, C. Wilmot, S. Phillips, 1994, The Journal of biological chemistry.

Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.

M. R. Parsons, M. McPherson, C. Wilmot, 2001, Biochemistry.

The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants.

M. McPherson, C. Wilmot, S. Phillips, 1999, Biochemistry.

Structure and Mechanism of Galactose Oxidase

Michael J. McPherson, Peter F. Knowles, M. McPherson, 2001 .

Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: implications for the mechanism of dioxygen activation.

C. Wilmot, V. Davidson, E. Yukl, 2011, Biochemistry.

Understanding quinone cofactor biogenesis in methylamine dehydrogenase through novel cofactor generation.

C. Wilmot, V. Davidson, A. Ashcroft, 2003, Biochemistry.

In Crystallo Posttranslational Modification Within a MauG/Pre–Methylamine Dehydrogenase Complex

C. Wilmot, V. Davidson, R. Sanishvili, 2010, Science.

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 .

C. Wilmot, V. Davidson, M. Feng, 2010, Biochemistry.

Galactose oxidase: molecular analysis and mutagenesis studies.

M. McPherson, C. Wilmot, S. Phillips, 1993, Biochemical Society transactions.

Crystallization studies of glycosylated and unglycosylated human recombinant interleukin‐2

I. Wilson, C. Wilmot, J. Arevalo, 1992, Proteins.

A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre‐methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis

C. Wilmot, Lyndal M. R. Jensen, N. Abu Tarboush, 2013, FEBS letters.

Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauG.

C. Wilmot, V. Davidson, M. Feng, 2012, Biochemistry.

Oxidative damage in MauG: implications for the control of high-valent iron species and radical propagation pathways.

C. Wilmot, V. Davidson, L. Higgins, 2013, Biochemistry.

Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG.

C. Wilmot, V. Davidson, M. Feng, 2013, Biochemistry.

Further insights into quinone cofactor biogenesis: probing the role of mauG in methylamine dehydrogenase tryptophan tryptophylquinone formation.

C. Wilmot, V. Davidson, L. Jones, 2004, Biochemistry.

A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent FeII/FeIII state and enhances charge resonance stabilization of the bis-FeIV state.

C. Wilmot, V. Davidson, M. Feng, 2015, Biochimica et biophysica acta.

The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis.

C. Wilmot, V. Davidson, M. Feng, 2011, Biochemistry.

A movie of catalysis in the copper-containing quinoenzyme amine oxidase

J. Hajdu, M. McPherson, C. Wilmot, 1999 .

Supporting Online Material Materials and Methods Som Text Figs. S1 to S5 Tables S1 to S3 References Neuronal Competition and Selection during Memory Formation

Alcino J. Silva, J. Guzowski, S. Kushner, 2022 .

The role of OleA His285 in orchestration of long‐chain acyl‐coenzyme A substrates

L. Wackett, C. Wilmot, M. Jensen, 2018, FEBS letters.

Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration.

K. Zahs, K. Ashe, J. Cleary, 2015, Cell reports.

β-Lactone Synthetase Found in the Olefin Biosynthesis Pathway.

L. Wackett, C. Wilmot, J. Richman, 2017, Biochemistry.