I. Clifton

发表

X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates.

J. Elkins, M. J. Ryle, R. Hausinger, 2002, Biochemistry.

Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2).

J. Zondlo, R. Syed, N. Oldham, 2006, Proceedings of the National Academy of Sciences of the United States of America.

The recording and analysis of synchrotron X-radiation Laue diffraction photographs

John R. Helliwell, Miroslav Z. Papiz, J. W. Campbell, 1989 .

Structural and biochemical analyses reveal how ornithine acetyl transferase binds acidic and basic amino acid substrates.

D. Ivison, C. Domene, C. Schofield, 2011, Organic & biomolecular chemistry.

Selective Inhibitors of the JMJD2 Histone Demethylases: Combined Nondenaturing Mass Spectrometric Screening and Crystallographic Approaches†

Christopher J. Schofield, Udo Oppermann, Nathan R. Rose, 2010, Journal of medicinal chemistry.

Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate.

N. Oldham, G. Jeschke, C. Schofield, 2005, Molecular bioSystems.

Ribosomal Oxygenases are Structurally Conserved from Prokaryotes to Humans

K. Kavanagh, F. von Delft, U. Oppermann, 2014, Nature.

Crystal structure of human thymidylate synthase: a structural mechanism for guiding substrates into the active site.

R. Stroud, C. Schiffer, D. Santi, 1995, Biochemistry.

Towards time-resolved diffraction studies with glycogen phosphorylase.

G. P. Reid, J. Hajdu, L. Johnson, 1991, Ciba Foundation symposium.

‘Chemical co-substrate rescue’ of phytanoyl-CoA 2-hydroxylase mutants causing Refsum’s Disease

M. D. Lloyd, M. Mukherji, A. Wierzbicki, 2001 .

Structural basis for binding of cyclic 2-oxoglutarate analogues to factor-inhibiting hypoxia-inducible factor.

A. Conejo-García, C. Schofield, K. Hewitson, 2010, Bioorganic & medicinal chemistry letters.

Spectroscopic studies reveal details of substrate-induced conformational changes distant from the active site in isopenicillin N synthase

C. Schofield, A. Tumber, W. Myers, 2022, The Journal of biological chemistry.

Crystal structure determination of an organometallic compound from synchrotron radiation Laue diffraction photographs

J. W. Campbell, I. Clifton, M. Harding, 1988 .

Synchrotron X-radiation protein crystallography: CEA film absorption factor as a function of wavelength 0.3≤λ≤2Å

R. Liddington, J. Helliwell, G. Diakun, 1985 .

Recent successes in time-resolved protein crystallography.

R. Neutze, I. Clifton, R. Wilmouth, 2000, Natural product reports.

On the limitations of the Laue method when applied to crystals of macromolecules

Steven C. Almo, Soichi Wakatsuki, Gregory A. Petsko, 1992 .

Structural studies on the reaction of isopenicillin N synthase with the substrate analogue δ -( L - α -aminoadipoyl)- L -cysteinyl- D - α -aminobutyrate

P. Roach, C. Schofield, P. Rutledge, 2003 .

Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2).

J. Zondlo, R. Syed, N. Oldham, 2006, Proceedings of the National Academy of Sciences of the United States of America.

Crystallization and preliminary X‐ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans

J. Hajdu, P. Roach, C. Schofield, 1995, Protein science : a publication of the Protein Society.

Resistance to the isocitrate dehydrogenase 1 mutant inhibitor ivosidenib can be overcome by alternative dimer-interface binding inhibitors

F. Armstrong, C. Schofield, J. McCullagh, 2022, Nature Communications.

Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates

Samuel T. Cahill, C. Fishwick, C. Schofield, 2016, Nature Communications.

The reaction cycle of isopenicillin N synthase observed by X-ray diffraction

P. Roach, P. Rutledge, N. Burzlaff, 1999, Nature.

13C-Carbamylation as a mechanistic probe for the inhibition of class D β-lactamases by avibactam and halide ions.

Samuel T. Cahill, C. Domene, C. Schofield, 2017, Organic & biomolecular chemistry.

'pH-jump' crystallographic analyses of gamma-lactam-porcine pancreatic elastase complexes.

P. A. Wright, C. Schofield, C J Schofield, 2000, The Biochemical journal.

Terminally Truncated Isopenicillin N Synthase Generates a Dithioester Product: Evidence for a Thioaldehyde Intermediate during Catalysis and a New Mode of Reaction for Non‐Heme Iron Oxidases

C. Schofield, P. Rutledge, T. Claridge, 2017, Chemistry.

Unexpected Oxidation of a Depsipeptide Substrate Analogue in Crystalline Isopenicillin N Synthase

P. Rutledge, I. Clifton, J. Baldwin, 2006, Chembiochem : a European journal of chemical biology.

Active-site-mediated elimination of hydrogen fluoride from a fluorinated substrate analogue by isopenicillin N synthase.

P. Rutledge, I. Clifton, J. Baldwin, 2004, The Biochemical journal.

Crystal Structure of Carbapenem Synthase (CarC)*

Maya Topf, Christopher J Schofield, M. Topf, 2003, Journal of Biological Chemistry.

Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.

C. Schofield, M. McDonough, I. Clifton, 2006, Journal of inorganic biochemistry.

Structural studies on human 2-oxoglutarate dependent oxygenases.

C. Schofield, R. Chowdhury, M. McDonough, 2010, Current opinion in structural biology.

Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana.

C. Schofield, I. Clifton, R. Welford, 2002, Structure.

Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-β-lactamase inhibition.

C. Schofield, Sheng-Yong Yang, J. Brem, 2017, Chemical communications.

Unique binding of a non-natural L,L,L-substrate by isopenicillin N synthase.

P. Rutledge, I. Clifton, J. Baldwin, 2005, Biochemical and biophysical research communications.

Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes

Geoffrey J. Barton, Peter L. Roach, Christopher J. Schofield, 1995, Nature.

Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme.

C. Schofield, Jingshan Ren, I. Clifton, 2004, Chemistry & biology.

Kinetic and crystallographic analysis of complexes formed between elastase and peptides from beta-casein.

P. A. Wright, C. Schofield, I. Clifton, 2001, European journal of biochemistry.

Structure of a specific acyl-enzyme complex formed between β-casomorphin-7 and porcine pancreatic elastase

J. Hajdu, C. Robinson, N. Westwood, 1997, Nature Structural Biology.

Interactions of isopenicillin N synthase with cyclopropyl-containing substrate analogues reveal new mechanistic insight.

J. Elkins, P. Roach, P. Rutledge, 2007, Biochemistry.

The oncometabolite 2‐hydroxyglutarate inhibits histone lysine demethylases

R. Klose, P. Ratcliffe, Eleanor A. L. Bagg, 2011, EMBO reports.

Crystal structure of a clavaminate synthase–Fe(II)–2‐oxoglutarate–substrate–NO complex: evidence for metal centred rearrangements

Christopher J Schofield, Karl Harlos, K. Harlos, 2002, FEBS letters.

Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases.

K. Harlos, C. Schofield, I. Clifton, 2001, European journal of biochemistry.

Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation.

J. Hajdu, P. Roach, C. Schofield, 1997, Nature.

Proteins of the penicillin biosynthesis pathway.

J. Hajdu, P. Roach, C. Schofield, 1997, Current opinion in structural biology.

Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1).

J. Boucher, B. Kessler, C. Schofield, 2011, Journal of molecular biology.

Studies on non-haem ferrous-dependent oxygenases and oxidases.

M. D. Lloyd, J. Hajdu, P. Roach, 1997, Biochemical Society transactions.

Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of a hydrolytic enzyme in clavulanic acid biosynthesis.

C. Robinson, J. Elkins, C. Schofield, 2002, The Biochemical journal.

X-ray free-electron laser studies reveal correlated motion during isopenicillin N synthase catalysis

M. Hunter, Y. Joti, K. Tono, 2021, Science Advances.

Structure of isopenicillinN synthase complexed with substrate and the mechanism ofpenicillin formation

J. Hajdu, P. Roach, C. Schofield, 1997, Nature.

X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate

Karl Edman, Christopher J. Schofield, Thomas R. Schneider, 2001, Nature Structural Biology.

Structure-function analysis of phytanoyl-CoA 2-hydroxylase mutations causing Refsum's disease.

M. D. Lloyd, M. Mukherji, A. Wierzbicki, 2001, Human molecular genetics.

Structural and Mechanistic Studies on the Inhibition of the Hypoxia-inducible Transcription Factor Hydroxylases by Tricarboxylic Acid Cycle Intermediates*

N. Oldham, C. Schofield, K. Hewitson, 2007, Journal of Biological Chemistry.

Alteration of the Co-substrate Selectivity of Deacetoxycephalosporin C Synthase

M. D. Lloyd, J. Frère, A. Dubus, 2001, The Journal of Biological Chemistry.

Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS).

M. D. Lloyd, K. Harlos, C. Schofield, 2001, Journal of molecular biology.

Anatomy of a simple acyl intermediate in enzyme catalysis: combined biophysical and modeling studies on ornithine acetyl transferase.

C. Wharton, C. Domene, C. Schofield, 2009, Journal of the American Chemical Society.

Macromolecular structure, function and dynamics by fast crystallography with synchrotron radiation

V. Fülöp, J. Hajdu, I. Andersson, 1991 .

Anaerobic crystallisation of an isopenicillin N synthase.Fe(II).substrate complex demonstrated by X-ray studies.

J. Hajdu, R. Strange, P. Roach, 1996, European journal of biochemistry.

The Interaction of Isopenicillin N Synthase with Homologated Substrate Analogues δ‐(L‐α‐Aminoadipoyl)‐L‐homocysteinyl‐D‐Xaa Characterised by Protein Crystallography

P. Rutledge, I. Clifton, J. Baldwin, 2013, Chembiochem : a European journal of chemical biology.

The crystal structure of isopenicillin N synthase with a dipeptide substrate analogue.

P. Rutledge, I. Clifton, J. Baldwin, 2013, Archives of biochemistry and biophysics.

The crystal structure of isopenicillin N synthase with δ-((L)-α-aminoadipoyl)-(L)-cysteinyl-(D)-methionine reveals thioether coordination to iron.

P. Rutledge, I. Clifton, J. Baldwin, 2011, Archives of biochemistry and biophysics.

Isopenicillin N Synthase Binds δ‐(L‐α‐Aminoadipoyl)‐L‐Cysteinyl‐D‐Thia‐allo‐Isoleucine through both Sulfur Atoms

P. Rutledge, I. Clifton, J. Baldwin, 2011, Chembiochem : a European journal of chemical biology.

Crystallographic studies on the binding of selectively deuterated LLD- and LLL-substrate epimers by isopenicillin N synthase.

Jeanette E. Stok, P. Rutledge, I. Clifton, 2010, Biochemical and biophysical research communications.

The crystal structure of an LLL-configured depsipeptide substrate analogue bound to isopenicillin N synthase.

Jeanette E. Stok, P. Rutledge, I. Clifton, 2010, Organic & biomolecular chemistry.

Structural Studies on the Reaction of Isopenicillin N Synthase with a Sterically Demanding Depsipeptide Substrate Analogue

P. Rutledge, I. Clifton, J. Baldwin, 2009, Chembiochem : a European journal of chemical biology.

A Cyclobutanone Analogue Mimics Penicillin in Binding to Isopenicillin N Synthase

P. Rutledge, I. Clifton, J. Baldwin, 2007, Chembiochem : a European journal of chemical biology.

Crystallographic studies on the reaction of isopenicillin N synthase with an unsaturated substrate analogue.

J. Elkins, P. Roach, P. Rutledge, 2003, Organic & biomolecular chemistry.

Alternative oxidation by isopenicillin N synthase observed by X-ray diffraction.

J. Elkins, P. Roach, J. M. Ogle, 2001, Chemistry & biology.

[Evaluation of Laue diffraction patterns.

S. Wakatsuki, E M Duke, I. Clifton, 1997, Methods in enzymology.

Laue crystallography: application to virus crystals.

J. W. Campbell, R. Liddington, J. Hajdu, 1989, Basic life sciences.

Mechanisms and structures of crotonase superfamily enzymes – How nature controls enolate and oxyanion reactivity

C. Schofield, I. Clifton, R. B. Hamed, 2008, Cellular and Molecular Life Sciences.

Calcium binding sites in tomato bushy stunt virus visualized by Laue crystallography.

J. W. Campbell, R. Liddington, J. Hajdu, 1990, Journal of molecular biology.

Millisecond X-ray diffraction and the first electron density map from Laue photographs of a protein crystal

J. W. Campbell, John W. Campbell, Ian J. Clifton, 1987, Nature.

Laue diffraction study on the structure of cytochrome c peroxidase compound I.

V. Fülöp, J. Hajdu, R. P. Phizackerley, 1994, Structure.

Inhibition of elastase by N-sulfonylaryl beta-lactams: anatomy of a stable acyl-enzyme complex.

N. Westwood, C. Schofield, R. Aplin, 1998, Biochemistry.

Crystallographic and mass spectrometric analyses of a tandem GNAT protein from the clavulanic acid biosynthesis pathway

T. Brown, C. Schofield, K. Hewitson, 2010, Proteins.

The crystal structure of an isopenicillin N synthase complex with an ethereal substrate analogue reveals water in the oxygen binding site

P. Rutledge, I. Clifton, J. Baldwin, 2013, FEBS letters.

New sources, newer detectors, old methods — the future of protein crystallography at synchrotrons

Janos Hajdu, Soichi Wakatsuki, Ian J. Clifton, 1994 .

CHAPTER 2:Introduction to Structural Studies on 2-Oxoglutarate-Dependent Oxygenases and Related Enzymes

C. Schofield, T. Leissing, R. Chowdhury, 2015 .

Isopenicillin N synthase mediates thiolate oxidation to sulfenate in a depsipeptide substrate analogue: implications for oxygen binding and a link to nitrile hydratase?

P. Rutledge, I. Clifton, J. Baldwin, 2008, Journal of the American Chemical Society.

Structural and mechanistic studies on anthocyanidin synthase catalysed oxidation of flavanone substrates: the effect of C-2 stereochemistry on product selectivity and mechanism.

Christopher J Schofield, Stuart C. Wilson, C. Schofield, 2005, Organic & biomolecular chemistry.