Matthew C. J. Wilce mostly deals with Active site, Biochemistry, T-cell receptor, Protein structure and Stereochemistry. His studies deal with areas such as Tyrosine, Lyase, Serine and Binding site as well as Active site. His research brings together the fields of Microbiology and Biochemistry.
His T-cell receptor research includes elements of Human leukocyte antigen and Major histocompatibility complex. His research in Protein structure intersects with topics in Glutathione S-transferase, Crystallography, Protein subunit and Amine gas treating. Matthew C. J. Wilce has researched Stereochemistry in several fields, including Glutathione, Isozyme, Catalysis and Molecular geometry.
His primary areas of study are Biochemistry, Protein structure, Crystallography, Stereochemistry and Binding site. His research in Protein structure intersects with topics in Peptide sequence, Protein subunit, Peptide and Drug discovery. Matthew C. J. Wilce works mostly in the field of Peptide sequence, limiting it down to topics relating to Cell biology and, in certain cases, Receptor.
The Crystallography study combines topics in areas such as Crystallization, Molecule and Green fluorescent protein. His Stereochemistry study combines topics in areas such as Amino acid, Haloalkane dehalogenase, Dehalogenase, Isothermal titration calorimetry and Molecular replacement. His Binding site study integrates concerns from other disciplines, such as RNA, Glutathione S-transferase, Biophysics, Molecular biology and Base pair.
His scientific interests lie mostly in Biochemistry, Biotin, DNA ligase, Protein structure and Binding site. Biochemistry is represented through his Enzyme, GRB7, Plasma protein binding, Leucine zipper and Binding domain research. The study incorporates disciplines such as Acetyl-CoA carboxylase, Isozyme, Small molecule and Staphylococcus aureus in addition to Biotin.
His work deals with themes such as Triazole, Repressor and Ligand, which intersect with DNA ligase. His Protein structure research includes themes of TXNIP, Crystallography, Protein folding, Receptor and Drug discovery. His Binding site research integrates issues from RNA, Molecular biology, Hormone, Internal medicine and Cell biology.
His primary areas of investigation include Biochemistry, Biotin, DNA ligase, Cell biology and Plasma protein binding. Peptide sequence, Target protein, GRB7, RIG-I and Peptide are the subjects of his Biochemistry studies. His DNA ligase research is multidisciplinary, incorporating elements of Triazole and Ligand.
His Triazole study deals with Drug discovery intersecting with Protein structure. In Protein structure, Matthew C. J. Wilce works on issues like HLA-G, which are connected to Stereochemistry. His work focuses on many connections between Cell biology and other disciplines, such as RNA, that overlap with his field of interest in Molecular biology, Binding site and Retinoic acid.
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Structure and function of glutathione S-transferases
Matthew C.J. Wilce;Michael W. Parker.
Biochimica et Biophysica Acta (1994)
CD1d–lipid-antigen recognition by the semi-invariant NKT T-cell receptor
Natalie Borg;Kwok Soon Wun;Lars Kjer-Nielsen;Matthew Charles James Wilce.
Mutations in the skeletal muscle α-actin gene in patients with actin myopathy and nemaline myopathy
Kristen J. Nowak;Kristen J. Nowak;Duangrurdee Wattanasirichaigoon;Hans H. Goebel;Matthew Wilce.
Nature Genetics (1999)
AB5 subtilase cytotoxin inactivates the endoplasmic reticulum chaperone BiP.
Adrienne W Paton;Travis Clarke Beddoe;Cheleste M Thorpe;James Whisstock.
Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 å resolution
Vinay Kumar;David M. Dooley;Hans C. Freeman;J. Mitchell Guss.
T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide.
Fleur Elizabeth Tynan;Scott R Burrows;Ashley Maurice Buckle;Craig Steven Clements.
Nature Immunology (2005)
Crystal Structures of the Copper-Containing Amine Oxidase from Arthrobacter globiformis in the Holo and Apo Forms: Implications for the Biogenesis of Topaquinone†,‡
M. C. J. Wilce;D. M. Dooley;H. C. Freeman;J. M. Guss.
Crystal structure of a theta-class glutathione transferase.
M. C. J. Wilce;P. G. Board;S. C. Feil;M. W. Parker.
The EMBO Journal (1995)
A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule
Fleur Elizabeth Tynan;Hugh Harrington Reid;Lars Kjer-Nielsen;John J Miles.
Nature Immunology (2007)
T Cell Allorecognition via Molecular Mimicry
Whitney Alison Macdonald;Zhenjun Chen;Stephanie Gras;Julia Kate Archbold.
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