What is he best known for?
The fields of study he is best known for:
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 most cited work include:
- Structure and function of glutathione S-transferases (493 citations)
- CD1d–lipid-antigen recognition by the semi-invariant NKT T-cell receptor (478 citations)
- Mutations in the skeletal muscle α-actin gene in patients with actin myopathy and nemaline myopathy (331 citations)
What are the main themes of his work throughout his whole career to date?
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.
He most often published in these fields:
- Biochemistry (38.42%)
- Protein structure (22.60%)
- Crystallography (21.47%)
What were the highlights of his more recent work (between 2011-2021)?
- Biochemistry (38.42%)
- Biotin (10.17%)
- DNA ligase (9.04%)
In recent papers he was focusing on the following fields of study:
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.
Between 2011 and 2021, his most popular works were:
- Macrophage migration inhibitory factor is required for NLRP3 inflammasome activation (59 citations)
- Sequence requirements for RNA binding by HuR and AUF1. (49 citations)
- Structure, function and selective inhibition of bacterial acetyl-coa carboxylase. (45 citations)
In his most recent research, the most cited papers focused on:
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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