What is he best known for?
The fields of study he is best known for:
Ashley M. Buckle focuses on Biochemistry, Protein structure, Barnase, Crystallography and Stereochemistry.
Protease, Enzyme, Protein folding, GroEL and Serine protease are among the areas of Biochemistry where he concentrates his study.
His work carried out in the field of Protein structure brings together such families of science as Perforin, Complement membrane attack complex, MACPF and Amino acid.
His Crystallography study often links to related topics such as Active site.
His Active site research incorporates themes from Biophysics, Glutamic acid, Reaction rate constant and Binding site.
The study incorporates disciplines such as Tripeptide and Green fluorescent protein in addition to Stereochemistry.
His most cited work include:
- An overview of the serpin superfamily (441 citations)
- PROTEIN-PROTEIN RECOGNITION : CRYSTAL STRUCTURAL ANALYSIS OF A BARNASE-BARSTAR COMPLEX AT 2.0-A RESOLUTION (301 citations)
- T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide. (242 citations)
What are the main themes of his work throughout his whole career to date?
His primary areas of investigation include Biochemistry, Protein structure, Stereochemistry, Crystallography and Computational biology.
The concepts of his Biochemistry study are interwoven with issues in Epitope and Thyroid peroxidase.
His study in Protein structure is interdisciplinary in nature, drawing from both Plasma protein binding, Cell biology, Biophysics, Conformational change and Binding site.
His Stereochemistry study combines topics from a wide range of disciplines, such as Protease, Trypsin inhibitor and Active site.
In general Crystallography study, his work on Crystal structure often relates to the realm of Barnase, thereby connecting several areas of interest.
His Serine protease research focuses on subjects like Proteases, which are linked to Serine, Serpin, Trypsin and Serine Proteinase Inhibitors.
He most often published in these fields:
- Biochemistry (26.46%)
- Protein structure (20.63%)
- Stereochemistry (13.76%)
What were the highlights of his more recent work (between 2018-2021)?
- Biophysics (12.17%)
- Antigen (4.23%)
- Stereochemistry (13.76%)
In recent papers he was focusing on the following fields of study:
Ashley M. Buckle mostly deals with Biophysics, Antigen, Stereochemistry, Scaffold and Monobody.
His work deals with themes such as Genetic code and Protein evolution, which intersect with Biophysics.
His Antigen research includes elements of Thyroiditis, Biochemistry, Ectodomain, Protein precursor and Antibody.
His work carried out in the field of Stereochemistry brings together such families of science as Serine protease, KLK4, Active site, Protein Data Bank and Conformational isomerism.
The subject of his Active site research is within the realm of Enzyme.
His Beta sheet study contributes to a more complete understanding of Protein structure.
Between 2018 and 2021, his most popular works were:
- Protein engineering: the potential of remote mutations (22 citations)
- Denisovan, modern human and mouse TNFAIP3 alleles tune A20 phosphorylation and immunity. (21 citations)
- Development and Differentiation in Monobodies Based on the Fibronectin Type 3 Domain (11 citations)
In his most recent research, the most cited papers focused on:
His primary areas of study are Biophysics, Antigen, Directed evolution, Computational biology and Serine protease.
Ashley M. Buckle has researched Biophysics in several fields, including Disulphide bonds, Tissue distribution, Fibronectin and Monobody.
His biological study spans a wide range of topics, including Amino acid, Protein design, Protein chemistry, Rational engineering and Protein engineering.
His Computational biology research is multidisciplinary, relying on both Homologous chromosome, Ancestral reconstruction, Protein stability and Target protein.
His Serine protease research integrates issues from Trypsin inhibitor, Beta sheet, Stereochemistry and Active site.
His research links Protein structure with Protease.
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