What is he best known for?
The fields of study he is best known for:
Biochemistry, Kallikrein, Stereochemistry, Protein structure and Trypsin are his primary areas of study.
His Biochemistry study frequently draws connections between adjacent fields such as Myelin basic protein.
His work on Tissue Kallikreins as part of general Kallikrein research is frequently linked to Protease-activated receptor, thereby connecting diverse disciplines of science.
His Stereochemistry study combines topics in areas such as Alpha helix, Helix, Alanine and Hydrogen bond.
His study in Protein structure is interdisciplinary in nature, drawing from both Crystallography, Single crystal, Water dimer, Mutant and Computational biology.
His studies in Crystallography integrate themes in fields like X-ray crystallography and Molecular physics.
His most cited work include:
- Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. (801 citations)
- Structural basis of amino acid alpha helix propensity. (390 citations)
- Cloning and Expression of the Gene for Pro-urokinase in Escherichia coli (224 citations)
What are the main themes of his work throughout his whole career to date?
Michael Blaber mostly deals with Biochemistry, Crystal structure, Mutant, Kallikrein and Stereochemistry.
Crystal structure is a subfield of Crystallography that Michael Blaber tackles.
His work on Globular protein as part of general Crystallography research is often related to Side chain, thus linking different fields of science.
His Mutant research focuses on subjects like Biophysics, which are linked to Function.
The study incorporates disciplines such as Proteases, Protease and Immunology in addition to Kallikrein.
His Stereochemistry research includes elements of Protein engineering, Cofactor, Enzyme, Hydrogen bond and Protein structure.
He most often published in these fields:
- Biochemistry (35.68%)
- Crystal structure (21.60%)
- Mutant (20.66%)
What were the highlights of his more recent work (between 2014-2021)?
- Fibroblast growth factor (12.21%)
- Stereochemistry (18.31%)
- Biochemistry (35.68%)
In recent papers he was focusing on the following fields of study:
Michael Blaber mainly focuses on Fibroblast growth factor, Stereochemistry, Biochemistry, Crystallography and Protein folding.
His research integrates issues of Glucosyltransferase and Glucosyltransferases in his study of Stereochemistry.
His Biochemistry study is mostly concerned with Amino acid, Kallikrein, Mutation, Fibroblast growth factor receptor 2 and Fibroblast growth factor receptor.
Protein tertiary structure and Serine is closely connected to Peptide sequence in his research, which is encompassed under the umbrella topic of Amino acid.
His work in the fields of Crystal structure overlaps with other areas such as Immunoglobulin Fab Fragments.
The various areas that he examines in his Protein folding study include Protein design and Protein secondary structure.
Between 2014 and 2021, his most popular works were:
- Structural basis for acceptor-substrate recognition of UDP-glucose: anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea (37 citations)
- Structural basis for acceptor-substrate recognition of UDP-glucose: anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea (37 citations)
- Accelerated healing in NONcNZO10/LtJ type 2 diabetic mice by FGF-1. (20 citations)
In his most recent research, the most cited papers focused on:
Michael Blaber focuses on Stereochemistry, Amino acid, Biochemistry, Mutation and Petunidin.
His Stereochemistry research is multidisciplinary, incorporating perspectives in Hydrophobic residue and Protein evolution.
His Amino acid study combines topics from a wide range of disciplines, such as Folding, Peptide sequence and Protein folding.
His research on Peptide sequence also deals with topics like
- Serine that connect with fields like Fibroblast growth factor and Heparin,
- Proteolytic enzymes which intersects with area such as Binding site.
Michael Blaber has included themes like Protein engineering and Plasma protein binding in his Mutation study.
He interconnects Protein structure, Stability study, Protein aggregation and Hydrogen bond in the investigation of issues within Protein engineering.
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