What is he best known for?
The fields of study he is best known for:
His main research concerns Protein structure, Crystallography, Stereochemistry, Peptide sequence and Orthomyxoviridae.
In his works, Peter M. Colman undertakes multidisciplinary study on Protein structure and Bcl-2-associated X protein.
He interconnects Folding, Dimer, Molecule and Immunoglobulin Fc Fragments in the investigation of issues within Crystallography.
His Stereochemistry research includes themes of Beta sheet and Crystal structure.
His study in the fields of Sequence alignment under the domain of Peptide sequence overlaps with other disciplines such as Groove.
His Orthomyxoviridae research is multidisciplinary, incorporating elements of Sialic acid and Neuraminidase.
His most cited work include:
- Rational design of potent sialidase-based inhibitors of influenza virus replication. (1526 citations)
- Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function (1521 citations)
- Conformations of immunoglobulin hypervariable regions. (1461 citations)
What are the main themes of his work throughout his whole career to date?
His primary areas of investigation include Neuraminidase, Stereochemistry, Crystallography, Protein structure and Virus.
His research integrates issues of Orthomyxoviridae, Antibody and Active site in his study of Neuraminidase.
His studies in Stereochemistry integrate themes in fields like Immunoglobulin G, Sialidase and Sequence.
His biological study spans a wide range of topics, including Dimer and Molecule.
His Protein structure research includes themes of Peptide sequence, Plasma protein binding, Cell biology and Binding site.
The Virus study which covers Vaccinia that intersects with Inhibitor of apoptosis.
He most often published in these fields:
- Neuraminidase (26.09%)
- Stereochemistry (27.27%)
- Crystallography (26.09%)
What were the highlights of his more recent work (between 2009-2021)?
- Apoptosis (20.55%)
- Cell biology (20.55%)
- Bcl-xL (11.86%)
In recent papers he was focusing on the following fields of study:
Peter M. Colman focuses on Apoptosis, Cell biology, Bcl-xL, Programmed cell death and Plasma protein binding.
His Apoptosis study incorporates themes from Cancer, Cancer research, Mutant, Molecular biology and Virus.
He interconnects Protein structure, Acquired immune system and Dendritic cell in the investigation of issues within Cell biology.
Protein structure and Peptide sequence are commonly linked in his work.
His Bcl-xL research includes elements of Cell culture, Benzoylurea, Peptidomimetic and In vitro.
His work deals with themes such as Bcl-2 family and Binding site, which intersect with Plasma protein binding.
Between 2009 and 2021, his most popular works were:
- Bax Crystal Structures Reveal How Bh3 Domains Activate Bax and Nucleate its Oligomerization to Induce Apoptosis. (361 citations)
- Bax Crystal Structures Reveal How Bh3 Domains Activate Bax and Nucleate its Oligomerization to Induce Apoptosis. (361 citations)
- Structure-guided design of a selective BCL-XL inhibitor (275 citations)
In his most recent research, the most cited papers focused on:
His scientific interests lie mostly in Apoptosis, Cell biology, Programmed cell death, Bcl-2-associated X protein and Protein structure.
The various areas that Peter M. Colman examines in his Apoptosis study include Plasma protein binding, Cancer research, Mutant, B cell and Molecular biology.
His Cell biology study combines topics in areas such as Dendritic cell, Actin cytoskeleton, Cytoskeleton and Cell membrane.
As a part of the same scientific family, Peter M. Colman mostly works in the field of Programmed cell death, focusing on In vitro and, on occasion, Pharmacology, Cell culture and Cancer.
He has researched Protein structure in several fields, including Peptide sequence and Mitochondrion.
His work carried out in the field of Bcl-xL brings together such families of science as Stereochemistry and Sequence.
This overview was generated by a machine learning system which analysed the scientist’s
body of work. If you have any feedback, you can
contact us
here.
