What is he best known for?
The fields of study he is best known for:
Christopher M. Dobson focuses on Protein folding, Biochemistry, Crystallography, Protein structure and Fibril.
His Protein folding research incorporates elements of Biophysics, Circular dichroism, Folding, Computational biology and Kinetics.
His Biochemistry research incorporates themes from Amyloid disease and Amyloid fibril.
His research integrates issues of Nuclear magnetic resonance spectroscopy, Protein secondary structure and Hydrogen bond in his study of Crystallography.
As a part of the same scientific family, Christopher M. Dobson mostly works in the field of Protein structure, focusing on Acylphosphatase and, on occasion, Mutation.
His Fibril study which covers Amyloid that intersects with Sequence, Amyloidosis, Monomer and Molecule.
His most cited work include:
- Protein Misfolding, Functional Amyloid, and Human Disease (4716 citations)
- Protein folding and misfolding (3516 citations)
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. (2076 citations)
What are the main themes of his work throughout his whole career to date?
Christopher M. Dobson mostly deals with Biophysics, Protein folding, Crystallography, Biochemistry and Amyloid.
His Biophysics research focuses on Protein aggregation and how it relates to In vitro.
His Protein folding research integrates issues from Protein structure, Computational biology and Folding.
His study explores the link between Crystallography and topics such as Nuclear magnetic resonance spectroscopy that cross with problems in Analytical chemistry.
The various areas that he examines in his Biochemistry study include Amyloid disease and Alpha-synuclein.
His Amyloid study frequently draws connections between related disciplines such as Nucleation.
He most often published in these fields:
- Biophysics (28.27%)
- Protein folding (26.80%)
- Crystallography (25.51%)
What were the highlights of his more recent work (between 2014-2021)?
- Biophysics (28.27%)
- Protein aggregation (16.11%)
- Amyloid (17.40%)
In recent papers he was focusing on the following fields of study:
His primary areas of study are Biophysics, Protein aggregation, Amyloid, Protein folding and Cell biology.
A large part of his Biophysics studies is devoted to Fibril.
Christopher M. Dobson usually deals with Fibril and limits it to topics linked to Kinetics and Nucleation.
Protein aggregation is a primary field of his research addressed under Biochemistry.
His studies in Amyloid integrate themes in fields like Microfluidics and Fluorescence.
Protein folding connects with themes related to Protein structure in his study.
Between 2014 and 2021, his most popular works were:
- Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade (873 citations)
- Widespread Proteome Remodeling and Aggregation in Aging C. elegans (311 citations)
- Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation (290 citations)
In his most recent research, the most cited papers focused on:
His primary areas of investigation include Biophysics, Protein aggregation, Alpha-synuclein, Biochemistry and Protein folding.
His research in Biophysics is mostly concerned with Fibril.
His studies deal with areas such as Proteome, Proteostasis, Chaperone and Drug discovery as well as Protein aggregation.
His research investigates the link between Biochemistry and topics such as Neurodegeneration that cross with problems in Caenorhabditis elegans.
His work deals with themes such as Amyloid fibril, Neuroscience, Protein structure, Computational biology and Peptide, which intersect with Protein folding.
His Protein structure research includes elements of Folding, Biomolecule, Nuclear magnetic resonance spectroscopy and Ribosome.
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