What is he best known for?
The fields of study he is best known for:
Tuomas P. J. Knowles mainly focuses on Biophysics, Fibril, Protein aggregation, Nucleation and Amyloid.
His Biophysics research integrates issues from Plasma protein binding, Amyloid beta, Peptide and Chaperone.
His Fibril research is multidisciplinary, incorporating perspectives in Heat shock protein, Protein secondary structure, Crystallography, Förster resonance energy transfer and Synuclein.
His studies in Protein aggregation integrate themes in fields like In vitro, Lipid bilayer and Chemical chaperone.
His Nucleation study combines topics in areas such as Monomer, Chemical kinetics, Kinetics, Statistical physics and Elongation.
His Amyloid study combines topics from a wide range of disciplines, such as Protein structure, Nanotechnology and Quartz crystal microbalance.
His most cited work include:
- The amyloid state and its association with protein misfolding diseases. (1240 citations)
- An analytical solution to the kinetics of breakable filament assembly (750 citations)
- Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism (727 citations)
What are the main themes of his work throughout his whole career to date?
His primary scientific interests are in Biophysics, Protein aggregation, Fibril, Amyloid and Nanotechnology.
His Biophysics research includes elements of Nucleation, Biochemistry, Peptide, Protein folding and Kinetics.
The various areas that Tuomas P. J. Knowles examines in his Nucleation study include Chemical physics and Elongation.
His Protein aggregation research is multidisciplinary, incorporating elements of Protein structure, In vitro and Alpha-synuclein.
His Fibril research incorporates themes from Amyloid fibril, Plasma protein binding, Crystallography, Oligomer and Monomer.
The study incorporates disciplines such as Supramolecular chemistry and Molecule in addition to Nanotechnology.
He most often published in these fields:
- Biophysics (38.89%)
- Protein aggregation (24.57%)
- Fibril (20.09%)
What were the highlights of his more recent work (between 2019-2021)?
- Biophysics (38.89%)
- Microfluidics (18.16%)
- Protein aggregation (24.57%)
In recent papers he was focusing on the following fields of study:
Tuomas P. J. Knowles spends much of his time researching Biophysics, Microfluidics, Protein aggregation, Peptide and Amyloid.
His biological study focuses on Fibril.
His Microfluidics research incorporates elements of Biological system, Molecule, Chemical engineering and Electrophoresis.
He interconnects Limiting, Membrane, Lipid bilayer and Toxicity in the investigation of issues within Protein aggregation.
His Peptide study incorporates themes from Mechanism of action, In silico, Structure–activity relationship and Rational design.
Tuomas P. J. Knowles combines subjects such as Air water interface, Kinetics and Protein folding with his study of Amyloid.
Between 2019 and 2021, his most popular works were:
- Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide. (50 citations)
- Half a century of amyloids: past, present and future (38 citations)
- The Amyloid Phenomenon and Its Significance in Biology and Medicine (38 citations)
In his most recent research, the most cited papers focused on:
Tuomas P. J. Knowles mainly investigates Biophysics, Peptide, Microfluidics, Phase and Amyloid.
Tuomas P. J. Knowles studies Fibril, a branch of Biophysics.
His Peptide study also includes fields such as
- Bapineuzumab which intersects with area such as Structure–activity relationship, Amyloid cascade, Kinetic analysis and Biochemistry,
- Mechanism of action and related Drug delivery, Antimicrobial, Tissue engineering and In vivo.
His research in Microfluidics intersects with topics in Protein Interaction Networks, Biological system, Shear and Human proteome project.
His work carried out in the field of Amyloid brings together such families of science as Ultrastructure and Engineering ethics.
His study looks at the relationship between Toxicity and topics such as Cell, which overlap with Membrane and Protein aggregation.
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