What is he best known for?
The fields of study he is best known for:
The scientist’s investigation covers issues in Biophysics, Nanotechnology, Förster resonance energy transfer, Analytical chemistry and Scanning ion-conductance microscopy.
His Biophysics research is multidisciplinary, relying on both Single-molecule experiment, Alpha-synuclein, Membrane, Cell membrane and Protein folding.
His Nanotechnology study combines topics from a wide range of disciplines, such as Optical microscope and Fluorescence.
His work deals with themes such as Immunoassay, Microfluidics, Molecule and DNA, which intersect with Fluorescence.
David Klenerman has researched Förster resonance energy transfer in several fields, including Quantum dot, Crystallography, Fibril and Arrhenius equation.
His Nanoscopic scale research includes themes of Electrode and Microscopy.
His most cited work include:
- Accurate whole human genome sequencing using reversible terminator chemistry (3039 citations)
- Arrayed biomolecules and their use in sequencing (545 citations)
- Direct observation of the interconversion of normal and toxic forms of α-synuclein. (510 citations)
What are the main themes of his work throughout his whole career to date?
David Klenerman focuses on Biophysics, Nanotechnology, Cell biology, Fluorescence and Microscopy.
His Biophysics research incorporates themes from Membrane, Protein aggregation, Single-molecule experiment and Alpha-synuclein.
His Nanotechnology study combines topics in areas such as Molecule and Single-cell analysis.
His work in Cell biology tackles topics such as Receptor which are related to areas like T-cell receptor.
His research in Fluorescence intersects with topics in DNA and Analytical chemistry.
His study in the field of Scanning ion-conductance microscopy is also linked to topics like Conductance.
He most often published in these fields:
- Biophysics (31.25%)
- Nanotechnology (17.71%)
- Cell biology (16.15%)
What were the highlights of his more recent work (between 2017-2021)?
- Biophysics (31.25%)
- Protein aggregation (9.90%)
- Cell biology (16.15%)
In recent papers he was focusing on the following fields of study:
His primary scientific interests are in Biophysics, Protein aggregation, Cell biology, Alpha-synuclein and Amyloid.
His Biophysics research includes elements of Membrane, Lipid bilayer, In vitro and Fluorescence.
His Fluorescence study which covers Protein folding that intersects with Amyloidogenic Proteins.
The concepts of his Protein aggregation study are interwoven with issues in Neuroscience, Neurodegeneration, Disease, Endogeny and Computational biology.
His Cell biology study integrates concerns from other disciplines, such as Inflammation, Receptor, Cell and Genetically modified mouse.
His biological study spans a wide range of topics, including Peptide, Early detection and Monomer.
Between 2017 and 2021, his most popular works were:
- FUS Phase Separation Is Modulated by a Molecular Chaperone and Methylation of Arginine Cation-π Interactions (294 citations)
- α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease (162 citations)
- Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms (96 citations)
In his most recent research, the most cited papers focused on:
His primary areas of investigation include Biophysics, Protein aggregation, Amyloid, Fibril and Alpha-synuclein.
The various areas that he examines in his Biophysics study include In vitro, Fluorescence, Oligomer, Neurodegeneration and Membrane.
His Fluorescence research is multidisciplinary, incorporating elements of Protein dynamics, Membrane protein and T-cell receptor.
His Protein aggregation study is concerned with the larger field of Cell biology.
In his research, Amyloid fibril and Single-molecule FRET is intimately related to Monomer, which falls under the overarching field of Amyloid.
His research integrates issues of Substantia nigra, ATP synthase, Immunology and Mitochondrial permeability transition pore in his study of Alpha-synuclein.
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