2022 - Breakthrough Prize in Life Sciences for the development of a robust and affordable method to determine DNA sequences on a massive scale, which has transformed the practice of science and medicine.
2012 - Fellow of the Royal Society, United Kingdom
2007 - Interdisciplinary Prize, Royal Society of Chemistry (UK)
Fellow of The Academy of Medical Sciences, United Kingdom
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.
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.
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.
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.
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.
Accurate whole human genome sequencing using reversible terminator chemistry
David R. Bentley;Shankar Balasubramanian;Harold P. Swerdlow;Harold P. Swerdlow;Geoffrey P. Smith.
Arrayed biomolecules and their use in sequencing
Shankar Balasubramanian;David Klenerman;Colin Barnes;Mark Allen Osborne.
Direct observation of the interconversion of normal and toxic forms of α-synuclein.
Nunilo Cremades;Samuel I.A. Cohen;Emma Deas;Andrey Y. Abramov.
Nanoscale live-cell imaging using hopping probe ion conductance microscopy.
Pavel Novak;Chao Li;Andrew I Shevchuk;Ruben Stepanyan.
Nature Methods (2009)
Studies on the structure and dynamics of the human telomeric G quadruplex by single-molecule fluorescence resonance energy transfer
Liming Ying;Jeremy J. Green;Haitao Li;David Klenerman.
Proceedings of the National Academy of Sciences of the United States of America (2003)
FUS Phase Separation Is Modulated by a Molecular Chaperone and Methylation of Arginine Cation-π Interactions
Seema Qamar;Guo Zhen Wang;Suzanne J. Randle;Francesco Simone Ruggeri.
Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation
Serene W. Chen;Srdja Drakulic;Emma Deas;Myriam Ouberai.
Proceedings of the National Academy of Sciences of the United States of America (2015)
The 2015 super-resolution microscopy roadmap
Stefan W. Hell;Stefan W. Hell;Steffen J. Sahl;Mark Bates;Xiaowei Zhuang.
Journal of Physics D (2015)
Multifunctional nanoprobes for nanoscale chemical imaging and localized chemical delivery at surfaces and interfaces.
Yasufumi Takahashi;Andrew I. Shevchuk;Pavel Novak;Yanjun Zhang.
Angewandte Chemie (2011)
The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β 1−40 peptide
Priyanka Narayan;Angel Orte;Angel Orte;Richard W Clarke;Benedetta Bolognesi.
Nature Structural & Molecular Biology (2012)
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