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Theory and applications of differential scanning fluorimetry in early-stage drug discovery
K Gao, R Oerlemans, MR Groves - Biophysical reviews, 2020 - Springer
Differential scanning fluorimetry (DSF) is an accessible, rapid, and economical biophysical
technique that has seen many applications over the years, ranging from protein folding state …
technique that has seen many applications over the years, ranging from protein folding state …
[HTML][HTML] MicroScale Thermophoresis: Interaction analysis and beyond
M Jerabek-Willemsen, T André, R Wanner… - Journal of Molecular …, 2014 - Elsevier
MicroScale Thermophoresis (MST) is a powerful technique to quantify biomolecular
interactions. It is based on thermophoresis, the directed movement of molecules in a …
interactions. It is based on thermophoresis, the directed movement of molecules in a …
Light-driven eco-evolutionary dynamics in a synthetic replicator system
Darwinian evolution involves the inheritance and selection of variations in reproducing
entities. Selection can be based on, among others, interactions with the environment …
entities. Selection can be based on, among others, interactions with the environment …
[HTML][HTML] Protein stability: a crystallographer's perspective
Protein stability is a topic of major interest for the biotechnology, pharmaceutical and food
industries, in addition to being a daily consideration for academic researchers studying …
industries, in addition to being a daily consideration for academic researchers studying …
Understanding protein non-folding
This review describes the family of intrinsically disordered proteins, members of which fail to
form rigid 3-D structures under physiological conditions, either along their entire lengths or …
form rigid 3-D structures under physiological conditions, either along their entire lengths or …
Natively unfolded proteins: a point where biology waits for physics
VN Uversky - Protein science, 2002 - Wiley Online Library
The experimental material accumulated in the literature on the conformational behavior of
intrinsically unstructured (natively unfolded) proteins was analyzed. Results of this analysis …
intrinsically unstructured (natively unfolded) proteins was analyzed. Results of this analysis …
Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism
L Nielsen, R Khurana, A Coats, S Frokjaer… - Biochemistry, 2001 - ACS Publications
In the search for the molecular mechanism of insulin fibrillation, the kinetics of insulin fibril
formation were studied under different conditions using the fluorescent dye thioflavin T …
formation were studied under different conditions using the fluorescent dye thioflavin T …
Evidence for a partially folded intermediate in α-synuclein fibril formation
VN Uversky, J Li, AL Fink - Journal of Biological Chemistry, 2001 - jbc.org
Intracellular proteinaceous aggregates (Lewy bodies and Lewy neurites) of α-synuclein are
hallmarks of neurodegenerative diseases such as Parkinson's disease, dementia with Lewy …
hallmarks of neurodegenerative diseases such as Parkinson's disease, dementia with Lewy …
Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein: a possible molecular link between Parkinson′ s disease and heavy …
VN Uversky, J Li, AL Fink - Journal of Biological Chemistry, 2001 - jbc.org
Parkinson's disease involves the aggregation of α-synuclein to form fibrils, which are the
major constituent of intracellular protein inclusions (Lewy bodies and Lewy neurites) in …
major constituent of intracellular protein inclusions (Lewy bodies and Lewy neurites) in …
Intrinsically disordered proteins from A to Z
VN Uversky - The international journal of biochemistry & cell biology, 2011 - Elsevier
The ideas that proteins might possess specific functions without being uniquely folded into
rigid 3D-structures and that these floppy polypeptides might constitute a noticeable part of …
rigid 3D-structures and that these floppy polypeptides might constitute a noticeable part of …