Temperature induced structural transitions from native to unfolded aggregated states of tobacco etch virus protease

Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON, and CDSSTR Methods with an Expanded Reference Set

Narasimha Sreerama, Robert W. Woody · Analytical Biochemistry · 2000 · 3K citations

Biochemistry, Biomolecular Structure Prediction, Protein Folding +13

Thioflavine T interaction with synthetic Alzheimer's disease <i>β</i>‐amyloid peptides: Detection of amyloid aggregation in solution

Harry LeVine · Protein Science · 1993 · 2.2K citations · Full text

Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency

Rachel B. Kapust, József Tőzsér, Jeffrey D. Fox et al. · Protein Engineering Design and Selection · 2001 · 864 citations · Full text

Catalytic Domain, Viral Replication, Engineering +18

The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds

Sean A. Hudson, Heath Ecroyd, Tak W. Kee et al. · FEBS Journal · 2009 · 590 citations

Neurochemical Biomarkers, Polyphenolics, Medicinal Chemistry +18

Refolding of recombinant proteins

Eliana De Bernardez Clark · Current Opinion in Biotechnology · 1998 · 474 citations

Recombinant Proteins, Protein Folding, Natural Sciences +6