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The Journal of Biological Chemistry|January 30, 2002
Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pHPierre O Souillac, Vladimir N Uversky, Ian S Millett, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 5, 2002
Exploring the folding landscape of a structured RNARick Russell, Xiaowei Zhuang, Hazen P Babcock, et al.
The Journal of Biological Chemistry|January 30, 2002
Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pHPierre O Souillac, Vladimir N Uversky, Ian S Millett, et al.
Journal of Pharmaceutical Sciences|March 28, 2003
Prediction of the association state of insulin using spectral parametersVladimir N Uversky, Liza Nielsen Garriques, Ian S Millett, et al.
Proceedings of the National Academy of Sciences of the United States of America|August 9, 2005
Unusual compactness of a polyproline type II structureBojan Zagrovic, Jan Lipfert, Eric J Sorin, et al.
The Journal of Biological Chemistry|January 29, 2002
Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleinsVladimir N Uversky, Jie Li, Pierre Souillac, et al.
FEBS Letters|January 21, 2014
A simple method for the determination of reduction potentials in heme proteinsIgor Efimov, Gary Parkin, Elizabeth S Millett, et al.
Brain Research. Molecular Brain Research|March 26, 2005
Effects of nitration on the structure and aggregation of alpha-synucleinVladimir N Uversky, Ghiam Yamin, Larissa A Munishkina, et al.
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