A kinetic study of β‐lactoglobulin amyloid fibril formation promoted by urea
Open Access
- 1 October 2002
- journal article
- Published by Wiley in Protein Science
- Vol. 11 (10) , 2417-2426
- https://doi.org/10.1110/ps.0217702
Abstract
Protein Science, the flagship journal of The Protein Society, serves an international forum for publishing original reports on all scientific aspects of protein molecules. The Journal publishes papers by leading scientists from all over the world that report on advances in the understanding of proteins in the broadest sense. Protein Science aims to unify this field by cutting across established disciplinary lines and focusing on “protein-centered” science.Keywords
This publication has 69 references indexed in Scilit:
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseasesNature, 2002
- Dependence on solution conditions of aggregation and amyloid formation by an SH3 domainJournal of Molecular Biology, 2001
- Independent Nucleation and Heterogeneous Assembly of Structure During Folding of Equine LysozymeJournal of Molecular Biology, 1999
- Heat- and cold-setting gels of β-lactoglobulin solutions. A DSC and TEM studyThermochimica Acta, 1998
- The equilibrium intermediate of β-lactoglobulin with non-native α-helical structureJournal of Molecular Biology, 1997
- The Burst-phase Intermediate in the Refolding of β-Lactoglobulin Studied by Stopped-flow Circular Dichroism and Absorption SpectroscopyJournal of Molecular Biology, 1996
- Effect of pH and insulin on fibrillogenesis of islet amyloid polypeptide in vitroBiochemistry, 1995
- β‐Lactoglobulin binds retinol and protoporphyrin IX at two different binding sitesFEBS Letters, 1990
- In vitro formation of amyloid fibrils from intact β2-microglobulinBiochemical and Biophysical Research Communications, 1985
- Ueber eine im Gehirn und Rückenmark des Menschen aufgefundene Substanz mit der chemischen Reaction der CelluloseVirchows Archiv, 1854