The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils
- 15 January 2003
- journal article
- Published by Elsevier in Journal of Structural Biology
- Vol. 141 (2) , 132-142
- https://doi.org/10.1016/s1047-8477(02)00606-8
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- β2-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitroJournal of Molecular Biology, 2001
- Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domainJournal of Molecular Biology, 2000
- Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packingThe EMBO Journal, 1999
- Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. CohenJournal of Molecular Biology, 1997
- Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helixStructure, 1996
- [URE3] as an Altered URE2 Protein: Evidence for a Prion Analog in Saccharomyces cerevisiaeScience, 1994
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Ψ, A cytoplasmic suppressor of super-suppressor in yeastHeredity, 1965
- X-Ray studies of the structure of hair, wool, and related fibres. II.- the molecular structure and elastic properties of hair keratinPhilosophical Transactions of the Royal Society A, 1933