β-Helix is a likely core structure of yeast prion Sup35 amyloid fibers
- 12 March 2004
- journal article
- Published by Elsevier BV in Biochemical and Biophysical Research Communications
- Vol. 315 (3), 739-745
- https://doi.org/10.1016/j.bbrc.2004.01.117
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Culture, Sports, Science and Technology
This publication has 38 references indexed in Scilit:
- Solid State NMR Reveals a pH-dependent Antiparallel β-Sheet Registry in Fibrils Formed by a β-Amyloid PeptideJournal of Molecular Biology, 2004
- Strong Growth Polarity of Yeast Prion Fiber Revealed by Single Fiber ImagingPublished by Elsevier BV ,2001
- Prions Affect the Appearance of Other Prions: The Story of [PIN+]Cell, 2001
- Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion DeterminantScience, 2000
- Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformationProceedings of the National Academy of Sciences of the United States of America, 2000
- The yeast non-Mendelian factor [ETA+] is a variant of [PSI+], a prion-like form of release factor eRF3The EMBO Journal, 1999
- Multiple-step method for making exceptionally well-oriented liquid-crystalline sols of macromolecular assembliesJournal of Molecular Biology, 1998
- [URE3] as an Altered URE2 Protein: Evidence for a Prion Analog in Saccharomyces cerevisiaeScience, 1994
- MOLSCRIPT: a program to produce both detailed and schematic plots of protein structuresJournal of Applied Crystallography, 1991
- Preparing well-oriented sols of straight bacterial flagellar filaments for X-ray fiber diffractionJournal of Molecular Biology, 1991