Stability, Folding, Dimerization, and Assembly Properties of the Yeast Prion Ure2p
- 19 January 2001
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 40 (6) , 1764-1773
- https://doi.org/10.1021/bi001916l
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- Structure of the Globular Region of the Prion Protein Ure2 from the Yeast Saccharomyces cerevisiaeStructure, 2001
- Structural Characterization of Saccharomyces cerevisiae Prion-like Protein Ure2Journal of Biological Chemistry, 1999
- Characterization of the interaction domains of Ure2p, a prion-like protein of yeastBiochemical Journal, 1999
- Glutamine repeats and neurodegenerative diseases: molecular aspectsTrends in Biochemical Sciences, 1999
- Prions of Yeast and FungiJournal of Biological Chemistry, 1999
- Differential resistance to proteinase K digestion of the yeast prion-like (Ure2p) protein synthesized in vitro in wheat germ extract and rabbit reticulocyte lysate cell-free translation systemsFEBS Letters, 1997
- Prion-Inducing Domain of Yeast Ure2p and Protease Resistance of Ure2p in Prion-Containing CellsScience, 1995
- Measuring Sedimentation, Diffusion, and Molecular Weights of Small Molecules by Direct Fitting of Sedimentation Velocity Concentration ProfilesPublished by Springer Nature ,1994
- Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structureJournal of Bacteriology, 1987