Small angle X-ray scattering study of the yeast prion Ure2p
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference37 articles.
1. Prion domain initiation of amyloid formation in vitro from native Ure2p;Taylor;Science,1999
2. Equilibrium folding properties of the yeast prion protein determinant Ure2;Perrett;J. Mol. Biol.,1999
3. Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast;Lacroute;J. Bacteriol.,1971
4. The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione S-transferases;Coshigano;Mol. Cell. Biol.,1991
5. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae;Wickner;Science,1994
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2. C-terminal 13-residue Truncation Induces Compact Trigger Factor Conformation and Severely Impairs its Dimerization Ability;Protein & Peptide Letters;2014-02
3. Deletion of a Ure2 C-terminal prion-inhibiting region promotes the rate of fibril seed formation and alters interaction with Hsp40;Protein Engineering Design and Selection;2010-11-12
4. The yeast prion protein Ure2: Structure, function and folding;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2006-03
5. The Yeast Prion Protein Ure2 Shows Glutathione Peroxidase Activity in Both Native and Fibrillar Forms;Journal of Biological Chemistry;2004-11
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