Opposing Effects of Glutamine and Asparagine Govern Prion Formation by Intrinsically Disordered Proteins
- 1 July 2011
- journal article
- research article
- Published by Elsevier BV in Molecular Cell
- Vol. 43 (1), 72-84
- https://doi.org/10.1016/j.molcel.2011.05.013
Abstract
No abstract availableKeywords
This publication has 80 references indexed in Scilit:
- Essential Role of Coiled Coils for Aggregation and Activity of Q/N-Rich Prions and PolyQ ProteinsCell, 2010
- The protein kingdom extended: Ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregationProgress in Biophysics and Molecular Biology, 2010
- Prions, protein homeostasis, and phenotypic diversityTrends in Cell Biology, 2010
- Modulation of Polyglutamine Conformations and Dimer Formation by the N-Terminus of HuntingtinJournal of Molecular Biology, 2009
- Examining Polyglutamine Peptide Length: A Connection between Collapsed Conformations and Increased AggregationJournal of Molecular Biology, 2009
- Intrinsic Protein Disorder and Interaction Promiscuity Are Widely Associated with Dosage SensitivityCell, 2009
- Thermodynamics of β-Sheet Formation in PolyglutamineBiophysical Journal, 2009
- A Systematic Survey Identifies Prions and Illuminates Sequence Features of Prionogenic ProteinsCell, 2009
- Atomistic Simulations of the Effects of Polyglutamine Chain Length and Solvent Quality on Conformational Equilibria and Spontaneous HomodimerizationJournal of Molecular Biology, 2008
- A polymer physics perspective on driving forces and mechanisms for protein aggregationArchives of Biochemistry and Biophysics, 2007