Amyloids in bacterial inclusion bodies
- 1 August 2009
- journal article
- review article
- Published by Elsevier in Trends in Biochemical Sciences
- Vol. 34 (8) , 408-416
Abstract
No abstract availableKeywords
This publication has 72 references indexed in Scilit:
- Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prionsThe EMBO Journal, 2008
- Bacterial Inclusion Bodies Contain Amyloid-Like StructurePLOS Biology, 2008
- The in Vivo and in Vitro Aggregation Properties of Globular Proteins Correlate With Their Conformational Stability: The SH3 CaseJournal of Molecular Biology, 2008
- Asymmetric segregation of protein aggregates is associated with cellular aging and rejuvenationProceedings of the National Academy of Sciences, 2008
- The Zyggregator method for predicting protein aggregation propensitiesChemical Society Reviews, 2008
- Folding versus aggregation: Polypeptide conformations on competing pathwaysArchives of Biochemistry and Biophysics, 2008
- AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptidesBMC Bioinformatics, 2007
- The Yin and Yang of protein foldingThe FEBS Journal, 2005
- Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteinsNature Biotechnology, 2004
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseasesNature, 2002