Supercharging Proteins Can Impart Unusual Resilience
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Open Access
- 1 August 2007
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 129 (33), 10110-10112
- https://doi.org/10.1021/ja071641y
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Mechanism of coupled folding and binding of an intrinsically disordered proteinNature, 2007
- Arginine Grafting to Endow Cell PermeabilityACS Chemical Biology, 2007
- The Fluorescent Toolbox for Assessing Protein Location and FunctionScience, 2006
- Engineering and characterization of a superfolder green fluorescent proteinNature Biotechnology, 2005
- Prediction of “Aggregation-prone” and “Aggregation-susceptible” Regions in Proteins Associated with Neurodegenerative DiseasesJournal of Molecular Biology, 2005
- The Pairwise Energy Content Estimated from Amino Acid Composition Discriminates between Folded and Intrinsically Unstructured ProteinsJournal of Molecular Biology, 2005
- Therapeutic approaches to protein-misfolding diseasesNature, 2003
- Rationalization of the effects of mutations on peptide andprotein aggregation ratesNature, 2003
- Removal of surface charge‐charge interactions from ubiquitin leaves the protein folded and very stableProtein Science, 2002
- CHEMICAL AND PHYSICAL BEHAVIOR OF CASEIN SOLUTIONSThe Journal of general physiology, 1921