Macromolecular Crowding in the Escherichia coli Periplasm Maintains α-Synuclein Disorder
- 1 February 2006
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 355 (5), 893-897
- https://doi.org/10.1016/j.jmb.2005.11.033
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Polycation‐induced oligomerization and accelerated fibrillation of human α‐synuclein in vitroProtein Science, 2003
- FlgM gains structure in living cellsProceedings of the National Academy of Sciences, 2002
- Accelerated α‐synuclein fibrillation in crowded milieuFEBS Letters, 2002
- Molecular Crowding Accelerates Fibrillization of α-Synuclein: Could an Increase in the Cytoplasmic Protein Concentration Induce Parkinson's Disease?Biochemistry, 2002
- In-Cell NMR SpectroscopyBiochemistry, 2001
- Solvent‐induced collapse of α‐synuclein and acid‐denatured cytochrome cProtein Science, 2001
- Macromolecular crowding: obvious but underappreciatedTrends in Biochemical Sciences, 2001
- Evaluation of Parameters Critical to Observing Proteins Inside LivingEscherichiacoliby In-Cell NMR SpectroscopyJournal of the American Chemical Society, 2001
- Parkinson's DiseaseNew England Journal of Medicine, 1998
- Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coliJournal of Molecular Biology, 1991