Protein folding in the cell envelope of Escherichia coli
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Microbiology (medical),Genetics,Applied Microbiology and Biotechnology,Immunology,Microbiology
Link
http://www.nature.com/articles/nmicrobiol2016107.pdf
Reference172 articles.
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2. Yu, H. et al. Protein misfolding occurs by slow diffusion across multiple barriers in a rough energy landscape. Proc. Natl Acad. Sci. USA 112, 8308–8313 (2015).
3. Uversky, V. N. Unusual biophysics of intrinsically disordered proteins. Biochim. Biophys. Acta 1834, 932–951 (2013).
4. Kovacs, D., Szabo, B., Pancsa, R. & Tompa, P. Intrinsically disordered proteins undergo and assist folding transitions in the proteome. Arch. Biochem. Biophys. 531, 80–89 (2013).
5. Orfanoudaki, G. & Economou, A. Proteome-wide subcellular topologies of E. coli polypeptides database (STEPdb). Mol. Cell Proteomics 13, 3674–3687 (2014).
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