Reactivity of disulfide bonds is markedly affected by structure and environment: implications for protein modification and stability-Reference-Cited by-同舟云学术

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Reactivity of disulfide bonds is markedly affected by structure and environment: implications for protein modification and stability

Published:2016-12 Issue:1 Volume:6 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Karimi Maryam,Ignasiak Marta T.,Chan Bun,Croft Anna K.,Radom Leo,Schiesser Carl H.,Pattison David I.,Davies Michael J.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep38572.pdf

Reference65 articles.

1. Thornton, J. M. Disulphide bridges in globular proteins. J Mol Biol 151, 261–287 (1981).

2. Wedemeyer, W. J., Welker, E., Narayan, M. & Scheraga, H. A. Disulfide bonds and protein folding. Biochemistry 39, 4207–4216 (2000).

3. Azimi, I., Wong, J. W. & Hogg, P. J. Control of mature protein function by allosteric disulfide bonds. Antioxid Redox Signal 14, 113–126, doi: 10.1089/ars.2010.3620 (2011).

4. Cook, K. M. & Hogg, P. J. Post-translational control of protein function by disulfide bond cleavage. Antioxid Redox Signal 18, 1987–2015, doi: 10.1089/ars.2012.4807 (2013).

5. Hogg, P. J. Disulfide bonds as switches for protein function. Trends Biochem Sci 28, 210–214 (2003).

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