Redox-dependent disulfide bond formation in SAP30L corepressor protein: Implications for structure and function-Reference-Cited by-同舟云学术

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Redox-dependent disulfide bond formation in SAP30L corepressor protein: Implications for structure and function

Published:2015-12-10 Issue:3 Volume:25 Page:572-586
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Laitaoja Mikko¹,Tossavainen Helena²,Pihlajamaa Tero²,Valjakka Jarkko³,Viiri Keijo⁴,Lohi Olli⁴,Permi Perttu²,Jänis Janne¹

Affiliation:

1. Department of Chemistry; University of Eastern Finland; Joensuu Finland

2. Institute of Biotechnology; University of Helsinki; Helsinki Finland

3. BioMediTech; University of Tampere; Tampere Finland

4. Center for Child Health Research and Tampere University Hospital; University of Tampere; Tampere Finland

Funder

National Graduate School of Organic Chemistry and Chemical Biology

Biocenter Finland

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2849/fullpdf

Reference65 articles.

1. The role of cysteine residues as redox-sensitive regulatory switches;Barford;Curr Opin Struct Biol,2004

2. Thiol-based redox switches in eukaryotic proteins;Brandes;Antioxid Redox Signal,2008

3. Zinc coordination environments in proteins as redox sensors and signal transducers;Maret;Antioxid Redox Signal,2006

4. Disulfides as redox switches: from molecular mechanisms to functional significance;Wouters;Antioxid Redox Signal,2010

5. Structural classification of zinc fingers;Krishna;Nucleic Acids Res,2003

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