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- Publisher Website: 10.1089/ars.2010.3620
- Scopus: eid_2-s2.0-78649484651
- PMID: 20831445
- WOS: WOS:000284572100012
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Article: Control of mature protein function by allosteric disulfide bonds
Title | Control of mature protein function by allosteric disulfide bonds |
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Authors | |
Issue Date | 2011 |
Citation | Antioxidants and Redox Signaling, 2011, v. 14, n. 1, p. 113-126 How to Cite? |
Abstract | Protein disulfide bonds are the links between the sulfur atoms of two cysteine amino acids. All the known life forms appear to make this bond. Most disulfide bonds perform a structural role by stabilizing the tertiary and quaternary structures. Some perform a functional role and can be characterized as either catalytic or allosteric disulfides. Catalytic disulfides/dithiols transfer electrons between proteins, whereas the allosteric bonds control the function of the protein in which they reside when they undergo redox change. There are currently five clear examples of allosteric disulfide bonds and a number of potential allosteric disulfides at various stages of characterization. The features of these bonds and how they control the activity of the respective proteins are discussed. A common aspect of the allosteric disulfides identified to date is that they all link β-strands or β-loops. |
Persistent Identifier | http://hdl.handle.net/10722/250956 |
ISSN | 2023 Impact Factor: 5.9 2023 SCImago Journal Rankings: 1.708 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Azimi, Iman | - |
dc.contributor.author | Wong, Jason W.H. | - |
dc.contributor.author | Hogg, Philip J. | - |
dc.date.accessioned | 2018-02-01T01:54:10Z | - |
dc.date.available | 2018-02-01T01:54:10Z | - |
dc.date.issued | 2011 | - |
dc.identifier.citation | Antioxidants and Redox Signaling, 2011, v. 14, n. 1, p. 113-126 | - |
dc.identifier.issn | 1523-0864 | - |
dc.identifier.uri | http://hdl.handle.net/10722/250956 | - |
dc.description.abstract | Protein disulfide bonds are the links between the sulfur atoms of two cysteine amino acids. All the known life forms appear to make this bond. Most disulfide bonds perform a structural role by stabilizing the tertiary and quaternary structures. Some perform a functional role and can be characterized as either catalytic or allosteric disulfides. Catalytic disulfides/dithiols transfer electrons between proteins, whereas the allosteric bonds control the function of the protein in which they reside when they undergo redox change. There are currently five clear examples of allosteric disulfide bonds and a number of potential allosteric disulfides at various stages of characterization. The features of these bonds and how they control the activity of the respective proteins are discussed. A common aspect of the allosteric disulfides identified to date is that they all link β-strands or β-loops. | - |
dc.language | eng | - |
dc.relation.ispartof | Antioxidants and Redox Signaling | - |
dc.title | Control of mature protein function by allosteric disulfide bonds | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1089/ars.2010.3620 | - |
dc.identifier.pmid | 20831445 | - |
dc.identifier.scopus | eid_2-s2.0-78649484651 | - |
dc.identifier.volume | 14 | - |
dc.identifier.issue | 1 | - |
dc.identifier.spage | 113 | - |
dc.identifier.epage | 126 | - |
dc.identifier.isi | WOS:000284572100012 | - |
dc.identifier.issnl | 1523-0864 | - |