| Redox signalling via the cellular thiolstat. | |
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MedLine Citation:
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PMID: 21936797 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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Research conducted during the last two decades has provided evidence for the existence of an extensive intracellular redox signalling, control and feedback network based on different cysteine-containing proteins and enzymes. Together, these proteins enable the living cell to sense and respond towards external and internal redox changes in a measured, gradual, appropriate and mostly reversible manner. The (bio)chemical basis of this regulatory 'thiolstat' is provided by the complex redox chemistry of the amino acid cysteine, which occurs in vivo in various sulfur chemotypes and is able to participate in different redox processes. Although our knowledge of the biological redox behaviour of sulfur (i.e. cysteine or methionine) is expanding, numerous questions still remain. Future research will need to focus on the individual proteins involved in this redox system, their particular properties and specific roles in cellular defence and survival. Once it is more fully understood, the cellular thiolstat and its individual components are likely to form prominent targets for drug design. |
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Authors:
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Claus Jacob |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Biochemical Society transactions Volume: 39 ISSN: 1470-8752 ISO Abbreviation: Biochem. Soc. Trans. Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-09-22 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7506897 Medline TA: Biochem Soc Trans Country: England |
Other Details:
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Languages: eng Pagination: 1247-53 Citation Subset: IM |
Affiliation:
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Division of Bioorganic Chemistry, School of Pharmacy, Saarland University, Campus, D-66123 Saarbrücken, Germany. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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