Literature DB >> 20609908

Measuring mitochondrial protein thiol redox state.

Raquel Requejo1, Edward T Chouchani, Thomas R Hurd, Katja E Menger, Mark B Hampton, Michael P Murphy.   

Abstract

Protein thiols are an important component of mammalian intramitochondrial antioxidant defenses owing to their selective interaction with reactive oxygen and nitrogen species (ROS and RNS). Reversible modifications of protein thiols resulting from these interactions are also an important aspect of redox signal transduction. Therefore, to assess how mitochondria respond to oxidative stress and act as nodes in redox signaling pathways, it is important to measure general changes to protein thiol redox states and also to identify the specific mitochondrial thiol proteins involved. Here we outline some of the approaches that can be used to accomplish these goals and thereby infer the multiple roles of mammalian mitochondrial protein thiols in antioxidant defense and redox signaling. Copyright (c) 2010 Elsevier Inc. All rights reserved.

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Year:  2010        PMID: 20609908     DOI: 10.1016/S0076-6879(10)74008-8

Source DB:  PubMed          Journal:  Methods Enzymol        ISSN: 0076-6879            Impact factor:   1.600


  10 in total

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Review 6.  Proteomic approaches to the characterization of protein thiol modification.

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  10 in total

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