Thiol-disulfide balance: from the concept of oxidative stress to that of redox regulation.

by: P Ghezzi, V Bonetto, M Fratelli

Antioxid Redox Signal, Vol. 7, No. 7-8. (g 2005), pp. 964-972.

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摘要

Originally, small thiols, including glutathione, were viewed as protective antioxidants, acting as free radical scavengers in the context of oxidative damage. Recently, there is a growing literature showing that protein glutathionylation (formation of protein-glutathione mixed disulfides) and other forms of cysteine oxidation may be a means of redox regulation under physiological conditions. This review discusses the importance of protein oxidation in redox regulation in view of the recent data originating from the application of redox proteomics to identify redox-sensitive targets.

@article{citeulike:333192, abstract = {Originally, small thiols, including glutathione, were viewed as protective antioxidants, acting as free radical scavengers in the context of oxidative damage. Recently, there is a growing literature showing that protein glutathionylation (formation of protein-glutathione mixed disulfides) and other forms of cysteine oxidation may be a means of redox regulation under physiological conditions. This review discusses the importance of protein oxidation in redox regulation in view of the recent data originating from the application of redox proteomics to identify redox-sensitive targets.}, address = {Mario Negri Institute for Pharmacological Research, Milan, Italy. ghezzi@marionegri.it}, author = {Ghezzi, P. and Bonetto, V. and Fratelli, M. }, citeulike-article-id = {333192}, doi = {http://dx.doi.org/10.1089/ars.2005.7.964}, issn = {1523-0864}, journal = {Antioxid Redox Signal}, keywords = {introduction}, number = {7-8}, pages = {964--972}, posted-at = {2007-05-03 01:57:39}, priority = {2}, title = {Thiol-disulfide balance: from the concept of oxidative stress to that of redox regulation.}, url = {http://dx.doi.org/10.1089/ars.2005.7.964}, volume = {7}, year = {2005} }

RIS record

TY - JOUR ID - citeulike:333192 L3 - citeulike-article-id:333192 TI - Thiol-disulfide balance: from the concept of oxidative stress to that of redox regulation. JF - Antioxid Redox Signal VL - 7 IS - 7-8 SP - 964 EP - 972 AD - Mario Negri Institute for Pharmacological Research, Milan, Italy. ghezzi@marionegri.it SN - 1523-0864 N2 - Originally, small thiols, including glutathione, were viewed as protective antioxidants, acting as free radical scavengers in the context of oxidative damage. Recently, there is a growing literature showing that protein glutathionylation (formation of protein-glutathione mixed disulfides) and other forms of cysteine oxidation may be a means of redox regulation under physiological conditions. This review discusses the importance of protein oxidation in redox regulation in view of the recent data originating from the application of redox proteomics to identify redox-sensitive targets. KW - introduction AU - Ghezzi, P AU - Bonetto, V AU - Fratelli, M PY - 2005///g UR - http://dx.doi.org/10.1089/ars.2005.7.964 ER -

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