Redox proteomics: identification of oxidatively modified proteins.

by: P Ghezzi, V Bonetto

Proteomics, Vol. 3, No. 7. (July 2003), pp. 1145-1153.

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Abstract

Reactive oxygen and nitrogen species may cause various types of chemical modifications on specific proteins, Such modifications if irreversible are often associated with permanent loss of function and may lead to the elimination or to the accumulation of the damaged proteins. Reversible modifications, particularly at the cysteine residues, may have a dual role of protection from cysteine irreversible oxidation and modulation of protein function (redox regulation). Here we will review the techniques available for identifying proteins based on their redox state. In particular, we will focus on protein carbonylation, tyrosine nitration and thiol-disulfide chemistry of cysteines, with special emphasis on glutathionylation, because these are the fields where the tools of proteome analysis have been applied.

@article{citeulike:431972, abstract = {Reactive oxygen and nitrogen species may cause various types of chemical modifications on specific proteins, Such modifications if irreversible are often associated with permanent loss of function and may lead to the elimination or to the accumulation of the damaged proteins. Reversible modifications, particularly at the cysteine residues, may have a dual role of protection from cysteine irreversible oxidation and modulation of protein function (redox regulation). Here we will review the techniques available for identifying proteins based on their redox state. In particular, we will focus on protein carbonylation, tyrosine nitration and thiol-disulfide chemistry of cysteines, with special emphasis on glutathionylation, because these are the fields where the tools of proteome analysis have been applied.}, address = {Mario Negri Institute for Pharmacological Research, Via Eritrea 62, 20157 Milan, Italy. ghezzi@marionegri.it}, author = {Ghezzi, P. and Bonetto, V. }, citeulike-article-id = {431972}, doi = {10.1002/pmic.200300435}, issn = {1615-9853}, journal = {Proteomics}, keywords = {introduction}, month = {July}, number = {7}, pages = {1145--1153}, posted-at = {2007-05-03 23:26:06}, priority = {2}, title = {Redox proteomics: identification of oxidatively modified proteins.}, url = {http://dx.doi.org/10.1002/pmic.200300435}, volume = {3}, year = {2003} }

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TY - JOUR ID - citeulike:431972 L3 - citeulike-article-id:431972 TI - Redox proteomics: identification of oxidatively modified proteins. JF - Proteomics VL - 3 IS - 7 SP - 1145 EP - 1153 AD - Mario Negri Institute for Pharmacological Research, Via Eritrea 62, 20157 Milan, Italy. ghezzi@marionegri.it SN - 1615-9853 N2 - Reactive oxygen and nitrogen species may cause various types of chemical modifications on specific proteins, Such modifications if irreversible are often associated with permanent loss of function and may lead to the elimination or to the accumulation of the damaged proteins. Reversible modifications, particularly at the cysteine residues, may have a dual role of protection from cysteine irreversible oxidation and modulation of protein function (redox regulation). Here we will review the techniques available for identifying proteins based on their redox state. In particular, we will focus on protein carbonylation, tyrosine nitration and thiol-disulfide chemistry of cysteines, with special emphasis on glutathionylation, because these are the fields where the tools of proteome analysis have been applied. KW - introduction AU - Ghezzi, P AU - Bonetto, V PY - 2003/07// UR - http://dx.doi.org/10.1002/pmic.200300435 ER -

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