Literature DB >> 15270699

Protein kinase function and glutathionylation.

Anthony N Anselmo1, Melanie H Cobb.   

Abstract

Intracellular reactive oxygen species are generated as a by-product of normal metabolic processes and can both damage cellular constituents and function as important signalling species. This signalling often involves changes in the thiol redox balance. As an antioxidant, glutathione serves in maintaining the reduced state of cellular protein thiol groups. The paper by Cross and Templeton appearing in this issue of the Biochemical Journal describes a mechanism by which glutathionylation plays a key role in the regulation of the kinase activity of MEKK1 [MAP (mitogen-activated protein kinase)/ERK (extracellular-signal-regulated kinase) kinase kinase; MAP3K] in response to oxidative stresses. This type of post-translational-modification glutathionylation may represent a general mechanism by which protein kinase function can be regulated.

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Year:  2004        PMID: 15270699      PMCID: PMC1133907          DOI: 10.1042/BJ20040873

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  11 in total

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Review 4.  Reactive oxygen species and programmed cell death.

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8.  Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP-binding domain.

Authors:  Janet V Cross; Dennis J Templeton
Journal:  Biochem J       Date:  2004-08-01       Impact factor: 3.857

9.  Regulation of cAMP-dependent protein kinase activity by glutathionylation.

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Review 7.  Cysteine Glutathionylation Acts as a Redox Switch in Endothelial Cells.

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8.  The effect of oxidant and the non-oxidant alteration of cellular thiol concentration on the formation of protein mixed-disulfides in HEK 293 cells.

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