Protein nitrotryptophan: Formation, significance and identification

Nuriel, Tal; Hansler, Alex; Gross, Steven S.

doi:10.1016/j.jprot.2011.05.032

Cited by 61 publications

(53 citation statements)

References 72 publications

(148 reference statements)

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“…Surprisingly, we also detected a substoichiometric (0.3 Ϯ 0.1/subunit) S-nitrosation of C47S/C101S double mutant GSTP1-1. The identity of the third S-nitrosation site (or sites) is unclear, but may represent S-nitrosation at another cysteine, or even nitration of tryptophan or tyrosine residues (29). Electrospray ionization-mass spectrometry did not suggest the presence of any additional modifications such as S-glutathionylation (data not shown), consistent with the mass spectrometric analysis of Lo Bello et al (22).…”

Section: Gstp1-1 S-nitrosation Probed Bysupporting

confidence: 80%

S-Nitrosation of Glutathione Transferase P1-1 Is Controlled by the Conformation of a Dynamic Active Site Helix

Balchin

Wallace

Dirr

2013

Journal of Biological Chemistry

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Background: S-Nitrosation is an emerging post-translational modification that is not yet well understood on a molecular level. Results: We propose a mechanism for S-nitrosation of glutathione transferase P1-1 by S-nitrosoglutathione. Conclusion: Cys 101 is nitrosated in a single step, but Cys 47 nitrosation is limited by the rate of helix 2 opening. Significance: Detailing the mechanism of spontaneous transnitrosation is crucial to understanding how protein S-nitrosation is controlled.

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Section: Gstp1-1 S-nitrosation Probed Bysupporting

confidence: 80%

S-Nitrosation of Glutathione Transferase P1-1 Is Controlled by the Conformation of a Dynamic Active Site Helix

Balchin

Wallace

Dirr

2013

Journal of Biological Chemistry

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“…Modifications of the Trp residue by RNS are relevant in physiological and pathological conditions (Ducrocq et al, 1999;Alvarez and Radi, 2003;Yamakura and Ikeda, 2006;Ascenzi et al, 2010b;Nuriel et al, 2011). Free Trp can be modified to several nitrated products (1-, 4-, 5-, 6-, and 7-nitrotryptophan), to 1-N-nitrosotryptophan, and to several oxidized products by reaction with various RNS, depending on the conditions used.…”

Section: Trp Nitrosylation and Nitrationmentioning

confidence: 99%

“…Free Trp can be modified to several nitrated products (1-, 4-, 5-, 6-, and 7-nitrotryptophan), to 1-N-nitrosotryptophan, and to several oxidized products by reaction with various RNS, depending on the conditions used. Among them, 1-N-nitrosotryptophan and 6-nitrotryptophan are the most abundant products in the reaction with peroxynitrite, 6-nitrotryptophan being the most abundant product in the reaction with the peroxidase/hydrogen peroxide/nitrite systems (Yamakura and Ikeda, 2006;Bregere et al, 2008;Nuriel et al, 2011).…”

Section: Trp Nitrosylation and Nitrationmentioning

confidence: 99%

Human serum albumin: From bench to bedside

Fanali

Masi

Trezza

et al. 2012

Molecular Aspects of Medicine

1,402

1,418

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“…The most common products of protein nitration are nitrotyrosine, and to a much lesser extent, nitrotryptophan (Fig. 5, B) [106]. Nitrotyrosine can be produced from the reaction between tyrosine and a strong nitrating agent like peroxynitrite and it is considered a general biomarker of disease progression [107].…”

Section: Tyrosine and Tryptophan Nitrationmentioning

confidence: 99%

“…The derivatization method involves blocking all primary amines, reducing nitroresidues to their amino-counterparts and selectively attaching an affinity handle (e.g. biotin) for enrichment or a reporter group for selective mass spectrometric detection [106,110].…”

Section: Tyrosine and Tryptophan Nitrationmentioning

confidence: 99%

Advances in purification and separation of posttranslationally modified proteins

Černý

Skalák

Cerná

et al. 2013

Journal of Proteomics

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Posttranslational modifications (PTMs) of proteins represent fascinating extensions of the dynamic complexity of living cells' proteomes. The results of enzymatically catalyzed or spontaneous chemical reactions, PTMs form a fourth tier in the gene -transcript -protein cascade, and contribute not only to proteins' biological functions, but also to challenges in their analysis. There have been tremendous advances in proteomics during the last decade. Identification and mapping of PTMs in proteins have improved dramatically, mainly due to constant increases in the sensitivity, speed, accuracy and resolution of mass spectrometry (MS). However, it is also becoming increasingly evident that simple gel-free shotgun MS profiling is unlikely to suffice for comprehensive detection and characterization of proteins and/or protein modifications present in low amounts. Here, we review current approaches for enriching and separating posttranslationally modified proteins, and their MS-independent detection. First, we discuss general approaches for proteome separation, fractionation and enrichment. We then consider the commonest forms of PTMs (phosphorylation, glycosylation and glycation, lipidation, methylation, acetylation, deamidation, ubiquitination and various redox modifications), and the best available methods for detecting and purifying proteins carrying these PTMs.

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Protein nitrotryptophan: Formation, significance and identification

Cited by 61 publications

References 72 publications

S-Nitrosation of Glutathione Transferase P1-1 Is Controlled by the Conformation of a Dynamic Active Site Helix

S-Nitrosation of Glutathione Transferase P1-1 Is Controlled by the Conformation of a Dynamic Active Site Helix

Human serum albumin: From bench to bedside

Advances in purification and separation of posttranslationally modified proteins

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