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Transduction of redox signaling by electrophile-protein reactions

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Transduction of redox signaling by electrophile-protein reactions. / Rudolph, Tanja K; Freeman, Bruce A.

In: SCIENCE SIGNALING, Vol. 2, No. 90, 29.09.2009, p. 7.

Research output: SCORING: Contribution to journal › SCORING: Review article › Research

Harvard

Rudolph, TK & Freeman, BA 2009, 'Transduction of redox signaling by electrophile-protein reactions', SCIENCE SIGNALING, vol. 2, no. 90, pp. 7. https://doi.org/10.1126/scisignal.290re7

APA

Rudolph, T. K., & Freeman, B. A. (2009). Transduction of redox signaling by electrophile-protein reactions. SCIENCE SIGNALING, 2(90), 7. https://doi.org/10.1126/scisignal.290re7

Vancouver

Rudolph TK, Freeman BA. Transduction of redox signaling by electrophile-protein reactions. SCIENCE SIGNALING. 2009 Sep 29;2(90):7. https://doi.org/10.1126/scisignal.290re7

Bibtex

@article{f2cf496d7efc481795f14ace1ba7480a,
title = "Transduction of redox signaling by electrophile-protein reactions",
abstract = "Over the last 50 years, the posttranslational modification (PTM) of proteins has emerged as a central mechanism for cells to regulate metabolism, growth, differentiation, cell-cell interactions, and immune responses. By influencing protein structure and function, PTM leads to a multiplication of proteome diversity. Redox-dependent PTMs, mediated by environmental and endogenously generated reactive species, induce cell signaling responses and can have toxic effects in organisms. PTMs induced by the electrophilic by-products of redox reactions most frequently occur at protein thiols; other nucleophilic amino acids serve as less favorable targets. Advances in mass spectrometry and affinity-chemistry strategies have improved the detection of electrophile-induced protein modifications both in vitro and in vivo and have revealed a high degree of amino acid and protein selectivity of electrophilic PTM. The identification of biological targets of electrophiles has motivated further study of the functional impact of various PTM reactions on specific signaling pathways and how this might affect organisms.",
keywords = "Animals, Cysteine/chemistry, Electrochemistry, Humans, Models, Biological, Models, Molecular, Oxidation-Reduction, Protein Processing, Post-Translational, Proteins/chemistry, Signal Transduction/physiology",
author = "Rudolph, {Tanja K} and Freeman, {Bruce A}",
year = "2009",
month = sep,
day = "29",
doi = "10.1126/scisignal.290re7",
language = "English",
volume = "2",
pages = "7",
journal = "SCI SIGNAL",
issn = "1945-0877",
publisher = "American Association for the Advancement of Science",
number = "90",

}

RIS

TY - JOUR

T1 - Transduction of redox signaling by electrophile-protein reactions

AU - Rudolph, Tanja K

AU - Freeman, Bruce A

PY - 2009/9/29

Y1 - 2009/9/29

N2 - Over the last 50 years, the posttranslational modification (PTM) of proteins has emerged as a central mechanism for cells to regulate metabolism, growth, differentiation, cell-cell interactions, and immune responses. By influencing protein structure and function, PTM leads to a multiplication of proteome diversity. Redox-dependent PTMs, mediated by environmental and endogenously generated reactive species, induce cell signaling responses and can have toxic effects in organisms. PTMs induced by the electrophilic by-products of redox reactions most frequently occur at protein thiols; other nucleophilic amino acids serve as less favorable targets. Advances in mass spectrometry and affinity-chemistry strategies have improved the detection of electrophile-induced protein modifications both in vitro and in vivo and have revealed a high degree of amino acid and protein selectivity of electrophilic PTM. The identification of biological targets of electrophiles has motivated further study of the functional impact of various PTM reactions on specific signaling pathways and how this might affect organisms.

AB - Over the last 50 years, the posttranslational modification (PTM) of proteins has emerged as a central mechanism for cells to regulate metabolism, growth, differentiation, cell-cell interactions, and immune responses. By influencing protein structure and function, PTM leads to a multiplication of proteome diversity. Redox-dependent PTMs, mediated by environmental and endogenously generated reactive species, induce cell signaling responses and can have toxic effects in organisms. PTMs induced by the electrophilic by-products of redox reactions most frequently occur at protein thiols; other nucleophilic amino acids serve as less favorable targets. Advances in mass spectrometry and affinity-chemistry strategies have improved the detection of electrophile-induced protein modifications both in vitro and in vivo and have revealed a high degree of amino acid and protein selectivity of electrophilic PTM. The identification of biological targets of electrophiles has motivated further study of the functional impact of various PTM reactions on specific signaling pathways and how this might affect organisms.

KW - Animals

KW - Cysteine/chemistry

KW - Electrochemistry

KW - Humans

KW - Models, Biological

KW - Models, Molecular

KW - Oxidation-Reduction

KW - Protein Processing, Post-Translational

KW - Proteins/chemistry

KW - Signal Transduction/physiology

U2 - 10.1126/scisignal.290re7

DO - 10.1126/scisignal.290re7

M3 - SCORING: Review article

C2 - 19797270

VL - 2

SP - 7

JO - SCI SIGNAL

JF - SCI SIGNAL

SN - 1945-0877

IS - 90

ER -