Posttranslational modification of proteins

Zsolt Radak

doi:10.1007/978-4-431-55333-5_14

Posttranslational modification of proteins

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

Proteins are subject to continuous reversible and irreversible modifications. These posttranslational modifications directly influence the stability and/or the function of proteins. Aging results in an increased half-life of proteins, which is associated with enhanced oxidative modifications of amino acid residues. Lysine residues are carbonylated, acetylated, and ubiquitinated, and cross talk between these modifications is crucial for the fate of proteins.

Original language	English
Title of host publication	Physical Activity, Exercise, Sedentary Behavior and Health
Publisher	Springer Japan
Pages	165-169
Number of pages	5
ISBN (Electronic)	9784431553335
ISBN (Print)	9784431553328
DOIs	https://doi.org/10.1007/978-4-431-55333-5_14
Publication status	Published - 2015 Jan 1
Externally published	Yes

Keywords

Acetylation
Carbonylation
Reactive oxygen species
Sirtuins
Ubiquitination

ASJC Scopus subject areas

Medicine(all)
Engineering(all)

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abstract = "Proteins are subject to continuous reversible and irreversible modifications. These posttranslational modifications directly influence the stability and/or the function of proteins. Aging results in an increased half-life of proteins, which is associated with enhanced oxidative modifications of amino acid residues. Lysine residues are carbonylated, acetylated, and ubiquitinated, and cross talk between these modifications is crucial for the fate of proteins.",

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KW - Carbonylation

KW - Reactive oxygen species

KW - Sirtuins

KW - Ubiquitination

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ER -

Posttranslational modification of proteins

Abstract

Keywords

ASJC Scopus subject areas

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