Posttranslational modification of proteins

Zsolt Radak

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

Posttranslational modification of proteins

Zsolt Radak^*

^*Corresponding author for this work

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)

Access to Document

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

Cite this

@inbook{582d6c151bdd4dd9b39a73d0ba3f8517,

title = "Posttranslational modification of proteins",

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.",

keywords = "Acetylation, Carbonylation, Reactive oxygen species, Sirtuins, Ubiquitination",

author = "Zsolt Radak",

note = "Funding Information: Research in the authors' laboratory is supported by grants AI-08814, GM27989, and GM29897 from the NIH, and NSF grant 79-00839PCM. The author thanks Miriam Boucher for her patience and expertise in preparing the manuscript, and Drs Asher Zilberstein, Anthony Sinsky and Rex Chisholm for their helpful comments. Publisher Copyright: {\textcopyright} 2015, Springer Japan.",

year = "2015",

month = jan,

day = "1",

doi = "10.1007/978-4-431-55333-5_14",

language = "English",

isbn = "9784431553328",

pages = "165--169",

booktitle = "Physical Activity, Exercise, Sedentary Behavior and Health",

publisher = "Springer Japan",

}

TY - CHAP

T1 - Posttranslational modification of proteins

AU - Radak, Zsolt

N1 - Funding Information: Research in the authors' laboratory is supported by grants AI-08814, GM27989, and GM29897 from the NIH, and NSF grant 79-00839PCM. The author thanks Miriam Boucher for her patience and expertise in preparing the manuscript, and Drs Asher Zilberstein, Anthony Sinsky and Rex Chisholm for their helpful comments. Publisher Copyright: © 2015, Springer Japan.

PY - 2015/1/1

Y1 - 2015/1/1

N2 - 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.

AB - 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.

KW - Acetylation

KW - Carbonylation

KW - Reactive oxygen species

KW - Sirtuins

KW - Ubiquitination

UR - http://www.scopus.com/inward/record.url?scp=84943328759&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84943328759&partnerID=8YFLogxK

U2 - 10.1007/978-4-431-55333-5_14

DO - 10.1007/978-4-431-55333-5_14

M3 - Chapter

AN - SCOPUS:84943328759

SN - 9784431553328

SP - 165

EP - 169

BT - Physical Activity, Exercise, Sedentary Behavior and Health

PB - Springer Japan

ER -

Posttranslational modification of proteins

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this