Adenylylation

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Adenylylation : renaissance of a forgotten post-translational modification. / Itzen, Aymelt; Blankenfeldt, Wulf; Goody, Roger S.

in: TRENDS BIOCHEM SCI, Jahrgang 36, Nr. 4, 04.2011, S. 221-8.

Publikationen: SCORING: Beitrag in Fachzeitschrift/ZeitungSCORING: ReviewForschung

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@article{a6c0b406f1f84d0aa9a633ed80d8273a,
title = "Adenylylation: renaissance of a forgotten post-translational modification",
abstract = "The stable post-translational modification of proteins by adenylylation or uridylylation was discovered more than four decades ago as a mechanism to regulate the activity of enzymes. Although many other processes involving the covalent transfer of an AMP residue to an amino acid side chain have been identified since then, these are transient adenylylation events that essentially use the free energy of ATP hydrolysis to activate specific processes. Recently, new examples of stable adenylylation of small GTPases involved in signal transduction and regulation of cellular events were discovered, which appear to modulate downstream processes such as cytoskeletal rearrangement and vesicular trafficking. We present a survey of the historical and modern phases of research in this area, focusing on the common and differing aspects of protein adenylylation.",
keywords = "Adenine, Adenosine Monophosphate, Animals, Glutamate Synthase, Humans, Protein Processing, Post-Translational, Proteins, Journal Article, Research Support, Non-U.S. Gov't, Review",
author = "Aymelt Itzen and Wulf Blankenfeldt and Goody, {Roger S}",
note = "Copyright {\textcopyright} 2010 Elsevier Ltd. All rights reserved.",
year = "2011",
month = apr,
doi = "10.1016/j.tibs.2010.12.004",
language = "English",
volume = "36",
pages = "221--8",
journal = "TRENDS BIOCHEM SCI",
issn = "0968-0004",
publisher = "Elsevier Limited",
number = "4",

}

RIS

TY - JOUR

T1 - Adenylylation

T2 - renaissance of a forgotten post-translational modification

AU - Itzen, Aymelt

AU - Blankenfeldt, Wulf

AU - Goody, Roger S

N1 - Copyright © 2010 Elsevier Ltd. All rights reserved.

PY - 2011/4

Y1 - 2011/4

N2 - The stable post-translational modification of proteins by adenylylation or uridylylation was discovered more than four decades ago as a mechanism to regulate the activity of enzymes. Although many other processes involving the covalent transfer of an AMP residue to an amino acid side chain have been identified since then, these are transient adenylylation events that essentially use the free energy of ATP hydrolysis to activate specific processes. Recently, new examples of stable adenylylation of small GTPases involved in signal transduction and regulation of cellular events were discovered, which appear to modulate downstream processes such as cytoskeletal rearrangement and vesicular trafficking. We present a survey of the historical and modern phases of research in this area, focusing on the common and differing aspects of protein adenylylation.

AB - The stable post-translational modification of proteins by adenylylation or uridylylation was discovered more than four decades ago as a mechanism to regulate the activity of enzymes. Although many other processes involving the covalent transfer of an AMP residue to an amino acid side chain have been identified since then, these are transient adenylylation events that essentially use the free energy of ATP hydrolysis to activate specific processes. Recently, new examples of stable adenylylation of small GTPases involved in signal transduction and regulation of cellular events were discovered, which appear to modulate downstream processes such as cytoskeletal rearrangement and vesicular trafficking. We present a survey of the historical and modern phases of research in this area, focusing on the common and differing aspects of protein adenylylation.

KW - Adenine

KW - Adenosine Monophosphate

KW - Animals

KW - Glutamate Synthase

KW - Humans

KW - Protein Processing, Post-Translational

KW - Proteins

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

KW - Review

U2 - 10.1016/j.tibs.2010.12.004

DO - 10.1016/j.tibs.2010.12.004

M3 - SCORING: Review article

C2 - 21256032

VL - 36

SP - 221

EP - 228

JO - TRENDS BIOCHEM SCI

JF - TRENDS BIOCHEM SCI

SN - 0968-0004

IS - 4

ER -