Source:http://linkedlifedata.com/resource/pubmed/id/19016432
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
2008-11-21
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| pubmed:abstractText |
Protein lysine acetylation, referring to acetylation of the epsilon-amino group of a lysine residue, has recently emerged as an important post-translational modification for regulating protein functions in various organisms. Like phosphorylation, lysine acetylation is a rapidly reversible and precisely controlled covalent modification that serves as a simple on/off switch or participates in a codified manner with other post-translational modifications to regulate protein functions in different cellular and developmental processes. This unit describes and discusses methods used for in vitro and in vivo determination of lysine acetylation.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
1934-3663
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 2008 by John Wiley & Sons, Inc.
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| pubmed:issnType |
Electronic
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| pubmed:volume |
Chapter 14
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
Unit 14.11
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| pubmed:meshHeading |
pubmed-meshheading:19016432-Acetylation,
pubmed-meshheading:19016432-Autoradiography,
pubmed-meshheading:19016432-Biochemistry,
pubmed-meshheading:19016432-Cellulose,
pubmed-meshheading:19016432-Humans,
pubmed-meshheading:19016432-Lysine,
pubmed-meshheading:19016432-Protein Processing, Post-Translational,
pubmed-meshheading:19016432-Proteins,
pubmed-meshheading:19016432-Radioactivity
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| pubmed:year |
2008
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| pubmed:articleTitle |
Analysis of protein lysine acetylation in vitro and in vivo.
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| pubmed:affiliation |
Rosalind and Morris Goodman Cancer Center and Department of Medicine, McGill University, Montreal, Canada.
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| pubmed:publicationType |
Journal Article
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