onr:"swepub:oai:lup.lub.lu.se:25eaed71-39ec-4d69-be63-403d1212d6e3"
Search: onr:"swepub:oai:lup.lub.lu.se:25eaed71-39ec-4d69-be63-403d1212d6e3" > Lysine Acetylation ...
- 1 of 1
- Previous record
- Next record
- To hitlist
Lysine Acetylation Stoichiometry Analysis at the Proteome Level
-
- Gil, Jeovanis (author)
- Lund University,Lunds universitet,LUCC: Lunds universitets cancercentrum,Övriga starka forskningsmiljöer,Biomarkörer och Epi,Sektion I,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,LUCC: Lund University Cancer Centre,Other Strong Research Environments,Biomarkers and epidemiology,Section I,Department of Clinical Sciences, Lund,Faculty of Medicine
-
- Encarnación-Guevara, Sergio (author)
- National Autonomous University of Mexico
- (creator_code:org_t)
- 2021-12-15
- 2022
- English 14 s.
- In: Methods in Molecular Biology. - New York, NY : Springer US. - 1064-3745 .- 1940-6029. ; 2420, s. 73-86
- Book chapter (peer-reviewed)
Abstract
Subject headings
Close
- Lysine acetylation is a widespread posttranslational modification (PTM) in all kingdoms of live. A large number of proteins involved in most of biological pathways are targets of this PTM. The lysine acetylation is a reversible modification controlled by two main groups of enzymes, lysine acetyltransferases responsible for transferring the acetyl group of acetylCoA to the side chain of lysine residues and lysine deacetylases which effectively remove the acetyl tag. Dysregulation of enzymes that control acetylation and/or target proteins have been associated with a growing number of human pathologies. Lysine acetylation is largely a modification that occurs at low stoichiometry at its target sites. Here we describe a method to identify lysine acetylation sites and estimate their site occupancy at the proteome scale. The method relies on a high-resolution mass spectrometry-based proteomics approach, which includes a specific chemical acetylation reaction on unmodified lysine residues that carry heavy isotopes. The procedures described here have been applied to cell line cultures and to clinically relevant samples stored as both snap-frozen and formalin-fixed paraffin-embedded (FFPE) tissues.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- Cell lines
- FFPE tissue
- Frozen tissue
- Lysine acetylation
- Mass spectrometry-based proteomics
- N-acetoxysuccinimide-d3
- Stoichiometry
Publication and Content Type
- kap (subject category)
- ref (subject category)
Find in a library
- Methods in Molecular Biology (Search for host publication in LIBRIS)
To the university's database
- 1 of 1
- Previous record
- Next record
- To hitlist
Find more in SwePub
- By the author/editor
- Gil, Jeovanis
- Encarnación-Guev ...
- About the subject
-
- NATURAL SCIENCES
- NATURAL SCIENCES
- and Biological Scien ...
- and Biochemistry and ...
- Articles in the publication
- Methods in Molec ...
- By the university
- Lund University
Search outside SwePub
- Extend your search to:
- Google Book Search
- Google Scholar
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.
- Copyright © LIBRIS - National Library Systems
- LIBRIS.kb.se
