Phosphoproteomics: searching for a needle in a haystack
Language English Country Netherlands Media print-electronic
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't, Review
PubMed
21839867
DOI
10.1016/j.jprot.2011.07.018
PII: S1874-3919(11)00339-3
Knihovny.cz E-resources
- MeSH
- Apoptosis physiology MeSH
- Cell Differentiation physiology MeSH
- Cell Division physiology MeSH
- Phosphoproteins analysis metabolism MeSH
- Phosphorylation physiology MeSH
- Mass Spectrometry methods MeSH
- Humans MeSH
- Peptides analysis metabolism MeSH
- Proteomics methods MeSH
- Gene Expression Regulation physiology MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Comparative Study MeSH
- Names of Substances
- Phosphoproteins MeSH
- Peptides MeSH
Most of the cellular processes are regulated by reversible phosphorylation of proteins, which in turn plays a critical role in the regulation of gene expression, cell division, signal transduction, metabolism, differentiation, and apoptosis. Mass spectrometry of phosphopeptides obtained from tryptic protein digests has become a powerful tool for characterization of phosphoproteins involved in these processes. However, there is a general need to significantly enrich the phosphopeptide content to compensate their low abundance, insufficient ionization, and suppression effects of non-phosphorylated peptides. This paper aims to give a comprehensive overview on the methods involved in recent phosphoproteomics. It presents a description of contemporary enrichment techniques with references to particular studies and compares different approaches to characterization of phosphoproteome by mass spectrometry.
References provided by Crossref.org
Amorphous TiO2 Nanotubes as a Platform for Highly Selective Phosphopeptide Enrichment
