About: Enrichment strategies for phosphoproteomics: state-of-the-art

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Enrichment strategies for phosphoproteomics: state-of-the-art Goto Sponge Distinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://dx.doi.org/10.1515/revac-2011-0025
Description	Protein phosphorylation is a key regulator in many biological processes, such as homeostasis, cellular signaling and communication, transcriptional and translational regulation, and apoptosis. The defects in this tightly controlled reversible post-translational modification have been described to contribute to genesis and progression of various diseases, emphasizing the importance of a systematic research of this phenomenon. Although considerable effort has been devoted to improving the analysis of phosphorylation by mass spectrometry, which is currently the method of choice to study protein phosphorylation, the detection and identification of phosphorylation sites remains challenging because of the low abundance and low ionization efficacy of phosphoproteins in comparison with nonphosphorylated proteins. To overcome this obstacle, different enrichment strategies for phosphorylated peptides/proteins have been established and optimized for subsequent mass spectrometry analysis. In this review, we will give an overview of the methods currently available for the enrichment of phosphorylated proteins and peptides including immunoprecipitation, chemical derivatization and affinity enrichment techniques. Protein phosphorylation is a key regulator in many biological processes, such as homeostasis, cellular signaling and communication, transcriptional and translational regulation, and apoptosis. The defects in this tightly controlled reversible post-translational modification have been described to contribute to genesis and progression of various diseases, emphasizing the importance of a systematic research of this phenomenon. Although considerable effort has been devoted to improving the analysis of phosphorylation by mass spectrometry, which is currently the method of choice to study protein phosphorylation, the detection and identification of phosphorylation sites remains challenging because of the low abundance and low ionization efficacy of phosphoproteins in comparison with nonphosphorylated proteins. To overcome this obstacle, different enrichment strategies for phosphorylated peptides/proteins have been established and optimized for subsequent mass spectrometry analysis. In this review, we will give an overview of the methods currently available for the enrichment of phosphorylated proteins and peptides including immunoprecipitation, chemical derivatization and affinity enrichment techniques. (en)
Title	Enrichment strategies for phosphoproteomics: state-of-the-art Enrichment strategies for phosphoproteomics: state-of-the-art (en)
skos:prefLabel	Enrichment strategies for phosphoproteomics: state-of-the-art Enrichment strategies for phosphoproteomics: state-of-the-art (en)
skos:notation	RIV/00216208:11150/12:10124171!RIV13-MSM-11150___
http://linked.open...avai/predkladatel	Lékařská fakulta v Hradci Králové
http://linked.open...avai/riv/aktivita	I P
http://linked.open...avai/riv/aktivity	I, P(GPP206/12/P338)
http://linked.open...iv/cisloPeriodika	1
http://linked.open...vai/riv/dodaniDat	2013
http://linked.open...aciTvurceVysledku	Řezáčová, Martina Tichý, Aleš Šalovská, Barbora
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Karlova v Praze / Lékařská fakulta v Hradci Králové
http://linked.open...dnocenehoVysledku	134461
http://linked.open...ai/riv/idVysledku	RIV/00216208:11150/12:10124171
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	phosphoproteomics; phosphopeptide enrichment; metal oxide affinity chromatography (en)
http://linked.open.../riv/klicoveSlovo	phosphopeptide enrichment metal oxide affinity chromatography phosphoproteomics
http://linked.open...odStatuVydavatele	IL - Stát Izrael
http://linked.open...ontrolniKodProRIV	[D5B638C43E33]
http://linked.open...i/riv/nazevZdroje	Reviews in Analytical Chemistry
http://linked.open...in/vavai/riv/obor	CB
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	5 (xsd:int)
http://linked.open...vavai/riv/projekt	Analýza fosfoproteomu leukemických buněčných linií po ozáření.
http://linked.open...UplatneniVysledku	2012
http://linked.open...v/svazekPeriodika	31
http://linked.open...iv/tvurceVysledku	Novotná, Eva Tichý, Aleš Vávrová, Jiřina Řezáčová, Martina Šalovská, Barbora
http://linked.open...ain/vavai/riv/wos	000305195900004
issn	0793-0135
number of pages	13 (xsd:int)
http://bibframe.org/vocab/doi	10.1515/revac-2011-0025
http://localhost/t...ganizacniJednotka	11150
is http://linked.open...avai/riv/vysledek of	Enrichment strategies for phosphoproteomics: state-of-the-art

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 84 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software