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Statements

Subject Item
n2:RIV%2F62156489%3A43210%2F13%3A00200669%21RIV15-MSM-43210___
rdf:type
skos:Concept n19:Vysledek
rdfs:seeAlso
http://www.sciencedirect.com/science/article/pii/S1874391913003254
dcterms:description
Posttranslational modifications (PTMs) of proteins represent fascinating extensions of the dynamic complexity of living cells' proteomes. The results of enzymatically catalyzed or spontaneous chemical reactions, PTMs form a fourth tier in the gene -- transcript -- protein cascade, and contribute not only to proteins' biological functions, but also to challenges in their analysis. There have been tremendous advances in proteomics during the last decade. Identification and mapping of PTMs in proteins have improved dramatically, mainly due to constant increases in the sensitivity, speed, accuracy and resolution of mass spectrometry (MS). However, it is also becoming increasingly evident that simple gel-free shotgun MS profiling is unlikely to suffice for comprehensive detection and characterization of proteins and/or protein modifications present in low amounts. Here, we review current approaches for enriching and separating posttranslationally modified proteins, and their MS-independent detection. First, we discuss general approaches for proteome separation, fractionation and enrichment. We then consider the commonest forms of PTMs (phosphorylation, glycosylation and glycation, lipidation, methylation, acetylation, deamidation, ubiquitination and various redox modifications), and the best available methods for detecting and purifying proteins carrying these PTMs. This article is part of a Special Issue entitled: Protein Modifications. Posttranslational modifications (PTMs) of proteins represent fascinating extensions of the dynamic complexity of living cells' proteomes. The results of enzymatically catalyzed or spontaneous chemical reactions, PTMs form a fourth tier in the gene -- transcript -- protein cascade, and contribute not only to proteins' biological functions, but also to challenges in their analysis. There have been tremendous advances in proteomics during the last decade. Identification and mapping of PTMs in proteins have improved dramatically, mainly due to constant increases in the sensitivity, speed, accuracy and resolution of mass spectrometry (MS). However, it is also becoming increasingly evident that simple gel-free shotgun MS profiling is unlikely to suffice for comprehensive detection and characterization of proteins and/or protein modifications present in low amounts. Here, we review current approaches for enriching and separating posttranslationally modified proteins, and their MS-independent detection. First, we discuss general approaches for proteome separation, fractionation and enrichment. We then consider the commonest forms of PTMs (phosphorylation, glycosylation and glycation, lipidation, methylation, acetylation, deamidation, ubiquitination and various redox modifications), and the best available methods for detecting and purifying proteins carrying these PTMs. This article is part of a Special Issue entitled: Protein Modifications.
dcterms:title
Advances in purification and separation of posttranslationally modified proteins Advances in purification and separation of posttranslationally modified proteins
skos:prefLabel
Advances in purification and separation of posttranslationally modified proteins Advances in purification and separation of posttranslationally modified proteins
skos:notation
RIV/62156489:43210/13:00200669!RIV15-MSM-43210___
n3:aktivita
n17:P
n3:aktivity
P(ED1.1.00/02.0068), P(EE2.3.30.0017), P(GAP305/12/2144)
n3:cisloPeriodika
30 October 2013
n3:dodaniDat
n10:2015
n3:domaciTvurceVysledku
n4:7777388 n4:6195601 n4:9071105 n4:3006484
n3:druhVysledku
n15:J
n3:duvernostUdaju
n7:S
n3:entitaPredkladatele
n11:predkladatel
n3:idSjednocenehoVysledku
59649
n3:idVysledku
RIV/62156489:43210/13:00200669
n3:jazykVysledku
n14:eng
n3:klicovaSlova
protein purification; protein modification; proteome
n3:klicoveSlovo
n20:protein%20purification n20:proteome n20:protein%20modification
n3:kodStatuVydavatele
NL - Nizozemsko
n3:kontrolniKodProRIV
[AFEAEE2A4C64]
n3:nazevZdroje
Journal of Proteomics
n3:obor
n13:CE
n3:pocetDomacichTvurcuVysledku
4
n3:pocetTvurcuVysledku
4
n3:projekt
n5:ED1.1.00%2F02.0068 n5:EE2.3.30.0017 n5:GAP305%2F12%2F2144
n3:rokUplatneniVysledku
n10:2013
n3:svazekPeriodika
92
n3:tvurceVysledku
Brzobohatý, Břetislav Černý, Martin Skalák, Jan Černá, Hana
n3:wos
328518000002
s:issn
1874-3919
s:numberOfPages
26
n18:doi
10.1016/j.jprot.2013.05.040
n16:organizacniJednotka
43210