The good, the bad, the ugly: Validating the mass spectrometric analysis of modified peptides

被引：24

作者：

Beck, Florian ^{[1
]}

Lewandrowski, Urs ^{[1
]}

Wiltfang, Matthias ^{[1
]}

Feldmann, Ingo ^{[1
]}

Geiger, Joerg ^{[2
]}

Sickmann, Albert ^{[1
,3
]}

Zahedi, Rene Peiman ^{[1
]}

机构：

[1] Leibniz Inst Analyt Wissensch ISAS eV, D-44139 Dortmund, Germany

[2] Univ Wurzburg, Inst Clin Biochem & Pathobiochem, D-97070 Wurzburg, Germany

[3] Ruhr Univ Bochum, Med Proteom Ctr MPC, Bochum, Germany

来源：

PROTEOMICS | 2011年 / 11卷 / 06期

关键词：

Glycosylation; Label-free; Phosporylation; Quality control; Quantification; Technology; N-LINKED GLYCOPROTEINS; OPEN-SOURCE LIBRARY; PROTEOMICS; MS/MS; ACID; MS; PHOSPHOPROTEOME; QUANTIFICATION; IDENTIFICATION; DEAMIDATION;

D O I：

10.1002/pmic.201000562

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Mass spectrometric characterization of protein modifications is usually based on single peptides. With the advent of large-scale PTM-focussed MS studies, vast amounts of data are generated continuously, providing biologists extremely valuable and virtually never-ending sources for targeted functional research. However, even more than for proteomics in general, appropriate strategies for quality control of the different steps of the analytical strategy are imperative to prevent functional researchers from doing Sisyphos work on false-positive and unconfident PTM assignments. Here, we describe strategies to address the important issue of quality control for PTM analysis on various levels of the analytical pipeline: sample preparation/processing, analysis/identification and finally data interpretation, for qualitative as well as quantitative studies.

引用

页码：1099 / 1109

页数：11

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