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iTRAQ protein quantification: a quality-controlled workflow

Julia M Burkhart, Marc Vaudel, ReneP Zahedi, Lennart Martens UGent and Albert Sickmann (2011) PROTEOMICS. 11(6). p.1125-1134
abstract
Reporter ion-based methods are among the major techniques to quantify peptides and proteins. Two main labels, tandem mass tag (TMT) and iTRAQ, are widely used by the proteomics community. They are, however, often applied as out-of-the-box methods, without thorough quality control. Thus, due to undiscovered limitations of the technique, irrelevant results might be trusted. To address this issue, we here propose a step-by-step quality control of the iTRAQ workflow. From sample preparation to final ratio calculation we provide metrics and techniques assessing the actual effectiveness of iTRAQ quantification as well as a novel method for more reliable protein ratio estimation.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
ORBITRAP, STRATEGY, ABUNDANCE, DATABASES, IDENTIFICATION, PEPTIDE, ISOBARIC TAGS, COMPARATIVE PROTEOMICS, ABSOLUTE QUANTIFICATION, MASS-SPECTROMETRY, Quantification, Mass spectrometry, ORBITRAP, iTRAQ
journal title
PROTEOMICS
Proteomics
volume
11
issue
6
pages
1125 - 1134
Web of Science type
Article
Web of Science id
000288137700015
JCR category
BIOCHEMICAL RESEARCH METHODS
JCR impact factor
4.505 (2011)
JCR rank
14/72 (2011)
JCR quartile
1 (2011)
ISSN
1615-9853
DOI
10.1002/pmic.201000711
project
Bioinformatics: from nucleotids to networks (N2N)
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1197848
handle
http://hdl.handle.net/1854/LU-1197848
date created
2011-03-28 11:38:43
date last changed
2016-12-19 15:46:03
@article{1197848,
  abstract     = {Reporter ion-based methods are among the major techniques to quantify peptides and proteins. Two main labels, tandem mass tag (TMT) and iTRAQ, are widely used by the proteomics community. They are, however, often applied as out-of-the-box methods, without thorough quality control. Thus, due to undiscovered limitations of the technique, irrelevant results might be trusted. To address this issue, we here propose a step-by-step quality control of the iTRAQ workflow. From sample preparation to final ratio calculation we provide metrics and techniques assessing the actual effectiveness of iTRAQ quantification as well as a novel method for more reliable protein ratio estimation.},
  author       = {Burkhart, Julia M and Vaudel, Marc and Zahedi, ReneP and Martens, Lennart and Sickmann, Albert},
  issn         = {1615-9853},
  journal      = {PROTEOMICS},
  keyword      = {ORBITRAP,STRATEGY,ABUNDANCE,DATABASES,IDENTIFICATION,PEPTIDE,ISOBARIC TAGS,COMPARATIVE PROTEOMICS,ABSOLUTE QUANTIFICATION,MASS-SPECTROMETRY,Quantification,Mass spectrometry,ORBITRAP,iTRAQ},
  language     = {eng},
  number       = {6},
  pages        = {1125--1134},
  title        = {iTRAQ protein quantification: a quality-controlled workflow},
  url          = {http://dx.doi.org/10.1002/pmic.201000711},
  volume       = {11},
  year         = {2011},
}

Chicago
Burkhart, Julia M, Marc Vaudel, ReneP Zahedi, Lennart Martens, and Albert Sickmann. 2011. “iTRAQ Protein Quantification: a Quality-controlled Workflow.” Proteomics 11 (6): 1125–1134.
APA
Burkhart, J. M., Vaudel, M., Zahedi, R., Martens, L., & Sickmann, A. (2011). iTRAQ protein quantification: a quality-controlled workflow. PROTEOMICS, 11(6), 1125–1134.
Vancouver
1.
Burkhart JM, Vaudel M, Zahedi R, Martens L, Sickmann A. iTRAQ protein quantification: a quality-controlled workflow. PROTEOMICS. 2011;11(6):1125–34.
MLA
Burkhart, Julia M, Marc Vaudel, ReneP Zahedi, et al. “iTRAQ Protein Quantification: a Quality-controlled Workflow.” PROTEOMICS 11.6 (2011): 1125–1134. Print.