Results 171 to 180 of about 17,544 (219)
Identification of candidate genes and proteins for tasseling stage drought tolerance through integrated transcriptomic and proteomic analysis approach in maize. [PDF]
Liu S +8 more
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Overexpression of Transferrin Receptor in Esophageal Squamous Cell Cancer Suggests Poor Prognosis and Potential Therapy. [PDF]
Ikenaga N +16 more
europepmc +1 more source
Rebalancing the seed proteome following deletion of vicilin-related genes in pea (Pisum sativum L.). [PDF]
Rayner T +14 more
europepmc +1 more source
iTRAQ protein quantification: A quality‐controlled workflow
AbstractReporter 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.
Albert Sickmann +2 more
exaly +4 more sources
A Statistical Model for iTRAQ Data Analysis [PDF]
We describe biological and experimental factors that induce variability in reporter ion peak areas obtained from iTRAQ experiments. We demonstrate how these factors can be incorporated into a statistical model for use in evaluating differential protein expression and highlight the benefits of using analysis of variance to quantify fold change.
Kevin Schey +2 more
exaly +3 more sources
Shotgun proteomics using the iTRAQ isobaric tags [PDF]
Shotgun proteomic methods involving isobaric tagging of peptides enable high-throughput proteomic analysis. iTRAQ reagents allow simultaneous identification and quantitation of proteins in four different samples using tandem mass spectrometry (MS). In this article, we provide a brief description of proteome analysis using iTRAQ reagents and review the ...
Kelvin H Lee, Leila H Choe
exaly +3 more sources
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2011
The identification of phosphorylation on proteins has become practicable for many laboratories in recent years, largely due to improvements in mass spectrometry (MS) and the development of methods to selectively enrich for phosphorylated peptides and proteins.
Alexandra M E, Jones, Thomas S, Nühse
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The identification of phosphorylation on proteins has become practicable for many laboratories in recent years, largely due to improvements in mass spectrometry (MS) and the development of methods to selectively enrich for phosphorylated peptides and proteins.
Alexandra M E, Jones, Thomas S, Nühse
openaire +2 more sources
Current Protocols in Plant Biology, 2017
AbstractWe present a simple one‐pot extraction protocol, which rapidly isolates hydrophilic metabolites, lipids, and proteins from the same pulverized plant sample. Also detailed is a global plant proteomics sample preparation method utilizing iTRAQ multiplexing reagents that enables deep proteome coverage due to the use of HPLC fractionation of the ...
Pubudu P. Handakumbura +4 more
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AbstractWe present a simple one‐pot extraction protocol, which rapidly isolates hydrophilic metabolites, lipids, and proteins from the same pulverized plant sample. Also detailed is a global plant proteomics sample preparation method utilizing iTRAQ multiplexing reagents that enables deep proteome coverage due to the use of HPLC fractionation of the ...
Pubudu P. Handakumbura +4 more
openaire +1 more source
Dissecting the iTRAQ Data Analysis
2016In the era of large-scale quantitative biology, mass spectrometry-based quantitative proteomics is progressively becoming indispensable for gaining insights into the biological systems at molecular level. Various quantitative study designs rely on chemical tagging approaches to study disease, stress, or drug response and temporal studies aiming at ...
Suruchi, Aggarwal, Amit Kumar, Yadav
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Quantification of Proteins by iTRAQ
2010Protein relative quantification is a key facet of many proteomics experiments. Several methods exist for this type of work, some of which are described elsewhere in this volume. In this chapter we will describe the use of isobaric tags for relative and absolute quantification (iTRAQ).
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