Results 181 to 190 of about 17,544 (219)
Some of the next articles are maybe not open access.

iTRAQ-Labeling for Biomarker Discovery

2013
Various mass-tagging approaches have been developed over the last few years that have enabled mass spectrometry-based relative and absolute quantification of proteins from complex samples. This, in turn, has facilitated proteomics research to address issues ranging from alterations in the proteome of various model systems in response to various stimuli
Leroi V, Desouza   +2 more
openaire   +2 more sources

Evaluating Cellular Viability by iTRAQ Proteomic Profiling

2023
Cellular health, functionality, response to environment, and other variables affecting cell, tissue, or organ viability are reflected in the cellular proteomes and metabolomes. These "omic" profiles are in constant flux even during normal cellular functioning, to maintain cellular homeostasis, in response to small environmental changes and maintenance ...
Anne, Poljak   +2 more
openaire   +2 more sources

iTRAQ-Based Proteomic Analysis of Rice Grains

2020
Cereal proteins have formed the basis of human diet worldwide, and their level of consumption is expected to increase. The knowledge of the protein composition and variation of the cereal grains is helpful for characterizing cereal varieties and to identify biomarkers for tolerance mechanisms.
Marouane, Baslam   +2 more
openaire   +2 more sources

iTRAQ-based proteomics reveals novel biomarkers of osteoarthritis [PDF]

open access: yesBiomarkers, 2013
We performed comprehensive proteomic analyses of articular cartilage by using the isobaric tags for relative and absolute quantitation (iTRAQ) method, and searched for candidate biomarkers for osteoarthritis (OA).Articular cartilage was collected from patients with OA or femoral neck fracture for the control group. Molecular variations were detected by
Daiki Ikeda   +2 more
exaly   +3 more sources

Optimized Fragmentation Conditions for iTRAQ-labeled Phosphopeptides

Journal of Proteome Research, 2013
Protein phosphorylation is an important post-translational modification that plays a regulatory role within numerous biological processes. The simultaneous identification, localization, and quantification of phosphorylated proteins is vital for understanding this dynamic control mechanism.
Dennis, Linke   +3 more
openaire   +2 more sources

On the iTRAQ of kinase inhibitors

Nature Biotechnology, 2007
Cellular targets of kinase inhibitors are identified by mass spectrometric analysis of binding to “kinobeads.”
openaire   +1 more source

iTRAQ Experimental Design for Plasma Biomarker Discovery

Journal of Proteome Research, 2008
There is considerable interest in using mass spectrometry for biomarker discovery in human blood plasma. We investigated aspects of experimental design for large studies that require analysis of multiple sample sets using iTRAQ reagents for sample multiplexing and quantitation.
Xiaomin, Song   +6 more
openaire   +2 more sources

Practical Integration of Multi-Run iTRAQ Data

2019
In this chapter, we describe some of the approaches we employ in the analysis of iTRAQ data in our group, with an emphasis on practical issues that can occur in larger multi-run projects. Our pipeline starts with a well-established iTRAQ workflow, makes use of protein level quantitation using ProteinPilot, and continues either via a global analysis in ...
Dana, Pascovici   +4 more
openaire   +2 more sources

iTRAQ comparison of proteomic profiles of endometrial receptivity

Journal of Proteomics, 2019
Endometrial receptivity is a limiting step in human reproduction. A disruption in the development of endometrial receptivity is responsible for recurrent implantation failures (RIF) of endometrial origin. To understand the molecular mechanisms behind the endometrial receptivity process, we used the isobaric tag for relative and absolute quantitation ...
Pérez Debén, Silvia   +7 more
openaire   +4 more sources

Novel method to investigate protein carbonylation by iTRAQ strategy

open access: yesAnalytical and Bioanalytical Chemistry, 2012
This paper reports a novel methodology for relative quantitative analysis of carbonylation sites in proteins by exploiting a new isobaric tag for relative and absolute quantitation (iTRAQ) derivative, iTRAQ hydrazide (iTRAQH), and the analytical power of linear ion trap instruments (QqLIT). Because of its operational simplicity, avoiding time-consuming
Gennaro Marino   +2 more
exaly   +4 more sources

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