Results 221 to 230 of about 12,092 (240)
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The phosphoproteomics data explosion
Current Opinion in Chemical Biology, 2009There are likely more than 500000 potential phosphorylation sites in a cellular proteome. This dynamic phosphorylation is under tight control of a variety of kinases and phosphatases. In recent years significant progress has been made in the large-scale analysis of these in vitro and in vivo protein phosphorylation events.
Lemeer, S.M., Heck, A.J.R.
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Plant phosphoproteomics: An update
PROTEOMICS, 2009Abstract Phosphoproteomics involves identification of phosphoproteins, precise mapping, and quantification of phosphorylation sites, and eventually, revealing their biological function. In plants, several systematic phosphoproteomic analyses have recently been performed to optimize in vitro
Kersten, B. +6 more
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Analysis of the Subcellular Phosphoproteome Using a Novel Phosphoproteomic Reactor
Journal of Proteome Research, 2010Protein phosphorylation is an important post-translational modification involved in the regulation of many cellular processes. Mass spectrometry has been successfully used to identify protein phosphorylation in specific pathways and for global phosphoproteomic analysis.
Houjiang, Zhou +8 more
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Phosphoproteomics in drug discovery
Drug Discovery Today, 2014Several important aspects of the drug discovery process, including target identification, mechanism of action determination and biomarker identification as well as drug repositioning, require complete understanding of the effects of drugs on protein phosphorylation in relevant biological systems.
Melody K. Morris +3 more
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DIGE-Based Phosphoproteomic Analysis
2017Here, we describe the detailed step-by-step protocol for detection of phosphoproteins in two-dimensional difference gel electrophoresis (DIGE) gels. A standard DIGE protocol is combined with subsequent post-staining with phosphospecific fluorescent dye.
Taras, Stasyk, Lukas Alfons, Huber
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Phosphoproteomics in photosynthetic organisms
ELECTROPHORESIS, 2014As primarily sessile organisms, photosynthetic species survive in dynamic environments by using elegant signaling pathways to manifest molecular responses to extracellular cues. These pathways exploit phosphorylation of specific amino acids (e.g. serine, threonine, tyrosine), which impact protein structure, function, and localization.
William O, Slade +3 more
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Databases for Plant Phosphoproteomics
2015Phosphorylation is the most studied posttranslational modification involved in signal transduction in stress responses, development, and growth. In the recent years large-scale phosphoproteomic studies were carried out using various model plants and several growth and stress conditions.
Waltraud X, Schulze +2 more
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Phosphoproteomic Analysis of Peptides
2013Posttranslational modifications represent a major mechanism by which cells control molecular events. Sample preparation is one of the biggest keys in terms of proteomic analysis, and especially when looking at phosphoproteomics. Here we describe two techniques that are used to identify phosphopeptides.
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Phosphoproteome Analysis in Yeast
2003Publisher Summary This chapter describes yeast phosphoproteome analysis using the specific example of the effects of the Reg1p regulatory subunit of Glc7p (PP-1C) on the yeast phosphoproteome. The chapter presents genomics and proteomics linked in order to determine the direct effects of a given gene product.
Rupa, Ray, Timothy A, Haystead
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SILAC-Based Temporal Phosphoproteomics
2014In recent years, thanks to advances in Mass Spectrometry (MS)-based quantitative proteomics, studies on signaling pathways have moved from a detailed description of individual components to system-wide analysis of entire signaling cascades, also providing spatio-temporal views of intracellular pathways.
Francavilla, Chiara +3 more
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