Results 231 to 240 of about 20,263 (273)
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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
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Phosphoproteome of Cryptococcus neoformans
Journal of Proteomics, 2014Cryptococcus neoformans is an encapsulated pathogenic yeast, which causes life threatening meningitis in immunocompromised individuals. C. neoformans var. grubii is the most prevalent and virulent form among the two varieties of C. neoformans - C. neoformans var. grubii and C. neoformans var. neoformans. The virulence of C.
Lakshmi Dhevi N, Selvan +10 more
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Illuminating the dark phosphoproteome
Science Signaling, 2019Identifying the targets of “dark” kinases will provide new biological and disease insights.
Elise J. Needham +4 more
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Phosphoproteomics takes it easy
Nature Biotechnology, 2015The EasyPhos pipeline simplifies analysis of phosphorylation-dependent signaling networks at high temporal resolution.
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2015
Cereals are the most important crop plant supplying staple food throughout the world. The economic importance and continued breeding of crop plants such as rice, maize, wheat, or barley require a detailed scientific understanding of adaptive and developmental processes.
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Cereals are the most important crop plant supplying staple food throughout the world. The economic importance and continued breeding of crop plants such as rice, maize, wheat, or barley require a detailed scientific understanding of adaptive and developmental processes.
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2020
In contrast to the canonical phosphoproteomes (P-Ser, P-Thr, P-Tyr), the noncanonial phosphoproteomes include phosphorylated side chains not typically acid-stable and thus often missed in standard phosphopeptide mass spectrometry protocols. In this regard the N-phosphohistidinyl residues, the beta aspartyl-phosphate residues, and the S-phosphocysteinyl
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In contrast to the canonical phosphoproteomes (P-Ser, P-Thr, P-Tyr), the noncanonial phosphoproteomes include phosphorylated side chains not typically acid-stable and thus often missed in standard phosphopeptide mass spectrometry protocols. In this regard the N-phosphohistidinyl residues, the beta aspartyl-phosphate residues, and the S-phosphocysteinyl
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Phosphoproteomics and cancer research
Clinical and Translational Oncology, 2009Protein phosphorylation plays key roles in the regulation of normal and cancer cells. It is a highly dynamic process. Protein kinases are the targets of several new cancer drugs and drug candidates. However, some of the main issues related to new drugs are how they function and the selection of those patients that will likely respond best to a ...
Ashman, Keith, Lopez Villar, Elena
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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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