Results 211 to 220 of about 12,092 (240)
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Current Protocols in Protein Science, 2007
AbstractProtein phosphorylation is one of the most important mechanisms of regulating protein function in cells, and it plays an important role in controlling diverse biological processes, including cellular proliferation, migration, and metabolism.
Jun, Zhong +2 more
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AbstractProtein phosphorylation is one of the most important mechanisms of regulating protein function in cells, and it plays an important role in controlling diverse biological processes, including cellular proliferation, migration, and metabolism.
Jun, Zhong +2 more
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WIREs Systems Biology and Medicine, 2010
AbstractCurrent analytical protein methods show phosphorylation to be the most ubiquitous, evolutionary conserved post‐translational modification Post‐Translational Modification (PTM). The reversible and transient nature of protein phosphorylation allows signal transduction pathways to carry out diverse cellular functions.
Nurhan, Ozlu +5 more
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AbstractCurrent analytical protein methods show phosphorylation to be the most ubiquitous, evolutionary conserved post‐translational modification Post‐Translational Modification (PTM). The reversible and transient nature of protein phosphorylation allows signal transduction pathways to carry out diverse cellular functions.
Nurhan, Ozlu +5 more
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Mass Spectrometry Reviews, 2010
AbstractProtein phosphorylation represents one of the most extensively studied post‐translational modifications, primarily due to the emergence of sensitive methods enabling the detection of this modification both in vitro and in vivo. The availability of enrichment methods combined with sensitive mass spectrometry instrumentation has played a crucial ...
Trost, Matthias +3 more
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AbstractProtein phosphorylation represents one of the most extensively studied post‐translational modifications, primarily due to the emergence of sensitive methods enabling the detection of this modification both in vitro and in vivo. The availability of enrichment methods combined with sensitive mass spectrometry instrumentation has played a crucial ...
Trost, Matthias +3 more
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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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