Results 141 to 150 of about 14,675 (189)
Scalable phosphotyrosine enrichment with SH2 superbinder enables deep profiling of EGF responses. [PDF]
EMBO JChang AT +4 more
europepmc +1 more source
Phosphoproteomics Taken to Heart [PDF]
Cell Cycle, 2013 The last decade has witnessed a tremendous advance in mass spectrometric instrumentation, sample preparation, and computational proteomics developments that now make it possible to analyze proteins1 or post-translational modifications (PTMs) of proteins2 on a global scale and compare their relative abundance between different cell states.
Alicia Lundby, Jesper V Olsen
exaly +4 more sources
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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
openaire +2 more sources
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
openaire +3 more sources
Quest for the Crypto‐phosphoproteome
ChemBioChem, 2020AbstractProtein phosphorylation is one of the most studied post‐translational modifications (PTMs). Despite the remarkable advances in phosphoproteomics, a chemically less‐stable subset of the phosphosites, which we call the crypto‐phosphoproteome, has remained underexplored due to technological challenges.
Seungmin Ahn +2 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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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.
Selvan, Lakshmi Dhevi N. +10 more
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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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