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Towards the Phosphoproteome of Trypanosomatids
2013The identification and localization of protein phosphorylation sites provide clues to what proteins or pathways might be activated in a given condition, helping to improve our understanding about signaling networks. Advances in strategies for enrichment of phosphorylated peptides/proteins, mass spectrometry (MS) instrumentation, and specific MS ...
Fabricio K, Marchini +4 more
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Enrichment Strategies in Phosphoproteomics
2016The comprehensive study of the phosphoproteome is heavily dependent on appropriate enrichment strategies that are most often, but not exclusively, carried out on the peptide level. In this chapter, I give an overview of the most widely used techniques. In addition to dedicated antibodies, phosphopeptides are enriched by their selective interaction with
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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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Analysis of Phosphoproteomics Data
2010Regulation of protein phosphorylation plays an important role in many cellular processes, particularly in signal transduction. Diseases such as cancer and inflammation are often linked to aberrant signaling pathways. Mass spectrometry-based methods allow monitoring the phosphorylation status in an unbiased and quantitative manner.
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Deciphering the human phosphoproteome
Nature Biotechnology, 2020Giulia Franciosa +2 more
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