Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

By Jesper V. Olsen, Florian Gnad, Boris Macek, Chanchal Kumar, P. Mortensen, Matthias Mann. Cell, 2006

3,603 citations recorded by the source corpus.

Subfields: Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/d0d1ab1b61bc1ca7da88069fad276304f8a9f5c6

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Citations in the corpus

PhosPhAt: a database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor (2007, background): “This usually implies manual interpretation of mass spectra and additional scoring algorithms ( 16 ).”
A phospho-dependent mechanism involving NCoR and KMT2D controls a permissive chromatin state at Notch target genes (2016, background): “Importantly, two independent global phosphorylation studies demonstrated that these two serine residues in NCoR are phosphorylated in cells (43,44).”
The crucial role of protein phosphorylation in cell signaling and its use as targeted therapy (Review) (2017, positive): “This endorses the view that the detailed study of phosphorylation networks may help to understand the physiological and pathological mechanisms (72-76).”
Rule-based modeling of biochemical systems with BioNetGen. (2009, methodology): “Blinov , M. L. , Faeder , J. R. , Goldstein , B. , and Hlavacek , W. S. (2004) BioNetGen: software for rule-based modeling of signal transduction based on the interactions of molecular domains .”
Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins. (2011, background): “…al., 1999; Yanagawa et al., 1997), and phosphorylation at threonine 269 (T269) and serine 272 (S272) was previously identified by large-scale phospho-peptide screening and individual mass-spectrometry analyses (Linares et al., 2011; Nousiainen et al., 2006; Olsen et al., 2006; Pankiv et al., 2010).”
Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases (2016, methodology): “High-resolution quantitative mass spectrometry (MS) has become the method of choice for confident identification of in vitro and in vivo phosphorylation events (Roux and Thibault, 2013; Lemeer and Heck, 2009; Olsen et al., 2006).”
PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse (2011, background): “A fourth, PHOSIDA (10), was launched in the fall of 2006.”
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. (2008, methodology): “Resulting peptide fractions were subjected to phosphopeptide enrichment on TiO2 beads prior to analysis by nanoscale liquid chromatography-tandem MS (LC-MS/MS) on a high-resolution linear ion trap/orbitrap (LTQ-Orbitrap) hybrid mass spectrometer (Larsen et al., 2005; Olsen et al., 2006) (Figure 2A).”
Serine/threonine phosphatases: mechanism through structure. (2009, background): “Proteomic analysis of 6600 phosphorylation sites on 2244 human proteins revealed that phosphoserine (pSer), phosphothreonine (pThr), and phosphotyrosine (pTyr) account for 86.4%, 11.8%, and 1.8%, respectively, of the phosphorylated amino acids (Olsen et al., 2006).”
Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling. (2014, methodology): “This has only recently become possible, on the basis of stable-isotope labeling techniques (Olsen et al., 2010; Wu et al., 2011).”