Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems.

By Tony Pawson. Cell, 2004

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A Correction to the Review Titled "Rules for Modeling Signal-Transduction Systems" by W. S. Hlavacek et al. (2006, background): “The behavior of a signal-transduction system depends on dynamic interactions among its proteins (4, 5).”
Maximum Entropy Reconstructions of Dynamic Signaling Networks from Quantitative Proteomics Data (2009, background): “integrate, and utilize external signals to achieve an appropriate phenotypic response are a subject currently of intense study[1].”
Phosphotyrosine interactome of the ErbB-receptor kinase family (2005, methodology): “One cell population was supplemented with normal isotopic abundance L-12 arginine (Sigma) and L-lysine, and the other with 99% isotopic abundance 13C6-arginine (Aldrich) and 13C6-lysine, as described (Ong et al, 2003).”
Structure and regulation of Src family kinases (2004, background): “…function and specificity of the SH2 and SH3 domains of Src and of their effect on the activity of the adjacent kinase domain have provided a powerful paradigm for the functional dissection of a host of modular signaling domains (see Pawson (2004) for an excellent review and historical perspective).”
Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways (2017, background): “Regardless, the newly phosphorylated tyrosine residues serve as docking sites for proteins harboring phosphor-tyrosine-binding residues, such as those with Src Homology 2 (SH2) and phosphotyrosine binding (PTB) domains [125].”