Assembly of Cell Regulatory Systems Through Protein Interaction Domains
By Tony Pawson, Piers Nash. Science, 2003
1,459 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/b03fc19473560a39bb33628b481cd64b20281795
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Citations in the corpus
- A Correction to the Review Titled "Rules for Modeling Signal-Transduction Systems" by W. S. Hlavacek et al. (2006, background): “A common effect of complex formation is an increase in the activity and specificity of an enzyme through colocalization of the enzyme with a substrate ( 18 , 19 ).”
- Sub‐angstrom modeling of complexes between flexible peptides and globular proteins (2010, background): “The modeling of a peptide–protein interaction can be roughly divided into several consecutive steps, each representing a smaller subproblem, in line with prevalent approaches for modeling16 and docking17 of globular proteins: (1) model the receptor structure (2) predict potential binding sites on th”
- Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis (2006, background): “Phosphorylated IRS proteins relay signals from receptors that bind these growth factors to both PI3K and Ra”
- Rosetta FlexPepDock web server—high resolution modeling of peptide–protein interactions (2011, background): “Peptide-mediated interactions indeed play key roles in major cellular processes, predominantly in signaling and regulatory networks that require short-lived signals (4), and also in cell localization, protein degradation and immune response (3,4).”
- PHOSIDA 2011: the posttranslational modification database (2010, neutral): “For example, almost all signaling pathways are controlled by reversible phosphorylation, ubiquitination and other PTMs (1,2).”
- Rule-based modeling of biochemical systems with BioNetGen. (2009, background): “, and Tatham , P. E. R. (2003) Signal Transduction .”
- A highly efficient rice green tissue protoplast system for transient gene expression and studying light/chloroplast-related processes (2011, background): “Proteins typically interact dynamically and form functional complexes to participate in signaling pathways and regulatory networks [39,40].”
- Motif switches: decision-making in cell regulation. (2012, background): “As a result, the regulatory potency of IDRs has been shown to extend far beyond the acknowledged canonical disordered regions such as the highly modified tails of histones [50] and the termini of tumour suppressor protein p53 [51], or the archetypal domain-binding motifs such as SH3, SH2 and PDZ lig”
- Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics (2004, background): “In growth factor signaling, stimulation of cell-surface receptors first triggers activation of the receptor itself and then of a large number of intracellular effector molecule”
- Does Selection Mold Molecular Networks? (2003, background): “For instance, the number and combination of protein domains that can mediate protein interactions in signal transduction networks are large and growing ( 1 ).”
- Functional dynamics of PDZ binding domains: a normal-mode analysis. (2005, background): “…signaling pathways by organizing networks of receptors and in targeting selected cellular proteins to multiprotein complexes (Hung and Sheng 2002; Pawson and Nash 2003; Sheng and Sala 2001; Zhang and Wang 2003): for example the scaffolding protein InaD (Inactivation no afterpotential D) contains…”
- Structure and regulation of Src family kinases (2004, background): “…revealed by the structural organization of Src – the use of protein interaction domains to regulate catalytic activity in a manner that inextricably couples targeting with catalytic activation – applies quite frequently, if not universally, in modular signaling proteins (Pawson and Nash, 2003).”