Protein tyrosine kinase structure and function.
By S. Hubbard, J. Till. Annual Review of Biochemistry, 2000
1,177 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/7b9c73a5c95f80d40457333407f1184345fe8a7e
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Citations in the corpus
- Ligand-induced endocytosis of the pattern recognition receptor FLS2 in Arabidopsis. (2006, background): “Autophosphorylation has been shown to play a crucial role in animal RTK activation (Hubbard and Till 2000) and also occurs in several plant RLKs including FLS2 (Nasrallah 2000; Gomez-Gomez et al.”
- The protein tyrosine kinase family of the human genome (2000, background): “Summary Hubbard and Till, 2000; Hunter, 2000; Robertson et al., 2000; Cole et al., 1999; Fischer, 1999; Schenk and Snaar-Jagalska, 1999; Hubbard et al., 1998; Porter and Vaillancourt, 1998; Hunter, 1997; Johnson et al., 1996; Hanks and Hunter, 1995 Non-receptor families Neet and Hunter, 1996 ABL…”
- Structure and regulation of Src family kinases (2004, background): “Bound nucleotide phosphates are in part coordinated by the glycine-rich G loop (also termed the P-loop, for phosphate binding) (Taylor et al., 1992; Hubbard and Till, 2000).”
- Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease. (2009, background): “Such conserved sites are abundant in the tyrosine kinase domain (32), indicating that this domain is under strong selection pressure to maintain the general IR signal transduction functions.”
- Vascular endothelial growth factor (VEGF) signaling in tumor progression. (2007, background): “Activation of the eceptor protein-tyrosine kinases and the initiation of sigal transduction involve autophosphorylation of tyrosine esidues [40].”
- Mechanisms of specificity in protein phosphorylation (2007, background): “Non-receptor Tyr kinases, for example, almost always have well-defined interaction domains, such as Src -homology-2 (SH2), SH3, integrin binding, focal adhesion binding, DNA binding, F-actin binding, pleckstrin homology, or Janus tyrosine kinase (JAK) homology domain”
- An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. (2003, background): “This domain rearrangement gives rise to the extended configuration, and breaks the tion causes them to become autophosphorylated within the activation loop (Hubbard and Till, 2000).”
- RTK and TGF-β signaling pathways genes in the sea urchin genome (2006, background): “a tyrosine kinase activity (RTK) and bind a variety of growth factors while the second comprises the receptors that phosphorylate serine or threonine residues and bind members of the TGFβ family (Hubbard and Till, 2000; Shi and Massague, 2003).”
- The FGFR Landscape in Cancer: Analysis of 4,853 Tumors by Next-Generation Sequencing (2015, background): “All four FGFRs share structural homology with vascular endothelial growth factor receptors (VEGFR), platelet-derived growth factor receptors (PDGFR), and other tyrosine kinase receptors, which has implications for pharmacologic therapy (2).”
- Oncogenic kinase signalling (2001, background): “Crystal structures of the inactive forms of the core cytoplasmic kinase domains of the insulin receptor (InsR), fibroblast growth factor receptor-1 (FGFR1) and Flk1 (vascular endothelial growth factor receptor-2 or VEGFR2) tyrosine kinases have provided a molecular understanding of the tight control”
- Lectin Receptor Kinases in Plants (2002, background): “This C-terminal domain is considered as a regulatory region susceptible to interact with signaling proteins (see Schlessinger, 2000, and Hubbard and Till, 2000 for review).”
- Plant Receptor-Like Kinase Gene Family: Diversity, Function, and Signaling (2001, background): “These differences in phosphorylation might reflect the differences in the mechanism of receptor activation observed in animal RTKs (13).”