Source:http://www.reactome.org/biopax/48887BiochemicalReaction1830
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Authored: Rothfels, K, 2012-02-09,
Edited: Rothfels, K, 2012-05-16,
Point mutations in FGFR2 that are thought to promote ligand-independent dimerization in the context of autosomal bone development disorders have also been identified in endometrial, ovarian, gastric and lung cancer (Greenman, 2007; Dutt, 2008; Davies, 2005; Byron, 2008; Byron, 2010, Pollock, 2007). Although functional studies on these mutations in FGFR2 in cancer cell lines is limited - only the S267P mutation identified in gastric cancer has been demonstrated biochemically to undergo ligand-independent dimerization (Anderson, 1998) - characterization of paralogous mutations in FGFR3 as well as in other mutations that create unpaired cysteine residues in FGFR2 support the notion that these mutant receptors undergo aberrant intermolecular disulphide bond formation that results in constitutive activation (Galvin, 1996; Neilson and Friesel,1995; Robertson, 1998; d'Avis, 1998),
Reviewed: Ezzat, S, 2012-05-15
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http://identifiers.org/pubmed/16140923,
http://identifiers.org/pubmed/17344846,
http://identifiers.org/pubmed/17525745,
http://identifiers.org/pubmed/18552176,
http://identifiers.org/pubmed/18757403,
http://identifiers.org/pubmed/20106510,
http://identifiers.org/pubmed/8755573,
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urn:biopax:UnificationXref:REACTOME DATABASE ID_2029983,
urn:biopax:UnificationXref:REACTOME_REACT_121101_1
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Dimerization of FGFR2 ligand-independent mutants
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