Title : Ultraviolet light induces redox reaction-mediated dimerization and superactivation of oncogenic Ret tyrosine kinases.

Pub. Date : 2000 Jan

PMID : 10637293






5 Functional Relationships(s)
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1 Before UV irradiation, small percentages of c-Ret (3-4%) and Ret-MEN2B (1-2%) and large percentages of Ret-MEN2A (30-40%) were dimerized through disulfide bonds. Disulfides ret proto-oncogene Homo sapiens
2 These dimerized Ret proteins were preferentially autophosphorylated, suggesting a close relation between up-regulated kinase activity and disulfide bond-mediated dimerization of Ret proteins. Disulfides ret proto-oncogene Homo sapiens
3 These dimerized Ret proteins were preferentially autophosphorylated, suggesting a close relation between up-regulated kinase activity and disulfide bond-mediated dimerization of Ret proteins. Disulfides ret proto-oncogene Homo sapiens
4 We found that UV irradiation promotes the disulfide bond-mediated dimerization of the Ret proteins, in close association with activation and superactivation of Ret kinases. Disulfides ret proto-oncogene Homo sapiens
5 We found that UV irradiation promotes the disulfide bond-mediated dimerization of the Ret proteins, in close association with activation and superactivation of Ret kinases. Disulfides ret proto-oncogene Homo sapiens