Title : Fusion proteins of the retinoic acid receptor-alpha recruit histone deacetylase in promyelocytic leukaemia.

Pub. Date : 1998 Feb 19

PMID : 9486655






5 Functional Relationships(s)
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1 However, treatment with RA induces differentiation of leukaemic blast cells and disease remission in PML-RARalpha APLs, whereas PLZF-RARa APLs are resistant to RA. Tretinoin PML nuclear body scaffold Homo sapiens
2 However, treatment with RA induces differentiation of leukaemic blast cells and disease remission in PML-RARalpha APLs, whereas PLZF-RARa APLs are resistant to RA. Tretinoin PML nuclear body scaffold Homo sapiens
3 High doses of RA release histone deacetylase activity from PML-RARalpha, but not from PLZF-RARalpha. Tretinoin PML nuclear body scaffold Homo sapiens
4 Therefore, recruitment of histone deacetylase is crucial to the transforming potential of APL fusion proteins, and the different effects of RA on the stability of the PML-RARalpha and PLZF-RARalpha co-repressor complexes determines the differential response of APLs to RA. Tretinoin PML nuclear body scaffold Homo sapiens
5 Therefore, recruitment of histone deacetylase is crucial to the transforming potential of APL fusion proteins, and the different effects of RA on the stability of the PML-RARalpha and PLZF-RARalpha co-repressor complexes determines the differential response of APLs to RA. Tretinoin PML nuclear body scaffold Homo sapiens