p38αMAPK interacts with and inhibits RARα: suppression of the kinase enhances the therapeutic activity of retinoids in acute myeloid leukemia cells. (Q39392644)

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English	p38αMAPK interacts with and inhibits RARα: suppression of the kinase enhances the therapeutic activity of retinoids in acute myeloid leukemia cells.	scientific article

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23 January 2020

p38αMAPK interacts with and inhibits RARα: suppression of the kinase enhances the therapeutic activity of retinoids in acute myeloid leukemia cells (English)

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23 January 2020

acute myeloid leukemia

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23 January 2020

Gabriela Paroni

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23 January 2020

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M Gianni

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N Bruck

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A Rambaldi

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G Borleri

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M Terao

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M Kurosaki

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C Rochette-Egly

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E Garattini

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22 February 2012

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23 January 2020

1850-1861

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23 January 2020

https://scigraph.springernature.com/pub.10.1038/leu.2012.50

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Cytodifferentiation by retinoids, a novel therapeutic option in oncology: rational combinations with other therapeutic agents

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Phosphorylation by p38MAPK and recruitment of SUG-1 are required for RA-induced RAR gamma degradation and transactivation

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P38MAPK-dependent phosphorylation and degradation of SRC-3/AIB1 and RARalpha-mediated transcription

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A coordinated phosphorylation cascade initiated by p38MAPK/MSK1 directs RARalpha to target promoters

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Protein kinases and the proteasome join in the combinatorial control of transcription by nuclear retinoic acid receptors

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Cyclin H binding to the RARalpha activation function (AF)-2 domain directs phosphorylation of the AF-1 domain by cyclin-dependent kinase 7.

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Inhibition of the peptidyl-prolyl-isomerase Pin1 enhances the responses of acute myeloid leukemia cells to retinoic acid via stabilization of RARalpha and PML-RARalpha

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Tyrosine kinase inhibitor STI571 potentiates the pharmacologic activity of retinoic acid in acute promyelocytic leukemia cells: effects on the degradation of RARalpha and PML-RARalpha

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