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HDAC3 — STAT3
Pathways - manually collected, often from reviews:
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Bind Interaction:
STAT3
—
HDAC3
Yuan et al., Science 2005*
-
IRef Bind_translation Interaction:
STAT3
—
HDAC3
(coimmunoprecipitation)
Yuan et al., Science 2005*
-
IRef Bind_translation Interaction:
STAT3
—
HDAC3
(experimental interaction detection)
Yuan et al., Science 2005*
-
IRef Biogrid Interaction:
HDAC3
—
STAT3
(physical association, affinity chromatography technology)
Tsuruma et al., Oncogene 2008*
-
IRef Biogrid Interaction:
HDAC3
—
STAT3
(physical association, affinity chromatography technology)
Yuan et al., Science 2005*
-
IRef Biogrid Interaction:
HDAC3
—
STAT3
(physical association, affinity chromatography technology)
Gupta et al., Leukemia 2012*
-
IRef Hprd Interaction:
Complex of 11 proteins
(in vivo)
Nagl et al., EMBO J 2007
-
IRef Hprd Interaction:
Complex of 100 proteins
(in vivo)
Nagl et al., EMBO J 2007
-
IRef Hprd Interaction:
STAT3
—
HDAC3
(in vivo)
Yuan et al., Science 2005*
Text-mined interactions from Literome
Dong et al., Oncogene 2003
:
Studies comparing NuMA-RARalpha with NuMA-RARalpha ( deltaCC ) demonstrated that the dimerization or alpha-helical coiled-coil domain of NuMA was required for homodimer formation, transcriptional repression of wild-type RARalpha, transcriptional
activation of
STAT3 , and stability of the
NuMA-RARalpha/SMRT complex
Gupta et al., Leukemia 2012
(Lymphoma, Large B-Cell, Diffuse) :
Regulation of
STAT3 by
histone deacetylase-3 in diffuse large B-cell lymphoma : implications for therapy