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Literature summary for 3.5.1.98 extracted from

  • Rossig, L.; Urbich, C.; Bruhl, T.; Dernbach, E.; Heeschen, C.; Chavakis, E.; Sasaki, K.; Aicher, D.; Diehl, F.; Seeger, F.; Potente, M.; Aicher, A.; Zanetta, L.; Dejana, E.; Zeiher, A.M.; Dimmeler, S.
    Histone deacetylase activity is essential for the expression of HoxA9 and for endothelial commitment of progenitor cells (2005), J. Exp. Med., 201, 1825-1835.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
Butyrate inhibition of histone deacetylases, results in down-regulation of HoxA9 expression Mus musculus
MS-275 inhibition of histone deacetylases, results in down-regulation of HoxA9 expression Mus musculus
trichostatin A inhibition of histone deacetylases, results in down-regulation of HoxA9 expression Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus histone deacetylases regulate the expression of HoxA9, which acts as a master switch to regulate the expression of prototypical endothelial-committed genes such as endothelial nitric oxide synthase, VE-cadherin, VEGF-R2, and mediates the shear stress-induced maturation of endothelial cells ?
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?

Organism

Organism UniProt Comment Textmining
Mus musculus
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Source Tissue

Source Tissue Comment Organism Textmining
mononuclear cell
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Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information histone deacetylases regulate the expression of HoxA9, which acts as a master switch to regulate the expression of prototypical endothelial-committed genes such as endothelial nitric oxide synthase, VE-cadherin, VEGF-R2, and mediates the shear stress-induced maturation of endothelial cells Mus musculus ?
-
?