Inhibition of Histone Demethylases by 4‐Carboxy‐2,2′‐Bipyridyl Compounds | Zendy

Chang KaiHsuan | Zendy; King Oliver N. F. | Zendy; Tumber Anthony | Zendy; Woon Esther C. Y. | Zendy; Heightman Tom D. | Zendy; McDonough Michael A. | Zendy; Schofield Christopher J. | Zendy; Rose Nathan R. | Zendy

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Inhibition of Histone Demethylases by 4‐Carboxy‐2,2′‐Bipyridyl Compounds

Author(s) -

Chang KaiHsuan,

King Oliver N. F.,

Tumber Anthony,

Woon Esther C. Y.,

Heightman Tom D.,

McDonough Michael A.,

Schofield Christopher J.,

Rose Nathan R.

Publication year - 2011

Publication title -

chemmedchem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.817

H-Index - 100

eISSN - 1860-7187

pISSN - 1860-7179

DOI - 10.1002/cmdc.201100026

Subject(s) - histone , epigenetics , ic50 , lysine , chemistry , lead compound , stereochemistry , structure–activity relationship , biochemistry , in vitro , biology , gene , amino acid

Exploiting epigenetics: 2‐Oxoglutarate (2OG)‐dependent histone lysine demethylases, such as JMJD2E, are potential therapeutic targets in a range of diseases. Through structure–activity relationship studies and analyses, we identified a potent 4‐carboxy‐2,2′‐bipyridyl compound, which inhibits JMJD2E with an IC 50 value of 110 n M , representing a 66‐fold improvement over the lead compound. These bipyridyl derivatives bind in the 2‐oxoglutarate binding site.

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