Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases.

Woon, Esther C Y; Tumber, Anthony; Kawamura, Akane; Hillringhaus, Lars; Ge, Wei; Rose, Nathan R; Ma, Jerome H Y; Chan, Mun Chiang; Walport, Louise J; Che, Ka Hing; Ng, Stanley S; Marsden, Brian D; Oppermann, Udo; McDonough, Michael A; Schofield, Christopher J

Woon, Esther C Y; Tumber, Anthony; Kawamura, Akane; Hillringhaus, Lars; Ge, Wei; Rose, Nathan R; Ma, Jerome H Y; Chan, Mun Chiang; Walport, Louise J; Che, Ka Hing; Ng, Stanley S; Marsden, Brian D; Oppermann, Udo; McDonough, Michael A; Schofield, Christopher J.

Affiliation

Woon EC; Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, UK.

Angew Chem Int Ed Engl ; 51(7): 1631-4, 2012 Feb 13.

Article in En | MEDLINE | ID: mdl-22241642

Subject(s)

Cross-Linking Reagents/pharmacology; Jumonji Domain-Containing Histone Demethylases/antagonists & inhibitors; Ketoglutaric Acids/pharmacology; Binding Sites/drug effects; Cross-Linking Reagents/chemical synthesis; Cross-Linking Reagents/chemistry; Humans; Jumonji Domain-Containing Histone Demethylases/chemistry; Ketoglutaric Acids/chemistry; Models, Molecular; Molecular Structure; Structure-Activity Relationship; Substrate Specificity

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Cross-Linking Reagents / Jumonji Domain-Containing Histone Demethylases / Ketoglutaric Acids Limits: Humans Language: En Journal: Angew Chem Int Ed Engl Year: 2012 Type: Article Affiliation country: United kingdom

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