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PMID: 22241642 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Angewandte Chemie (International ed. in English) ·Vol. 51 ·No. 7 ·2012-02-13 ·Pages 1631-4

Woon EC, Tumber A, Kawamura A, Hillringhaus L, Ge W, Rose NR, Ma JH, Chan MC, Walport LJ, Che KH, Ng SS, Marsden BD, Oppermann U, McDonough MA, Schofield CJ

Abstract

暂无摘要

MeSH Terms

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

Chemicals

Cross-Linking Reagents Ketoglutaric Acids Jumonji Domain-Containing Histone Demethylases

Authors & Affiliations

15 authors, click to expand affiliations / ORCID

Woon Esther C Y

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

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

Article Info

Journal

Angewandte Chemie (International ed. in English)

Abbr.

Angew Chem Int Ed Engl

ISSN

1521-3773

DOI

10.1002/anie.201107833

Published

2012-02-13

Epub

2012-00-12

Pages

1631-4

Language

English

Region

Germany

NLM ID

0370543

Subset

Grants

Wellcome Trust · 092809 · United Kingdom

Biotechnology and Biological Sciences Research Council · BB/D005949/1 · United Kingdom

External Links

PubMed source DOI: 10.1002/anie.201107833 View journal details

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

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