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Linking of 2-Oxoglutarate and Substrate Binding Sites Enables Potent and Highly Selective Inhibition of JmjC Histone Demethylases.
Published in:
Angewandte Chemie, 2012, v. 124, n. 7, p. 1663, doi. 10.1002/ange.201107833
By:
- 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.
Publication type:
Article
Quantitative High-Throughput Screening Identifies 8-Hydroxyquinolines as Cell-Active Histone Demethylase Inhibitors.
Published in:
PLoS ONE, 2010, v. 5, n. 11, p. 1, doi. 10.1371/journal.pone.0015535
By:
- King, Oliver N. F.;
- Li, Xuan Shirley;
- Sakurai, Masaaki;
- Kawamura, Akane;
- Rose, Nathan R.;
- Ng, Stanley S.;
- Quinn, Amy M.;
- Rai, Ganesha;
- Mott, Bryan T.;
- Beswick, Paul;
- Klose, Robert J.;
- Oppermann, Udo;
- Jadhav, Ajit;
- Heightman, Tom D.;
- Maloney, David J.;
- Schofield, Christopher J.;
- Simeonov, Anton
Publication type:
Article
Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity.
Published in:
Nature, 2007, v. 448, n. 7149, p. 87, doi. 10.1038/nature05971
By:
- Ng, Stanley S.;
- Kavanagh, Kathryn L.;
- McDonough, Michael A.;
- Butler, Danica;
- Pilka, Ewa S.;
- Lienard, Benoit M. R.;
- Bray, James E.;
- Savitsky, Pavel;
- Gileadi, Opher;
- von Delft, Frank;
- Rose, Nathan R.;
- Offer, John;
- Scheinost, Johanna C.;
- Borowski, Tomasz;
- Sundstrom, Michael;
- Schofield, Christopher J.;
- Oppermann, Udo
Publication type:
Article
Ribosomal oxygenases are structurally conserved from prokaryotes to humans.
Published in:
Nature, 2014, v. 510, n. 7505, p. 422, doi. 10.1038/nature13263
By:
- Chowdhury, Rasheduzzaman;
- Sekirnik, Rok;
- Brissett, Nigel C.;
- Krojer, Tobias;
- Ho, Chia-hua;
- Ng, Stanley S.;
- Clifton, Ian J.;
- Ge, Wei;
- Kershaw, Nadia J.;
- Fox, Gavin C.;
- Muniz, Joao R. C.;
- Vollmar, Melanie;
- Phillips, Claire;
- Pilka, Ewa S.;
- Kavanagh, Kathryn L.;
- von Delft, Frank;
- Oppermann, Udo;
- McDonough, Michael A.;
- Doherty, Aidan J.;
- Schofield, Christopher J.
Publication type:
Article
Linking of 2-Oxoglutarate and Substrate Binding Sites Enables Potent and Highly Selective Inhibition of JmjC Histone Demethylases.
Published in:
Angewandte Chemie International Edition, 2012, v. 51, n. 7, p. 1631, doi. 10.1002/anie.201107833
By:
- 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.
Publication type:
Article

Found: 5

Linking of 2-Oxoglutarate and Substrate Binding Sites Enables Potent and Highly Selective Inhibition of JmjC Histone Demethylases.

Quantitative High-Throughput Screening Identifies 8-Hydroxyquinolines as Cell-Active Histone Demethylase Inhibitors.

Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity.

Ribosomal oxygenases are structurally conserved from prokaryotes to humans.

Linking of 2-Oxoglutarate and Substrate Binding Sites Enables Potent and Highly Selective Inhibition of JmjC Histone Demethylases.