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S-adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3.
Jayaram, Hariharan; Hoelper, Dominik; Jain, Siddhant U; Cantone, Nico; Lundgren, Stefan M; Poy, Florence; Allis, C David; Cummings, Richard; Bellon, Steven; Lewis, Peter W.
Afiliação
  • Jayaram H; Constellation Pharmaceuticals, Cambridge, MA 02142;
  • Hoelper D; Wisconsin Institute of Discovery, University of Wisconsin, Madison, WI 53715; Biomolecular Chemistry, School of Medicine and Public Health, University of Wisconsin, Madison, WI 53715;
  • Jain SU; Wisconsin Institute of Discovery, University of Wisconsin, Madison, WI 53715; Biomolecular Chemistry, School of Medicine and Public Health, University of Wisconsin, Madison, WI 53715;
  • Cantone N; Constellation Pharmaceuticals, Cambridge, MA 02142;
  • Lundgren SM; Wisconsin Institute of Discovery, University of Wisconsin, Madison, WI 53715; Biomolecular Chemistry, School of Medicine and Public Health, University of Wisconsin, Madison, WI 53715;
  • Poy F; Constellation Pharmaceuticals, Cambridge, MA 02142;
  • Allis CD; Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University, New York, NY 10065 alliscd@rockefeller.edu Richard.Cummings@constellationpharma.com Steve.Bellon@constellationpharma.com plewis@discovery.wisc.edu.
  • Cummings R; Constellation Pharmaceuticals, Cambridge, MA 02142; alliscd@rockefeller.edu Richard.Cummings@constellationpharma.com Steve.Bellon@constellationpharma.com plewis@discovery.wisc.edu.
  • Bellon S; Constellation Pharmaceuticals, Cambridge, MA 02142; alliscd@rockefeller.edu Richard.Cummings@constellationpharma.com Steve.Bellon@constellationpharma.com plewis@discovery.wisc.edu.
  • Lewis PW; Wisconsin Institute of Discovery, University of Wisconsin, Madison, WI 53715; Biomolecular Chemistry, School of Medicine and Public Health, University of Wisconsin, Madison, WI 53715; alliscd@rockefeller.edu Richard.Cummings@constellationpharma.com Steve.Bellon@constellationpharma.com plewis@discove
Proc Natl Acad Sci U S A ; 113(22): 6182-7, 2016 May 31.
Article em En | MEDLINE | ID: mdl-27185940
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: S-Adenosilmetionina / Histonas / Histona-Lisina N-Metiltransferase / Lisina / Metionina / Mutação Limite: Humans Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2016 Tipo de documento: Article
Texto completo
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XML
PubMed Links
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: S-Adenosilmetionina / Histonas / Histona-Lisina N-Metiltransferase / Lisina / Metionina / Mutação Limite: Humans Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2016 Tipo de documento: Article