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Conformational dynamics of the TTD-PHD histone reader module of the UHRF1 epigenetic regulator reveals multiple histone-binding states, allosteric regulation, and druggability.
Houliston, R Scott; Lemak, Alexander; Iqbal, Aman; Ivanochko, Danton; Duan, Shili; Kaustov, Lilia; Ong, Michelle S; Fan, Lixin; Senisterra, Guillermo; Brown, Peter J; Wang, Yun-Xing; Arrowsmith, Cheryl H.
Afiliação
  • Houliston RS; From the Princess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
  • Lemak A; From the Princess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
  • Iqbal A; the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
  • Ivanochko D; From the Princess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
  • Duan S; From the Princess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
  • Kaustov L; From the Princess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
  • Ong MS; From the Princess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
  • Fan L; the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
  • Senisterra G; the Small-Angle X-ray Scattering Core Facility, Frederick National Laboratory for Cancer Research, Leidos Biomedical Research Inc., Frederick, Maryland 21702, and.
  • Brown PJ; the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
  • Wang YX; the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
  • Arrowsmith CH; the NCI, National Institutes of Health, Frederick, Maryland 21702.
J Biol Chem ; 292(51): 20947-20959, 2017 12 22.
Article em En | MEDLINE | ID: mdl-29074623
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Estimuladoras de Ligação a CCAAT Limite: Humans Idioma: En Ano de publicação: 2017 Tipo de documento: Article
Texto completo
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Estimuladoras de Ligação a CCAAT Limite: Humans Idioma: En Ano de publicação: 2017 Tipo de documento: Article