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A Sensitive and Flexible Assay for Determining Histone Deacetylase 1 (HDAC1) Activity.
Wu, Mei-Yi; Wu, Ray-Chang.
Afiliación
  • Wu MY; Department of Biochemistry and Molecular Medicine, The George Washington University, 2300 I Street, NW, Washington, DC, 20037, USA.
  • Wu RC; Department of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX, 77030, USA.
Methods Mol Biol ; 1436: 3-13, 2016.
Article en En | MEDLINE | ID: mdl-27246204
Histones acetylation and deacetylation constitute part of the so-called "histone code" and work in concert with other posttranslational modifications to determine the activity of genes. Deacetylation of histone is carried out by a class of enzymes, known as histone deacetylases (HDACs). The action of HDAC is countered by histone acetyltransferases. Although histone is the best characterized substrate of HDACs, increasing evidence also indicates that non-histone proteins are equally important subtract of HDACs. Since HDACs play an important role in normal physiological and pathophysiological conditions, a sensitive and flexible deacetylation assay that can reliably detect HDAC activity and identify potential novel targets of HDACs is critical.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Immunoblotting / Histona Desacetilasa 1 Tipo de estudio: Diagnostic_studies Límite: Humans Idioma: En Revista: Methods Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Immunoblotting / Histona Desacetilasa 1 Tipo de estudio: Diagnostic_studies Límite: Humans Idioma: En Revista: Methods Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos