Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2.

Tao, Ye; Zhong, Chen; Zhu, Junjun; Xu, Shutong; Ding, Jianping

Tao, Ye; Zhong, Chen; Zhu, Junjun; Xu, Shutong; Ding, Jianping.

Tao Y; National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, and University of Chinese Academy of Sciences, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 2
Zhong C; National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, and University of Chinese Academy of Sciences, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 2
Zhu J; National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, and University of Chinese Academy of Sciences, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 2
Xu S; National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, and University of Chinese Academy of Sciences, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 2
Ding J; National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, and University of Chinese Academy of Sciences, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 2

Nucleic Acids Res ; 45(10): 5707-5719, 2017 Jun 02.

Article en En | MEDLINE | ID: mdl-28334966

Asunto(s)

Histona Acetiltransferasas/química; Histonas/genética; Proteínas de Homeodominio/genética; Proteínas Nucleares/genética; Procesamiento Proteico-Postraduccional; Proteínas Supresoras de Tumor/genética; Acetilación; Secuencias de Aminoácidos; Sitios de Unión; Cromatina/química; Cromatina/metabolismo; Clonación Molecular; Cristalografía por Rayos X; Escherichia coli/genética; Escherichia coli/metabolismo; Expresión Génica; Células HEK293; Chaperonas de Histonas; Histonas/metabolismo; Proteínas de Homeodominio/química; Proteínas de Homeodominio/metabolismo; Humanos; Modelos Moleculares; Proteínas Nucleares/química; Proteínas Nucleares/metabolismo; Nucleosomas/genética; Nucleosomas/metabolismo; Unión Proteica; Conformación Proteica en Hélice alfa; Conformación Proteica en Lámina beta; Dominios y Motivos de Interacción de Proteínas; Isoformas de Proteínas/química; Isoformas de Proteínas/genética; Isoformas de Proteínas/metabolismo; Proteínas Recombinantes/química; Proteínas Recombinantes/genética; Proteínas Recombinantes/metabolismo; Especificidad por Sustrato; Transcripción Genética; Proteínas Supresoras de Tumor/química; Proteínas Supresoras de Tumor/metabolismo

Texto completo

Imprimir

XML

PubMed Links

Search on Google

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Proteínas Nucleares / Histonas / Procesamiento Proteico-Postraduccional / Proteínas de Homeodominio / Proteínas Supresoras de Tumor / Histona Acetiltransferasas Idioma: En Año: 2017 Tipo del documento: Article

Texto completo

Imprimir

XML

PubMed Links

Search on Google