Newly acquired N-terminal extension targets threonyl-tRNA synthetase-like protein into the multiple tRNA synthetase complex.

Zhou, Xiao-Long; Chen, Yun; Zeng, Qi-Yu; Ruan, Zhi-Rong; Fang, Pengfei; Wang, En-Duo

Zhou, Xiao-Long; Chen, Yun; Zeng, Qi-Yu; Ruan, Zhi-Rong; Fang, Pengfei; Wang, En-Duo.

Afiliación

Zhou XL; State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China.
Chen Y; State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China.
Zeng QY; State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China.
Ruan ZR; State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China.
Fang P; State Key Laboratory of Bioorganic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 345 Lingling Road, Shanghai 200032, China.
Wang ED; State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China.

Nucleic Acids Res ; 47(16): 8662-8674, 2019 09 19.

Article en En | MEDLINE | ID: mdl-31287872

Asunto(s)

Arginino-ARNt Ligasa/genética; Citocinas/genética; Complejos Multienzimáticos/genética; Proteínas de Neoplasias/genética; Proteínas de Unión al ARN/genética; Treonina-ARNt Ligasa/genética; Secuencia de Aminoácidos; Animales; Arginino-ARNt Ligasa/metabolismo; Clonación Molecular; Citocinas/metabolismo; Escherichia coli/genética; Escherichia coli/metabolismo; Expresión Génica; Células HEK293; Humanos; Leucina Zippers; Ratones; Complejos Multienzimáticos/metabolismo; Músculo Esquelético/metabolismo; Proteínas de Neoplasias/metabolismo; Fosforilación; Plásmidos/química; Plásmidos/metabolismo; Unión Proteica; Proteínas de Unión al ARN/metabolismo; Proteínas Recombinantes/genética; Proteínas Recombinantes/metabolismo; Alineación de Secuencia; Homología de Secuencia de Aminoácido; Treonina-ARNt Ligasa/metabolismo; Técnicas del Sistema de Dos Híbridos

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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Arginino-ARNt Ligasa / Treonina-ARNt Ligasa / Citocinas / Proteínas de Unión al ARN / Complejos Multienzimáticos / Proteínas de Neoplasias Límite: Animals / Humans Idioma: En Revista: Nucleic Acids Res Año: 2019 Tipo del documento: Article País de afiliación: China

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