Your browser doesn't support javascript.
loading
Structural and Functional Insights into Host Death Domains Inactivation by the Bacterial Arginine GlcNAcyltransferase Effector.
Ding, Jingjin; Pan, Xing; Du, Lijie; Yao, Qing; Xue, Juan; Yao, Hongwei; Wang, Da-Cheng; Li, Shan; Shao, Feng.
Afiliação
  • Ding J; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; National Institute of Biological Sciences, Beijing 102206, China. Electronic address: jding@ibp.ac.cn.
  • Pan X; Bio-Medical Center, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, China; Institute of Infection and Immunity, Taihe Hospital, Hubei University of Medicine, Shiyan, Hubei 442000, China.
  • Du L; Institute of Infection and Immunity, Taihe Hospital, Hubei University of Medicine, Shiyan, Hubei 442000, China.
  • Yao Q; National Institute of Biological Sciences, Beijing 102206, China.
  • Xue J; Institute of Infection and Immunity, Taihe Hospital, Hubei University of Medicine, Shiyan, Hubei 442000, China.
  • Yao H; College of Chemistry and Chemical Engineering, High-Field Nuclear Magnetic Resonance Center, Xiamen University, Xiamen, Fujian 361005, China.
  • Wang DC; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
  • Li S; Bio-Medical Center, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, China; Institute of Infection and Immunity, Taihe Hospital, Hubei University of Medicine, Shiyan, Hubei 442000, China. Electronic address: lishan@mail.hzau.edu.cn.
  • Shao F; National Institute of Biological Sciences, Beijing 102206, China; Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, Beijing 102206, China. Electronic address: shaofeng@nibs.ac.cn.
Mol Cell ; 74(5): 922-935.e6, 2019 06 06.
Article em En | MEDLINE | ID: mdl-30979585

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Conformação Proteica / Proteínas de Escherichia coli / Fatores de Virulência / Escherichia coli Enteropatogênica / Interações Hospedeiro-Patógeno Limite: Animals / Humans Idioma: En Revista: Mol Cell Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2019 Tipo de documento: Article País de publicação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Conformação Proteica / Proteínas de Escherichia coli / Fatores de Virulência / Escherichia coli Enteropatogênica / Interações Hospedeiro-Patógeno Limite: Animals / Humans Idioma: En Revista: Mol Cell Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2019 Tipo de documento: Article País de publicação: Estados Unidos