Your browser doesn't support javascript.
loading
A structurally conserved site in AUP1 binds the E2 enzyme UBE2G2 and is essential for ER-associated degradation.
Smith, Christopher E; Tsai, Yien Che; Liang, Yu-He; Khago, Domarin; Mariano, Jennifer; Li, Jess; Tarasov, Sergey G; Gergel, Emma; Tsai, Borong; Villaneuva, Matthew; Clapp, Michelle E; Magidson, Valentin; Chari, Raj; Byrd, R Andrew; Ji, Xinhua; Weissman, Allan M.
Afiliação
  • Smith CE; Laboratory of Protein Dynamics and Signaling, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America.
  • Tsai YC; Laboratory of Protein Dynamics and Signaling, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America.
  • Liang YH; Center for Structural Biology, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America.
  • Khago D; Center for Structural Biology, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America.
  • Mariano J; Laboratory of Protein Dynamics and Signaling, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America.
  • Li J; Center for Structural Biology, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America.
  • Tarasov SG; Center for Structural Biology, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America.
  • Gergel E; Laboratory of Protein Dynamics and Signaling, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America.
  • Tsai B; Laboratory of Protein Dynamics and Signaling, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America.
  • Villaneuva M; Laboratory of Protein Dynamics and Signaling, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America.
  • Clapp ME; Genome Modification Core, Frederick National Laboratory for Cancer Research, Frederick, Maryland, United States of America.
  • Magidson V; Optical Microscopy and Analysis Laboratory, Frederick National Laboratory for Cancer Research, Frederick, Maryland, United States of America.
  • Chari R; Genome Modification Core, Frederick National Laboratory for Cancer Research, Frederick, Maryland, United States of America.
  • Byrd RA; Center for Structural Biology, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America.
  • Ji X; Center for Structural Biology, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America.
  • Weissman AM; Laboratory of Protein Dynamics and Signaling, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America.
PLoS Biol ; 19(12): e3001474, 2021 12.
Article em En | MEDLINE | ID: mdl-34879065

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Enzimas de Conjugação de Ubiquitina / Degradação Associada com o Retículo Endoplasmático / Proteínas de Membrana Tipo de estudo: Risk_factors_studies Limite: Humans Idioma: En Revista: PLoS Biol Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Enzimas de Conjugação de Ubiquitina / Degradação Associada com o Retículo Endoplasmático / Proteínas de Membrana Tipo de estudo: Risk_factors_studies Limite: Humans Idioma: En Revista: PLoS Biol Ano de publicação: 2021 Tipo de documento: Article