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Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly.
Cuéllar, Jorge; Ludlam, W Grant; Tensmeyer, Nicole C; Aoba, Takuma; Dhavale, Madhura; Santiago, César; Bueno-Carrasco, M Teresa; Mann, Michael J; Plimpton, Rebecca L; Makaju, Aman; Franklin, Sarah; Willardson, Barry M; Valpuesta, José M.
  • Cuéllar J; Centro Nacional de Biotecnología, Campus de la Universidad Autónoma de Madrid, 28049, Madrid, Spain.
  • Ludlam WG; Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT, 84602, USA.
  • Tensmeyer NC; Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT, 84602, USA.
  • Aoba T; Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT, 84602, USA.
  • Dhavale M; Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT, 84602, USA.
  • Santiago C; Centro Nacional de Biotecnología, Campus de la Universidad Autónoma de Madrid, 28049, Madrid, Spain.
  • Bueno-Carrasco MT; Centro Nacional de Biotecnología, Campus de la Universidad Autónoma de Madrid, 28049, Madrid, Spain.
  • Mann MJ; Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT, 84602, USA.
  • Plimpton RL; Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT, 84602, USA.
  • Makaju A; Department of Internal Medicine, Nora Eccles Harrison Cardiovascular Research and Training Institute, University of Utah, Salt Lake City, UT, 84112, USA.
  • Franklin S; Department of Internal Medicine, Nora Eccles Harrison Cardiovascular Research and Training Institute, University of Utah, Salt Lake City, UT, 84112, USA.
  • Willardson BM; Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT, 84602, USA. bmwillardson@chem.byu.edu.
  • Valpuesta JM; Centro Nacional de Biotecnología, Campus de la Universidad Autónoma de Madrid, 28049, Madrid, Spain. jmv@cnb.csic.es.
Nat Commun ; 10(1): 2865, 2019 06 28.
Article en En | MEDLINE | ID: mdl-31253771
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Chaperonina con TCP-1 / Serina-Treonina Quinasas TOR / Homóloga LST8 de la Proteína Asociada al mTOR / Proteína Reguladora Asociada a mTOR Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Año: 2019 Tipo del documento: Article
Texto completo
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Chaperonina con TCP-1 / Serina-Treonina Quinasas TOR / Homóloga LST8 de la Proteína Asociada al mTOR / Proteína Reguladora Asociada a mTOR Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Año: 2019 Tipo del documento: Article