Your browser doesn't support javascript.
loading
Msp1/ATAD1 maintains mitochondrial function by facilitating the degradation of mislocalized tail-anchored proteins.
Chen, Yu-Chan; Umanah, George K E; Dephoure, Noah; Andrabi, Shaida A; Gygi, Steven P; Dawson, Ted M; Dawson, Valina L; Rutter, Jared.
Afiliación
  • Chen YC; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City UT, USA.
  • Umanah GK; Neuroregeneration and Stem Cell Programs, Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, MD, USA Department of Neurology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
  • Dephoure N; Department of Cell Biology, Harvard Medical School, Boston, MA, USA.
  • Andrabi SA; Neuroregeneration and Stem Cell Programs, Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, MD, USA Department of Neurology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
  • Gygi SP; Department of Cell Biology, Harvard Medical School, Boston, MA, USA.
  • Dawson TM; Neuroregeneration and Stem Cell Programs, Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, MD, USA Department of Neurology, Johns Hopkins University School of Medicine, Baltimore, MD, USA Solomon H. Snyder Department of Neuroscience, Johns Hopkins University Sc
  • Dawson VL; Neuroregeneration and Stem Cell Programs, Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, MD, USA Department of Neurology, Johns Hopkins University School of Medicine, Baltimore, MD, USA Solomon H. Snyder Department of Neuroscience, Johns Hopkins University Sc
  • Rutter J; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City UT, USA rutter@biochem.utah.edu.
EMBO J ; 33(14): 1548-64, 2014 Jul 17.
Article en En | MEDLINE | ID: mdl-24843043
Asunto(s)
Palabras clave
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Adenosina Trifosfatasas / Proteínas de Saccharomyces cerevisiae / Proteínas Ligadas a Lípidos / Proteolisis / Mitocondrias Límite: Animals / Humans Idioma: En Revista: EMBO J Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Adenosina Trifosfatasas / Proteínas de Saccharomyces cerevisiae / Proteínas Ligadas a Lípidos / Proteolisis / Mitocondrias Límite: Animals / Humans Idioma: En Revista: EMBO J Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos