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Phosphorylation at distinct subcellular locations underlies specificity in mTORC2-mediated activation of SGK1 and Akt.
Gleason, Catherine E; Oses-Prieto, Juan A; Li, Kathy H; Saha, Bidisha; Situ, Gavin; Burlingame, Alma L; Pearce, David.
Affiliation
  • Gleason CE; Department of Medicine, Division of Nephrology, UCSF, San Francisco, CA 94143, USA catie@circlepharma.com.
  • Oses-Prieto JA; Departments of Chemistry and Pharmaceutical Chemistry, UCSF, San Francisco, CA 94143, USA.
  • Li KH; Departments of Chemistry and Pharmaceutical Chemistry, UCSF, San Francisco, CA 94143, USA.
  • Saha B; Department of Medicine, Division of Nephrology, UCSF, San Francisco, CA 94143, USA.
  • Situ G; Department of Medicine, Division of Nephrology, UCSF, San Francisco, CA 94143, USA.
  • Burlingame AL; Departments of Chemistry and Pharmaceutical Chemistry, UCSF, San Francisco, CA 94143, USA.
  • Pearce D; Department of Medicine, Division of Nephrology, UCSF, San Francisco, CA 94143, USA.
J Cell Sci ; 132(7)2019 04 09.
Article in En | MEDLINE | ID: mdl-30837283

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Phosphorylation / Protein Serine-Threonine Kinases / Immediate-Early Proteins / Proto-Oncogene Proteins c-akt / Mechanistic Target of Rapamycin Complex 2 Limits: Humans Language: En Journal: J Cell Sci Year: 2019 Type: Article Affiliation country: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Phosphorylation / Protein Serine-Threonine Kinases / Immediate-Early Proteins / Proto-Oncogene Proteins c-akt / Mechanistic Target of Rapamycin Complex 2 Limits: Humans Language: En Journal: J Cell Sci Year: 2019 Type: Article Affiliation country: United States