Browsing by Author "Andreu, Catherine"

Now showing items 1-3 of 3

    • ALS-linked protein disulfide isomerase variants cause motor dysfunction 
      Woehlbier, Ute; Colombo Flores, Alicia; Saaranen, Mirva J.; Pérez, Viviana; Ojeda, Jorge; Bustos, Fernando J.; Andreu, Catherine; Torres, Mauricio; Valenzuela, Vicente; Medinas Bilches, Danilo; Rozas, Pablo; Vidal, René L.; López González, Rodrigo; Salameh, Johnny; Fernández Collemann, Sara; Muñoz, Natalia; Matus, Soledad; Armisen Yáñez, Ricardo; Sagredo, Alfredo; Palma, Karina; Irrázabal, Thergiory; Almeida, Sandra; González Pérez, Paloma; Campero, Mario; Gao, Fen-Biao; Henny, Pablo; Van Zundert, Brigitte; Ruddock, Lloyd W.; Concha, Miguel L.; Henríquez, Juan P.; Brown, Robert H.; Hetz Flores, Claudio (Wiley-Blackwell, 2016)
      Disturbance of endoplasmic reticulum (ER) proteostasis is a common feature of amyotrophic lateral sclerosis (ALS). Protein disulfide isomerases (PDIs) are ER foldases identified as possible ALS biomarkers, as well as ...
    • Functional Role of the Disulfide Isomerase ERp57 in Axonal Regeneration 
      Castillo, Valentina; Oñate, Maritza G.; Woehlbier, Ute; Rozas, Pablo; Andreu, Catherine; Medinas Bilches, Danilo; Valdés, Pamela; Osorio, Fabiola; Mercado, Gabriela; Vidal, René L.; Kerr, Bredford; Court, Felipe A.; Hetz Flores, Claudio (Public Library Science, 2015)
      ERp57 (also known as grp58 and PDIA3) is a protein disulfide isomerase that catalyzes disulfide bonds formation of glycoproteins as part of the calnexin and calreticulin cycle. ERp57 is markedly upregulated in most common ...
    • The Protein-disulfide Isomerase ERp57 Regulates the Steady-state Levels of the Prion Protein 
      Torres, Mauricio; Medinas Bilches, Danilo; Matamala, José Manuel; Woehlbier, Ute; Cornejo, Víctor Hugo; Solda, Tatiana; Andreu, Catherine; Rozas, Pablo; Matus, Soledad; Muñoz, Natalia; Vergara, Carmen; Cartier Rovirosa, Luis; Soto, Claudio; Molinari, Maurizio; Hetz Flores, Claudio (Amer Soc Biochemistry Molecular Biology, 2015)
      Although the accumulation of a misfolded and protease-resistant form of the prion protein (PrP) is a key event in prion pathogenesis, the cellular factors involved in its folding and quality control are poorly understood. ...