Browsing by Author "Soto, Claudio"

Now showing items 1-11 of 11

    • Brains from non-Alzheimer's individuals containing amyloid deposits accelerate Aβ deposition in vivo 
      Durán Aniotz, Claudia; Morales, Rodrigo; Moreno González, Inés; Hu, Ping Ping; Soto, Claudio (BioMed Central, 2013)
      Background: One of the main features of Alzheimer’s disease (AD) is the presence of Aβ deposits, which accumulate in the brain years before the onset of symptoms. We and others have demonstrated that cerebral Aβ-amyloidosis ...
    • Calcium and gadolinium ions stimulate the GTPase activity of purified chicken brain tubulin through a ... 
      Soto, Claudio; Rodríguez, Patricio H.; Monasterio Opazo, Octavio (1996)
      Ca2+ and Gd3+ stimulated the GTPase activity of chicken brain tubulin 13- and 26-fold, respectively. Mg2+, Tb3+, and Na+ had no effect. This GTPase activity showed a saturation behavior with Ca2+ and Gd3+ with a maximal ...
    • Cell-free propagation of prion strains 
      Castilla, Joaquín; Morales, Rodrigo; Saá, Paula; Barría, Marcelo; Gambetti, Pierluigi; Soto, Claudio (NATURE PUBLISHING GROUP, 2008-10-08)
      Prions are the infectious agents responsible for prion diseases, which appear to be composed exclusively by the misfolded prion protein (PrPSc). Disease is transmitted by the autocatalytic propagation of PrPSc misfolding ...
    • Crossing the species barrier by PrPSc replication in vitro generates unique infectious Prions 
      Castilla, Joaquín; González Romero, Dennisse; Saá, Paula; Morales, Rodrigo; Castro, Jorge de; Soto, Claudio (CELL PRESS, 2008-09-05)
      Prions are unconventional infectious agents composed exclusively of misfolded prion protein (PrPSc), which transmits the disease by propagating its abnormal conformation to the cellular prion protein (PrPC). A key ...
    • De novo generation of infectious prions in vitro produces a new disease phenotype 
      Barría, Marcelo; Mukherjee, Abhisek; González Romero, Dennisse; Morales, Rodrigo; Soto, Claudio (2009)
      Prions are the proteinaceous infectious agents responsible for Transmissible Spongiform Encephalopathies. Compelling evidence supports the hypothesis that prions are composed exclusively of a misfolded version of the prion ...
    • Molecular cross talk between misfolded proteins in animal models of alzheimer's and prion diseases 
      Morales, Rodrigo; Estrada, Lisbell D.; Diaz-Espinoza, Rodrigo; Morales-Scheihing, Diego; Jara, Maria C.; Castilla, Joaquin; Soto, Claudio (2010)
      The central event in protein misfolding disorders (PMDs) is the accumulation of a misfolded form of a naturally expressed protein. Despite the diversity of clinical symptoms associated with different PMDs, many similarities ...
    • Perturbation of endoplasmic reticulum homeostasis facilitates prion replication 
      Hetz Flores, Claudio; Castilla, Joaquín; Soto, Claudio (2007)
      Prion diseases are fatal and infectious neurodegenerative disorders characterized by the accumulation of an abnormally folded form of the prion protein ( PrP), termed PrPSc. Prion replication triggers endoplasmic reticulum ...
    • Prion Protein Misfolding Affects Calcium Homeostasis and Sensitizes Cells to Endoplasmic Reticulum Stress 
      Torres, Mauricio; Castillo, Karen; Armisen Yáñez, Ricardo; Stutzin Schottlander, Andrés; Soto, Claudio; Hetz Flores, Claudio (2010)
      Prion-related disorders (PrDs) are fatal neurodegenerative disorders characterized by progressive neuronal impairment as well as the accumulation of an abnormally folded and protease resistant form of the cellular prion ...
    • Prion replication alters the distribution of synaptophysin and caveolin 1 in neuronal lipid rafts 
      Russelakis Carneiro, Milene; Hetz Flores, Claudio; Maundrell, Kinsey; Soto, Claudio (AMER SOC INVESTIGATIVE PATHOLOGY, 2004-11)
      The main event in the pathogenesis of prion diseases is the conversion of the cellular prion protein (PrPC) into the abnormal, protease-resistant prion protein (PrPres). PrPC is a GPI-anchored protein located in lipid rafts ...
    • The Endoplasmic Reticulum Chaperone GRP78/BiP Modulates Prion Propagation in vitro and in vivo 
      Park, Kyung Won; Eun Kim, Gyoung; Morales, Rodrigo; Moda, Fabio; Moreno González, Inés; Concha Marambio, Luis; Lee, Amy S.; Hetz Flores, Claudio; Soto, Claudio (Nature Publishing Group, 2017)
      © The Author(s) 2017. Prion diseases are fatal neurodegenerative disorders affecting several mammalian species, characterized by the accumulation of the misfolded form of the prion protein, which is followed by the induction ...
    • Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis 
      Hetz Flores, Claudio; Lee, Ann Hwee; González Romero, Dennisse; Thielen, Peter; Castilla, Joaquín; Soto, Claudio; Glimcher, Laurie H. (2008)
      The unfolded protein response (UPR) is a conserved adaptive reaction that increases cell survival under endoplasmic reticulum (ER) stress conditions. X-box-binding protein-1 (XBP-1) is a key transcriptional regulator of ...