TY  - JOUR
AU  - Guerrero-Gómez, David
AU  - Mora-Lorca, José Antonio
AU  - Sáenz-Narciso, Beatriz
AU  - Naranjo-Galindo, Francisco José
AU  - Muñoz-Lobato, Fernando
AU  - Parrado-Fernández, Cristina
AU  - Goikolea, Julen
AU  - Cedazo-Minguez, Ángel
AU  - Link, Christopher D
AU  - Neri, Christian
AU  - Sequedo, María Dolores
AU  - Vázquez-Manrique, Rafael P
AU  - Fernández-Suárez, Elena
AU  - Goder, Veit
AU  - Pané, Roser
AU  - Cabiscol, Elisa
AU  - Askjaer, Peter
AU  - Cabello, Juan
AU  - Miranda-Vizuete, Antonio
PY  - 2019
DO  - 10.1038/s41418-018-0270-9
UR  - http://hdl.handle.net/10668/13573
T2  - Cell death and differentiation
AB  - In the presence of aggregation-prone proteins, the cytosol and endoplasmic reticulum (ER) undergo a dramatic shift in their respective redox status, with the cytosol becoming more oxidized and the ER more reducing. However, whether and how changes in...
LA  - en
KW  - Amyloid beta-Peptides
KW  - Animals
KW  - Autophagy
KW  - Basic Helix-Loop-Helix Transcription Factors
KW  - Caenorhabditis elegans
KW  - Caenorhabditis elegans Proteins
KW  - Cell Line
KW  - Endoplasmic Reticulum
KW  - Glutathione
KW  - Glutathione Reductase
KW  - Homeostasis
KW  - Humans
KW  - Maleates
KW  - Muscle Cells
KW  - Neurons
KW  - Oxidation-Reduction
KW  - Peptides
KW  - Phenotype
KW  - Protein Aggregation, Pathological
KW  - Proteolysis
KW  - Proteostasis
KW  - Saccharomyces cerevisiae
KW  - Sequestosome-1 Protein
KW  - alpha-Synuclein
TI  - Loss of glutathione redox homeostasis impairs proteostasis by inhibiting autophagy-dependent protein degradation.
TY  - research article
VL  - 26
ER  -