Dipòsit Digital de Documents de la UAB 6 registres trobats  La cerca s'ha fet en 0.00 segons. 
1.
11 p, 9.5 MB Acute lymphoblastic leukemia necessitates GSH-dependent ferroptosis defenses to overcome FSP1-epigenetic silencing / Pontel, Lucas B. (Instituto de Investigación en Biomedicina de Buenos Aires) ; Bueno-Costa, Alberto (Institut Germans Trias i Pujol. Institut de Recerca contra la Leucèmia Josep Carreras) ; Morellato, Agustín E. (Instituto de Investigación en Biomedicina de Buenos Aires) ; Santos, Juliana (Institut Germans Trias i Pujol. Institut de Recerca contra la Leucèmia Josep Carreras) ; Roué, Gaël (Institut Germans Trias i Pujol. Institut de Recerca contra la Leucèmia Josep Carreras) ; Esteller, M (Institut Germans Trias i Pujol. Institut de Recerca contra la Leucèmia Josep Carreras) ; Universitat Autònoma de Barcelona
Ferroptosis is a form of cell death triggered by phospholipid hydroperoxides (PLOOH) generated from the iron-dependent oxidation of polyunsaturated fatty acids (PUFAs). To prevent ferroptosis, cells rely on the antioxidant glutathione (GSH), which serves as cofactor of the glutathione peroxidase 4 (GPX4) for the neutralization of PLOOHs. [...]
2022 - 10.1016/j.redox.2022.102408
Redox biology, Vol. 55 (september 2022) , p. 102408  
2.
15 p, 4.1 MB Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity / Carija, Anita (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pinheiro, Francisca (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pujols Pujol, Jordi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Brás, Inês C. (University Medicine Göttingen) ; Lázaro, Diana Fernandes (University Medicine Göttingen) ; Santambrogio, Carlo (University of Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ; Grandori, Rita (University of Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ; Outeiro, Tiago Fleming (Max Planck Institute for Experimental Medicine) ; Navarro, Susanna (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
The aggregation of α-synuclein (α-syn) into amyloid fibrils is a major pathological hallmark of Parkinson's disease (PD) and other synucleinopathies. The mechanisms underlying the structural transition of soluble and innocuous α-syn to aggregated neurotoxic forms remains largely unknown. [...]
2019 - 10.1016/j.redox.2019.101135
Redox biology, Vol. 22 (April 2019) , art. 101135  
3.
11 p, 1.0 MB Cardiomyocyte hypertrophy induced by Endonuclease G deficiency requires reactive oxygen radicals accumulation and is inhibitable by the micropeptide humanin / Blasco, Natividad (Institut de Recerca Biomèdica de Lleida) ; Cámara, Yolanda (Hospital Universitari Vall d'Hebron. Institut de Recerca) ; Núñez, Estefanía (Centro de Investigación Biomédica en Red en Enfermedades Cardiovasculares) ; Beà, Aida (Institut de Recerca Biomèdica de Lleida) ; Barés, Gisel (Institut de Recerca Biomèdica de Lleida) ; Forné, Carles (Institut de Recerca Biomèdica de Lleida) ; Ruíz-Meana, Marisol (Hospital Universitari Vall d'Hebron. Institut de Recerca) ; Girón, Cristina (Institut de Recerca Biomèdica de Lleida) ; Barba, Ignasi (Hospital Universitari Vall d'Hebron. Institut de Recerca) ; Garcia-Arumi, Elena (Hospital Universitari Vall d'Hebron. Institut de Recerca) ; García-Dorado, David (Hospital Universitari Vall d'Hebron. Institut de Recerca) ; Vázquez, Jesús (Centro de Investigación Biomédica en Red en Enfermedades Cardiovasculares) ; Martí, Ramon A. (Hospital Universitari Vall d'Hebron. Institut de Recerca) ; Llovera, Marta (Institut de Recerca Biomèdica de Lleida) ; Sanchis, Daniel (Institut de Recerca Biomèdica de Lleida)
The endonuclease G gene (Endog), which codes for a mitochondrial nuclease, was identified as a determinant of cardiac hypertrophy. How ENDOG controls cardiomyocyte growth is still unknown. Thus, we aimed at finding the link between ENDOG activity and cardiomyocyte growth. [...]
2018 - 10.1016/j.redox.2018.02.021
Redox biology, Vol. 16 (march 2018) , p. 146-156  
4.
16 p, 2.3 MB Iron-loaded transferrin (Tf) is detrimental whereas iron-free Tf confers protection against brain ischemia by modifying blood Tf saturation and subsequent neuronal damage / Gregorio-Rocasolano Barbany, Núria de (Institut Germans Trias i Pujol. Hospital Universitari Germans Trias i Pujol) ; Martí Sistac, Octavi (Universitat Autònoma de Barcelona) ; Ponce, Jovita (Institut Germans Trias i Pujol) ; Castelló Ruiz, María (Instituto de Investigación Sanitaria La Fe) ; Millán Torné, Mònica (Institut Germans Trias i Pujol. Hospital Universitari Germans Trias i Pujol) ; Guirao, Verónica (Institut Germans Trias i Pujol) ; García Yébenes, Isaac (Universidad Complutense de Madrid. Departamento de Farmacología) ; Salom, Juan B. (Instituto de Investigación Sanitaria La Fe) ; Ramos Cabrer, Pedro (Hospital Clínico Universitario (Santiago de Compostela, Galícia)) ; Alborch, Enrique (Instituto de Investigación Sanitaria La Fe) ; Lizasoain, Ignacio (Universidad Complutense de Madrid. Departamento de Farmacología) ; Castillo, José (Hospital Clínico Universitario (Santiago de Compostela, Galícia)) ; Dávalos, Antoni (Institut Germans Trias i Pujol. Hospital Universitari Germans Trias i Pujol) ; Gasull Dalmau, Teresa (Institut Germans Trias i Pujol)
Despite transferrin being the main circulating carrier of iron in body fluids, and iron overload conditions being known to worsen stroke outcome through reactive oxygen species (ROS)-induced damage, the contribution of blood transferrin saturation (TSAT) to stroke brain damage is unknown. [...]
2018 - 10.1016/j.redox.2017.11.026
Redox biology, Vol. 15 (May 2018) , p. 143-158  
5.
10 p, 1.2 MB A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation / Marinelli, Patrizia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Graña Montes, Ricardo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Bañó-Polo, Manuel (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Fernández Gallegos, María Rosario (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Papaleo, Elena (Kræftens Bekæmpelse) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Oxidatively modified forms of proteins accumulate during aging. Oxidized protein conformers might act as intermediates in the formation of amyloids in age-related disorders. However, it is not known whether this amyloidogenic conversion requires an extensive protein oxidative damage or it can be promoted just by a discrete, localized post-translational modification of certain residues. [...]
2017 - 10.1016/j.redox.2017.10.022
Redox biology, Vol. 14 (April 2018) , p. 566-575  
6.
13 p, 1.1 MB Protein aggregation into insoluble deposits protects from oxidative stress / Carija, Anita (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Sánchez de Groot, Natalia (Centre de Regulació Genòmica) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Protein misfolding and aggregation have been associated with the onset of neurodegenerative disorders. Recent studies demonstrate that the aggregation process can result in a high diversity of protein conformational states, however the identity of the specific species responsible for the cellular damage is still unclear. [...]
2017 - 10.1016/j.redox.2017.03.027
Redox biology, Vol. 12 (Aug. 2017) , p. 699-711  

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