Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Tomás Aragón"'
Autor:
Didio Alberto Ortiz, Nuria Peregrín, Miguel Valencia, Rodrigo Vinueza-Gavilanes, Elisa Marín-Ordovas, Roberto Ferrero, María Jesús Nicolás, Gloria González-Aseguinolaza, Montserrat Arrasate, Tomás Aragón
Publikováno v:
Translational Neurodegeneration, Vol 13, Iss 1, Pp 1-5 (2024)
Externí odkaz:
https://doaj.org/article/0766beaa99ca4b3eb0b071dad2693434
Autor:
Nuria Peregrín Pastor, Elias Marlin, Miguel Valencia, Roberto Ferrero, Maria Jesus Nicolás Apesteguía, Rodrigo Vinueza-Gavilanes, Julio Artieda, Monserrat Arrasate, Tomás Aragón
Publikováno v:
IBRO Neuroscience Reports, Vol 15, Iss , Pp S472- (2023)
Externí odkaz:
https://doaj.org/article/04e13ad62ba042f08226c2146de8aacf
Autor:
Jorge Juan Bravo González, Rodrigo Vinueza-Gavilanes, Africa Vales, Sarka Jelinkova, Gloria Gonzalez-Asteguinolaza, Maria S. Aymerich, Etienne Herzog, Tomás Aragón, Monserrat Arrasate
Publikováno v:
IBRO Neuroscience Reports, Vol 15, Iss , Pp S373- (2023)
Externí odkaz:
https://doaj.org/article/0d1cd9d3a04e4636af40435154119acc
Autor:
Rodrigo Vinueza-Gavilanes, Jorge Juan Bravo-González, Leyre Basurco, Chiara Boncristiani, Joaquín Fernández-Irigoyen, Enrique Santamaría, Irene Marcilla, Alberto Pérez-Mediavilla, María Rosario Luquin, Africa Vales, Gloria González-Aseguinolaza, María Soledad Aymerich, Tomás Aragón, Montserrat Arrasate
Publikováno v:
Neurobiology of Disease, Vol 183, Iss , Pp 106166- (2023)
Synucleinopathies are a group of neurodegenerative diseases without effective treatment characterized by the abnormal aggregation of alpha-synuclein (aSyn) protein. Changes in levels or in the amino acid sequence of aSyn (by duplication/triplication
Externí odkaz:
https://doaj.org/article/25360ce393ad40769705ef541732c8f6
Autor:
Silvia Gómez-Puerta, Roberto Ferrero, Tobias Hochstoeger, Ivan Zubiri, Jeffrey Chao, Tomás Aragón, Franka Voigt
Publikováno v:
eLife, Vol 11 (2022)
Endoplasmic reticulum (ER) to nucleus homeostatic signaling, known as the unfolded protein response (UPR), relies on the non-canonical splicing of XBP1 mRNA. The molecular switch that initiates splicing is the oligomerization of the ER stress sensor
Externí odkaz:
https://doaj.org/article/cc5ee2b790d849498e0cc49095d5486d
Autor:
Rodrigo Vinueza-Gavilanes, Ignacio Íñigo-Marco, Laura Larrea, Marta Lasa, Beatriz Carte, Enrique Santamaría, Joaquín Fernández-Irigoyen, Ricardo Bugallo, Tomás Aragón, Rafael Aldabe, Montserrat Arrasate
Publikováno v:
Neurobiology of Disease, Vol 137, Iss , Pp 104781- (2020)
Alpha-synuclein (aSyn) protein levels are sufficient to drive Parkinson's disease (PD) and other synucleinopathies. Despite the biomedical/therapeutic potential of aSyn protein regulation, little is known about mechanisms that limit/control aSyn leve
Externí odkaz:
https://doaj.org/article/67e0990734b34eb9969a4ddd16bcc80c
Publikováno v:
F1000Research, Vol 8 (2019)
Since its discovery more than 25 years ago, great progress has been made in our understanding of the unfolded protein response (UPR), a homeostatic mechanism that adjusts endoplasmic reticulum (ER) function to satisfy the physiological demands of the
Externí odkaz:
https://doaj.org/article/eb97b9b0e45447359e205555bbc357f7
Autor:
Annalisa Deodati, Josepmaría Argemí, Daniela Germani, Antonella Puglianiello, Anna Alisi, Cristiano De Stefanis, Roberto Ferrero, Valerio Nobili, Tomás Aragón, Stefano Cianfarani
Publikováno v:
PLoS ONE, Vol 13, Iss 6, p e0198490 (2018)
Early life events are associated with the susceptibility to chronic diseases in adult life. Perturbations of endoplasmic reticulum (ER) homeostasis activate the unfolded protein response (UPR), which contributes to the development of metabolic altera
Externí odkaz:
https://doaj.org/article/b4ed11d0edd64d0da0ff6e06a8179ed5
Autor:
Eelco van Anken, David Pincus, Scott Coyle, Tomás Aragón, Christof Osman, Federica Lari, Silvia Gómez Puerta, Alexei V Korennykh, Peter Walter
Publikováno v:
eLife, Vol 3 (2014)
Insufficient protein-folding capacity in the endoplasmic reticulum (ER) induces the unfolded protein response (UPR). In the ER lumen, accumulation of unfolded proteins activates the transmembrane ER-stress sensor Ire1 and drives its oligomerization.
Externí odkaz:
https://doaj.org/article/c6817a80e37e4180bc5d1af037ef86b9
Autor:
Marta Zamarbide, Eva Martinez-Pinilla, Ana Ricobaraza, Tomás Aragón, Rafael Franco, Alberto Pérez-Mediavilla
Publikováno v:
PLoS ONE, Vol 8, Iss 8, p e71082 (2013)
Understanding how neural cells handle proteostasis stress in the endoplasmic reticulum (ER) is important to decipher the mechanisms that underlie the cell death associated with neurodegenerative diseases and to design appropriate therapeutic tools. H
Externí odkaz:
https://doaj.org/article/e90813c3e0574b4ba4743db0ce5c6be7