Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Natàlia Carulla"'
Autor:
Sonia Ciudad, Eduard Puig, Thomas Botzanowski, Moeen Meigooni, Andres S. Arango, Jimmy Do, Maxim Mayzel, Mariam Bayoumi, Stéphane Chaignepain, Giovanni Maglia, Sarah Cianferani, Vladislav Orekhov, Emad Tajkhorshid, Benjamin Bardiaux, Natàlia Carulla
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Formation of amyloid-beta (Aβ) oligomer pores in the membrane of neurons has been proposed to explain neurotoxicity in Alzheimer´s disease. Here authors present the 3D- structure of an Aβ oligomer formed in a membrane mimicking environment and obs
Externí odkaz:
https://doaj.org/article/2c0e9ea1270e440fb213d992e9ac74ae
Publikováno v:
Frontiers in Molecular Biosciences, Vol 5 (2018)
We have recently reported on the preparation of a membrane-associated β-barrel Pore-Forming Aβ42 Oligomer (βPFOAβ42). It corresponds to a stable and homogeneous Aβ42 oligomer that inserts into lipid bilayers as a well-defined pore and adopts a s
Externí odkaz:
https://doaj.org/article/9d3741fc28994ae3bce05e30c9cb736c
Autor:
Emad Tajkhorshid, Eduard Puig, Sonia Ciudad, Thomas Botzanowski, Mariam Bayoumi, Vladislav Yu. Orekhov, Benjamin Bardiaux, Giovanni Maglia, Sarah Cianférani, Andres S. Arango, Stéphane Chaignepain, Jimmy Do, Moeen Meigooni, Natàlia Carulla, Maxim Mayzel
Publikováno v:
Nature Communications, 11(1):3014. Nature Publishing Group
Nature Communications
Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.3014. ⟨10.1038/s41467-020-16566-1⟩
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Nature Communications, 2020, 11 (1), pp.3014. ⟨10.1038/s41467-020-16566-1⟩
Nature Communications
Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.3014. ⟨10.1038/s41467-020-16566-1⟩
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Nature Communications, 2020, 11 (1), pp.3014. ⟨10.1038/s41467-020-16566-1⟩
Formation of amyloid-beta (Aβ) oligomer pores in the membrane of neurons has been proposed to explain neurotoxicity in Alzheimerʼs disease (AD). Here, we present the three-dimensional structure of an Aβ oligomer formed in a membrane mimicking envi
Autor:
Marcelo J. Kogan, Andreas Tapia-Arellano, Freddy Celis, Marcelo Campos, Natàlia Carulla, Eduardo Gallardo-Toledo, Italo Moglia, Mauricio Baez, Rodrigo Rivera
Publikováno v:
Materials scienceengineering. C, Materials for biological applications. 128
Gold nanoparticles (GNP) are tunable nanomaterials that can be used to develop rational therapeutic inhibitors against the formation of pathological aggregates of proteins. In the case of the pathological aggregation of the amyloid-β protein (Aβ),
Publikováno v:
ACS chemical neuroscience. 11(20)
Somatostatin (SST14) is strongly related to Alzheimer's disease (AD), as its levels decline during aging, it regulates the proteolytic degradation of the amyloid beta peptide (Aβ), and it binds to Aβ oligomers
Somatostatin (SST14) is strongly related to Alzheimer’s disease (AD), as its levels decline during aging, it regulates the proteolytic degradation of the amyloid beta peptide (Aβ), and it binds to Aβ oligomers in vivo. Recently, the 3D structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9ba4c9168d988116caebc628e6dfb50
https://doi.org/10.1101/2020.05.11.088153
https://doi.org/10.1101/2020.05.11.088153
Autor:
Natàlia Carulla, Raquel García-Castellanos, Nicholas S. Berrow, Bernat Serra-Vidal, Martí Ninot-Pedrosa, Montserrat Serra-Batiste
Publikováno v:
Dipòsit Digital de la UB
Universidad de Barcelona
Recercat. Dipósit de la Recerca de Catalunya
instname
Universidad de Barcelona
Recercat. Dipósit de la Recerca de Catalunya
instname
Background: The aggregation of the amyloid-beta peptide (Aβ) in the brain is strongly associated with Alzheimer´s disease (AD). However, the heterogeneous and transient nature of this process has prevented identification of the exact molecular form
Autor:
Natàlia Carulla, Moeen Meigooni, Jimmy Do, Emad Tajkhorshid, Maxim Mayzel, Benjamin Bardiaux, Sonia Ciudad, Eduard Puig, Sarah Cianférani, Giovanni Maglia, Mariam Bayoumi, Vladislav Yu. Orekhov, Stéphane Chaignepain, Andres S. Arango, Thomas Botzanowski
The formation of amyloid-beta (Aβ) oligomer pores in the membrane of neurons has been proposed as the means to explain neurotoxicity in Alzheimer’s disease (AD). It is therefore critical to characterize Aβ oligomer samples in membrane-mimicking e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57f575715ab50208a8bd616a7a2d4125
https://doi.org/10.1101/759472
https://doi.org/10.1101/759472
Autor:
Montserrat, Serra-Batiste, Martí, Ninot-Pedrosa, Eduard, Puig, Sonia, Ciudad, Margarida, Gairí, Natàlia, Carulla
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1779
The formation of amyloid-β peptide (Aβ) oligomers at the cellular membrane is considered a crucial process that underlies neurotoxicity in Alzheimer's disease (AD). To obtain structural information on this type of oligomers, we were inspired by mem
Autor:
Aurelio Vázquez de la Torre, Marina Gay, Sílvia Vilaprinyó-Pascual, Roberta Mazzucato, Montserrat Serra-Batiste, Marta Vilaseca, Natàlia Carulla
Publikováno v:
Dipòsit Digital de la UB
Universidad de Barcelona
Recercat. Dipósit de la Recerca de Catalunya
instname
Universidad de Barcelona
Recercat. Dipósit de la Recerca de Catalunya
instname
Brain-derived amyloid-β (Aβ) dimers are associated with Alzheimer's disease (AD). However, their covalent nature remains controversial. This feature is relevant, as a covalent cross-link has been proposed to make brain-derived dimers (brain dimers)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14f10b072bbee8dda080cd5b1f212531
http://hdl.handle.net/2445/121061
http://hdl.handle.net/2445/121061