No se han encontrado coincidencias con Oligomers., pero utilizando en su lugar Oligomers ...
Resultados globales: 11 registros encontrados en 0.02 segundos.
Artículos, Encontrados 8 registros
Documentos de investigación, Encontrados 3 registros
Artículos Encontrados 8 registros  
1.
52 p, 705.6 KB Role of Amyloid-β and Tau Proteins in Alzheimer's Disease : Confuting the Amyloid Cascade / Gulisano, W. (Department of Biomedical and Biotechnological Sciences. Section of Physiology. University of Catania) ; Maugeri, Daniele (Department of Biomedical and Biotechnological Sciences. Section of Physiology. University of Catania) ; Baltrons Soler, Ma. Antonia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Fà, Mauro (Taub Institute for Research on Alzheimer's Disease and the Aging Brain. Department of Medicine. Columbia University) ; Amato, Arianna (Department of Anaesthesiology. Università Cattolica Del Sacro Cuore) ; Palmeri, Agostino (Department of Biomedical and Biotechnological Sciences. Section of Physiology. University of Catania) ; D'Adamio, Luciano (Department of Pharmacology. Physiology and Neuroscience. Rutgers University) ; Grassi, Claudio (Institute of Human Physiology. Università Cattolica Del Sacro Cuore) ; Devanand, D.P. (Department of Psychiatry. Columbia University. College of Phys. and Surg.) ; Honig, Lawrence S. (Department of Neurology. Columbia University. College of Phys. and Surg.) ; Puzzo, Daniela (Department of Biomedical and Biotechnological Sciences. Section of Physiology. University of Catania) ; Arancio, Ottavio (Taub Institute for Research on Alzheimer's Disease and the Aging Brain. Department of Medicine. Columbia University)
The "Amyloid Cascade Hypothesis" has dominated the Alzheimer's disease (AD) field in the last 25 years. It posits that the increase of amyloid-β (Aβ) is the key event in AD that triggers tau pathology followed by neuronal death and eventually, the disease. [...]
2018 - 10.3233/JAD-179935
Journal of Alzheimer's disease, Vol. 64 Núm. s1 (2018) , p. S611-S631  
2.
11 p, 2.1 MB A glimpse into the structural properties of α-synuclein oligomers / Santos, Jaime (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Pallarès i Goitiz, Irantzu (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)
α-Synuclein (αS) aggregation is the main neurological hallmark of a group of debilitating neurodegenerative disorders, collectively referred to as synucleinopathies, of which Parkinson's disease is the most prevalent. [...]
2023 - 10.1002/biof.2021
BioFactors, (December 2023) , p. 1-11  
3.
10 p, 508.1 KB Extracellular vesicles : where the amyloid precursor protein carboxyl-terminal fragments accumulate and amyloid-β oligomerizes / Pérez-González, Rocío (Institut d'Investigació Biomèdica Sant Pau) ; Kim, Y. (New York University School of Medicine) ; Miller, C. (Nathan S. Kline Institute) ; Pacheco-Quinto, J. (Biomedical Research Institute of New Jersey) ; Eckman, E.A. (Biomedical Research Institute of New Jersey) ; Levy, E. (New York University School of Medicine) ; Universitat Autònoma de Barcelona
Pleiotropic roles are proposed for brain extracellular vesicles (EVs) in the development of Alzheimer's disease (AD). Our previous studies have suggested a beneficial role for EVs in AD, where the endosomal system in vulnerable neurons is compromised, contributing to the removal of accumulated material from neurons. [...]
2020 - 10.1096/fj.202000823R
FASEB Journal, Vol. 34 Núm. 9 (january 2020) , p. 12922-12931  
4.
14 p, 6.1 MB OligoBinders : Bioengineered Soluble Amyloid-like Nanoparticles to Bind and Neutralize SARS-CoV-2 / Behbahanipour, Molood (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Benoit, Roger (Paul Scherrer Institut. Division of Biology and Chemistry) ; 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 coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection has become a primary health concern. Molecules that prevent viral entry into host cells by interfering with the interaction between SARS-CoV-2 spike (S) protein and the human angiotensin-converting enzyme 2 receptor (ACE2r) opened a promising avenue for virus neutralization. [...]
2023 - 10.1021/acsami.2c18305
ACS applied materials & interfaces, Vol. 15, Issue 9 (February 2023) , p. 11444-11457  
5.
180.1 KB Editorial : role of ribonucleases in immune response regulation during infection and cancer / Boix i Borràs, Esther (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Acquati, Francesco (Università degli studi di Insubria. Dipartimento di Biotecnologie e Scienze della Vita) ; Leonidas, Demetres (University of Thessaly. Department of Biochemistry and Biotechnology) ; Pulido-Gomez, David (University of Oxford. Nuffield Department of Medicine)
2020 - 10.3389/fimmu.2020.00236
Frontiers in immunology, Vol. 11 (Feb. 2020) , art. 236  
6.
12 p, 1.4 MB Al-pillared montmorillonite obtained in concentrated media. Effect of the anions (nitrate, sulfate and chloride) associated with the Al species / Aouad, Amina (Université d'Orléans) ; Pineau, Alain (Université d'Orléans) ; Tchoubar, Denise (CRT Plasma-Laser) ; Bergaya, Faïza (Université d'Orléans)
Basic Al chloride, sulfate and nitrate were prepared by hydrolysis of Al chloride followed by precipitation with a Na sulfate solution, then re-dissolution in a Ba nitrate solution. The three laboratory-synthesized oligomers and solid, commercial chlorhydrol were characterized by X-ray diffraction, Al nuclear magnetic resonance and scanning electron microscopy coupled with energy dispersion spectroscopy analysis. [...]
2006 - 10.1346/CCMN.2006.0540509
Clays and Clay Minerals, Vol. 54, Núm. 5 (2006) , p. 626-637  
7.
12 p, 2.4 MB The antigen-binding fragment of human gamma immunoglobulin prevents amyloid β-peptide folding into β-sheet to form oligomers / Valls-Comamala, Victòria (Universitat Pompeu Fabra. Laboratori de Fisiologia Molecular) ; Guivernau, Biuse (Universitat Pompeu Fabra. Laboratori de Fisiologia Molecular) ; Bonet, Jaume (Universitat Pompeu Fabra. Unitat de Recerca en Informàtica Biomèdica (GRIB)) ; Puig Font, Marta (Universitat Pompeu Fabra. Laboratori de Fisiologia Molecular) ; Peralvarez-Marin, Alex (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Palomer, Ernest (Universitat Pompeu Fabra. Laboratori de Fisiologia Molecular) ; Fernàndez-Busquets, Xavier (Institut de Bioenginyeria de Catalunya) ; Altafaj, Xavier (Institut d'Investigació Biomèdica de Bellvitge) ; Tajes, Marta (Institut Hospital del Mar d'Investigacions Mèdiques) ; Puig-Pijoan, Albert (Parc de Salut MAR de Barcelona) ; Vicente, Rubén (Universitat Pompeu Fabra. Laboratori de Fisiologia Molecular) ; Oliva Miguel, Baldomero (Universitat Pompeu Fabra. Unitat de Recerca en Informàtica Biomèdica (GRIB)) ; Muñoz, Francisco J. (Universitat Pompeu Fabra. Laboratori de Fisiologia Molecular)
The amyloid beta-peptide (Aβ) plays a leading role in Alzheimer's disease (AD) physiopathology. Even though monomeric forms of Aβ are harmless to cells, Aβ can aggregate into β-sheet oligomers and fibrils, which are both neurotoxic. [...]
2017 - 10.18632/oncotarget.17074
Oncotarget, Vol. 8, Num. 25 (June 2017) , p. 41154-41165  
8.
44 p, 2.3 MB Early intervention in the 3xTg-AD mice with an amyloid β-antibody fragment ameliorates first hallmarks of Alzheimer disease / Gimenez-Llort, Lydia (Universitat Autònoma de Barcelona. Institut de Neurociències) ; Rivera Hernández, Geovanny (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Marin Argany, Marta (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Sánchez Quesada, José Luis (Institut d'Investigació Biomèdica Sant Pau) ; Villegas Hernández, Sandra (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona
The single-chain variable fragment, scFv-h3D6, has been shown to prevent in vitro toxicity induced by the amyloid β (Aβ) peptide in neuroblastoma cell cultures by withdrawing Aβ oligomers from the amyloid pathway. [...]
2013 - 10.4161/mabs.25424
MAbs, Vol. 5 Issue 5(Sep 2013) , p. 665-864  

Documentos de investigación Encontrados 3 registros  
1.
1 p, 10.8 MB Deciphering hIAPP : a novel way to cure diabetes / Ruiz López, Iñigo ; Pallarès i Goitiz, Irantzu, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Facultat de Biociències
Human islet amyloid polypeptide (hIAPP) is produced by pancreatic β-cells and is involved in type-II diabetes mellitus (T2DM) pathogenesis. In T2DM, the loss of pancreatic β-cell mass is accompanied by the accumulation of amyloid deposits of hIAPP. [...]
2019-05-29
Grau en Biotecnologia [815]  
2.
145 p, 1.9 MB Mathematical modeling of oligomerization and biased signaling of G-protein-coupled receptors / Zhou, Bin ; Giraldo, Jesús, dir. ; Universitat Autònoma de Barcelona. Institut de Neurociències
Los receptores acoplados a proteínas G (GPCRs) juegan un papel muy importante en una gran variedad de procesos biológicos. Estos receptores están localizados en la membrana y median las rutas de señalización celulares. [...]
G-protein-coupled receptors (GPCRs) play very important roles in a great variety of biological processes. They are located in the membrane and mediate the signaling pathways in the cell. It is widely accepted that these receptors often form oligomers which may have significant physiological functions. [...]

[Barcelona] : Universitat Autònoma de Barcelona, 2019.  
3.
163 p, 10.3 MB Supramolecular organisation and biological properties of tumor targeted, self-assembling protein nanoparticles / Pesarrodona Roches, Mireia ; Villaverde Corrales, Antonio, dir. (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ; Vázquez Gómez, Esther, dir. (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ; Ferrer-Miralles, Neus, dir. (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ; Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia
Degut a la seva flexibilitat funcional i arquitectònica, l'ús de proteïnes recombinants formades per múltiples dominis representen una eina interesant pel desenvolupament de nanopartícules capaces de transportar fàrmacs de manera específica. [...]
Recombinant multidomain protein building-blocks have demonstrated to be an appealing biotechnological approach for the development of cell-targeted, nanoscale drug carriers on account of protein functional and architectonic versatility. [...]

[Barcelona] : Universitat Autònoma de Barcelona, 2017  

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