1.
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13 p, 4.6 MB |
Aβ40 Aggregation under Changeable Conditions
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Curto, Jofre Seira (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Fernández Gallegos, María Rosario (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Cladera i Cerdà, Josep (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Benseny Cases, Núria (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Sánchez de Groot, Natalia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Homeostasis is crucial for cell function, and disturbances in homeostasis can lead to health disorders. Under normal conditions, intracellular pH is maintained between 7. 35 and 7. 45. Altered endosomal and lysosomal pH together with a general drop in brain pH are associated with the aggregation of amyloid-β-peptide (Aβ) and the development of Alzheimer's disease. [...]
2023 - 10.3390/ijms24098408
International journal of molecular sciences, Vol. 24, Issue 9 (May 2023) , art. 8408
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2.
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9 p, 1.5 MB |
In situ identification and G4-PPI-His-Mal-dendrimer-induced reduction of early-stage amyloid aggregates in Alzheimer's disease transgenic mice using synchrotron-based infrared imaging
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Benseny Cases, Núria (ALBA Laboratori de Llum de Sincrotró) ;
Álvarez-Marimon, Elena (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Aso, Ester (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Carmona, Margarita (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Klementieva, Oxana (Lund University. Department of Experimental Medical Science) ;
Appelhans, Dietmar (Leibniz Institute of Polymer Research) ;
Ferrer, Isidro (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Cladera i Cerdà, Josep (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Amyloid plaques composed of Aβ amyloid peptides and neurofibrillary tangles are a pathological hallmark of Alzheimer Disease. In situ identification of early-stage amyloid aggregates in Alzheimer's disease is relevant for their importance as potential targets for effective drugs. [...]
2021 - 10.1038/s41598-021-96379-4
Scientific reports, Vol. 11 (September 2021) , art. 18368
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3.
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9 p, 2.4 MB |
Pre-plaque conformational changes in Alzheimer's disease-linked Aβ and APP
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Klementieva, O. (Lund University. Department of Experimental Medical Science) ;
Willén, K. (Lund University. Department of Experimental Medical Science) ;
Martinsson, Isak (Lund University. Department of Experimental Medical Science) ;
Israelsson, B. (Lund University. Department of Experimental Medical Science) ;
Engdahl, A. (Lund University. MAX IV Laboratory) ;
Cladera i Cerdà, Josep (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Uvdal, P. (Lund University. Department of Chemistry) ;
Gouras, G. K. (Lund University. Department of Experimental Medical Science)
Reducing levels of the aggregation-prone Aβ peptide that accumulates in the brain with Alzheimer's disease (AD) has been a major target of experimental therapies. An alternative approach may be to stabilize the physiological conformation of Aβ. [...]
2017 - 10.1038/ncomms14726
Nature communications, Vol. 8 (March 2017) , art. 14726
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4.
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10 p, 2.4 MB |
In situ structural characterization of early amyloid aggregates in Alzheimer's disease transgenic mice and Octodon degus
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Benseny Cases, Núria (ALBA Laboratori de Llum de Sincrotró) ;
Álvarez Marimon, Elena (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Aso, Ester (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Carmona, Margarita (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Klementieva, Oxana (Lund University) ;
Appelhans, Dietmar (Leibniz Institute of Polymer Research) ;
Ferrer, Isidro (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Cladera i Cerdà, Josep (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Amyloid plaques composed of Aβ amyloid peptides and neurofibrillary tangles are a pathological hallmark of Alzheimer's disease. In situ identification of early-stage amyloid aggregates in Alzheimer's disease is relevant for their importance as potential targets for effective drugs. [...]
2020 - 10.1038/s41598-020-62708-2
Scientific reports, Vol. 10 (april 2020)
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5.
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11 p, 2.1 MB |
Structural biology workflow for the expression and characterization of functional human sodium glucose transporter type 1 in Pichia pastoris
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Suades, Albert (Stockholm University. Department of Biochemistry and Biophysics) ;
Alcaraz, Antonio (Universitat Jaume I. Departament de Física) ;
Cruz, Esteban (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Álvarez Marimon, Elena (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Whitelegge, Julian P. (David Geffen School of Medicine) ;
Manyosa, Joan (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Cladera i Cerdà, Josep (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Peralvarez-Marin, Alex (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Heterologous expression of human membrane proteins is a challenge in structural biology towards drug discovery. Here we report a complete expression and purification process of a functional human sodium/D-glucose co-transporter 1 (hSGLT1) in Pichia pastoris as representative example of a useful strategy for any human membrane protein. [...]
2019 - 10.1038/s41598-018-37445-2
Scientific reports, Vol. 9 (February 2019) , art. 1203
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6.
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12 p, 3.3 MB |
Poly(propylene imine) dendrimers with histidine-maltose shell as novel type of nanoparticles for synapse and memory protection
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Aso, Ester (ALBA Laboratori de Llum de Sincrotró) ;
Martinsson, Isak (Wallenberg Neuroscience Center) ;
Appelhans, Dietmar (Leibniz Institute of Polymer Research Dresden) ;
Effenberg, Christiane (Leibniz Institute of Polymer Research Dresden) ;
Benseny Cases, Núria (ALBA Laboratori de Llum de Sincrotró) ;
Cladera i Cerdà, Josep (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Gouras, Gunnar (Wallenberg Neuroscience Center) ;
Ferrer, Isidro (Hospital Universitari de Bellvitge) ;
Klementieva, Oxana (Wallenberg Neuroscience Center)
Poly(propylene imine) dendrimers have been shown to be promising 3-dimensional polymers for the use in the pharmaceutical and biomedical applications. Our aims of this study were first, to synthesize a novel type of dendrimer with poly(propylene imine) core and maltose-histidine shell (G4HisMal) assessing if maltose-histidine shell can improve the biocompatibility and the ability to cross the blood-brain barrier, and second, to investigate the potential of G4HisMal to protect Alzheimer disease transgenic mice from memory impairment. [...]
2019 - 10.1016/j.nano.2019.01.010
Nanomedicine, Vol. 17 (April 2019) , p. 198-209
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7.
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14 p, 2.6 MB |
Myoglobinopathy is an adult-onset autosomal dominant myopathy with characteristic sarcoplasmic inclusions
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Olivé i Plana, Montse (Institut d'Investigació Biomèdica de Bellvitge) ;
Engvall, Martin (Karolinska University Hospital and Karolinska Institutet (Suècia)) ;
Ravenscroft, Gianina (University of Western Australia. Harry Perkins Institute of Medical Research) ;
Cabrera Serrano, Macarena (Hospital Universitario Virgen del Rocío (Sevilla, Andalusia)) ;
Jiao, Hong (Karolinska University Hospital and Karolinska Institutet (Suècia)) ;
Bortolotti, Carlo Augusto (University of Modena and Reggio Emilia) ;
Pignataro, Marcello (University of Modena and Reggio Emilia) ;
Lambrughi, Matteo (University of Modena and Reggio Emilia) ;
Jiang, Haibo (The University of Western Australia) ;
Forrest, Alistair R. R. (University of Western Australia. Harry Perkins Institute of Medical Research) ;
Benseny Cases, Núria (ALBA Laboratori de Llum de Sincrotró) ;
Hofbauer, Stefan (BOKU-University of Natural Resources and Life Sciences) ;
Obinger, Christian (BOKU-University of Natural Resources and Life Sciences) ;
Battistuzzi, Gianantonio (University of Modena and Reggio Emilia) ;
Bellei, Marzia (University of Modena and Reggio Emilia) ;
Borsari, Marco (University of Modena and Reggio Emilia) ;
Di Rocco, Giulia (University of Modena and Reggio Emilia) ;
Viola, Helena M. (The University of Western Australia) ;
Hool, Livia C. (Victor Chang Cardiac Research Institute) ;
Cladera i Cerdà, Josep (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Lagerstedt-Robinson, Kristina (Karolinska University Hospital and Karolinska Institutet (Suècia)) ;
Xiang, Fengqing (Karolinska Institutet (Estocolm, Suècia)) ;
Wredenberg, Anna (Karolinska Institutet (Estocolm, Suècia)) ;
Miralles, Francesc (Hospital Universitari Son Espases (Palma de Mallorca, Balears)) ;
Baiges, Juanjo (Hospital de Tortosa Verge de la Cinta) ;
Malfatti, Edoardo (Centre de Référence de Pathologie Neuromusculaire Paris-Est) ;
Romero, Norma B. (Centre de Référence de Pathologie Neuromusculaire Paris-Est) ;
Streichenberger, Nathalie (Université Claude Bernard Lyon) ;
Vial, Christophe (Electromyographie-Groupement Hospitalier Est) ;
Claeys, Kristl G. (KU Leuven-University of Leuven) ;
Straathof, Chiara S. M. (Leiden University Medical Center) ;
Goris, An (KU Leuven-University of Leuven) ;
Freyer, Christoph (Karolinska Institutet (Estocolm, Suècia)) ;
Lammens, Martin (Radboud University Medical Center) ;
Bassez, Guillaume (East-Paris University (UPEC)) ;
Kere, Juha (King's College London) ;
Clemente, Paula (Karolinska Institutet (Estocolm, Suècia)) ;
Sejersen, Thomas (Karolinska Institutet (Estocolm, Suècia)) ;
Udd, Bjarne (Tampere University Hospital) ;
Vidal, Noemí (Institut d'Investigació Biomèdica de Bellvitge) ;
Ferrer, Isidro (Universitat de Barcelona) ;
Edström, Lars (Karolinska Institutet (Estocolm, Suècia)) ;
Wedell, Anna (Karolinska University Hospital and Karolinska Institutet (Suècia)) ;
Laing, Nigel G. (University of Western Australia. Harry Perkins Institute of Medical Research)
Myoglobin, encoded by MB, is a small cytoplasmic globular hemoprotein highly expressed in cardiac myocytes and oxidative skeletal myofibers. Myoglobin binds O facilitates its intracellular transport and serves as a controller of nitric oxide and reactive oxygen species. [...]
2019 - 10.1038/s41467-019-09111-2
Nature communications, Vol. 10 (March 2019) , art. 1396
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8.
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1 p, 82.3 KB |
Biofísics de la UAB acorralen la SIDA
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Cladera i Cerdà, Josep (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Un equip de biofísics de la UAB desentranya el procés molecular de la SIDA i ens presenta els seus resultats. Al seu laboratori van recrear artificialment part del procés víric i les seves conclusions són interessants. [...] Un equipo de biofísicos de la UAB desentraña el proceso molecular del SIDA y nos presenta sus resultados. En su laboratorio recrearon artificialmente parte del mismo proceso vírico y sus conclusiones son interesantes. [...] A team of biophysicists at the UAB have discovered the molecular process involved in AIDS and present their results. In their laboratory they artificially recreated part of the viral process and their conclusions are interesting. [...]
2006
UAB divulga, març 2006, p. 1-1
3 documents
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9.
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1 p, 78.0 KB |
Dendrimer : un producte nanotecnològic contra l'Alzheimer
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Cladera i Cerdà, Josep (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Dendrimer és el nom d'una molècula sintètica que neix d'un procés nanotecnològic utilitzada per diversos sectors de les ciències aplicades per desenvolupar els seus treballs. Tal és el cas d'un grup d'investigadors de la UAB que utilitza els dendrimers com a fàrmacs per combatre malalties neurodegeneratives com l'Alzheimer. Dendrimer es el nombre de una molécula sintética que nace de un proceso nanotecnológico utilizada por varios sectores de las ciencias aplicadas para desarrollar sus trabajos. Tal es caso de un grupo de investigadores de la UAB que utiliza los dendrimers como fármacos para combatir enfermedades neurodegenerativas como el Alzheimer. [...] Dendrimer is the name of a synthetic molecule which is produced by a nanotechnological process used by various sectors of the applied sciences to carry out their work. Such is the case of a group of researchers at the UAB who use dendrimers as drugs to fight neurodegenerative diseases such as Alzheimer.
2006
UAB divulga, juny 2006, p. 1-1
3 documents
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