Dipòsit Digital de Documents de la UAB 4 registres trobats  La cerca s'ha fet en 0.00 segons. 
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11 p, 2.5 MB The small aromatic compound SynuClean-D inhibits the aggregation and seeded polymerization of multiple α-synuclein strains / Peña Díaz, Samuel (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") ; Vasili, Eftychia (Max Planck Institute for Experimental Medicine) ; Pinheiro, Francisca (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Santos, Jaime (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Manglano-Artuñedo, Zoe (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Outeiro, Tiago Fleming (Scientific Employee With a Honorary Contract. Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE)) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Parkinson's disease is a neurodegenerative disorder characterized by the loss of dopaminergic neurons in the substantia nigra, as well as the accumulation of intraneuronal proteinaceous inclusions known as Lewy bodies and Lewy neurites. [...]
2022 - 10.1016/j.jbc.2022.101902
Journal of biological chemistry, Vol. 298, Issue 5 (May 2022) , art. 101902  
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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  
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4 p, 393.4 KB Copper(II) and the pathological H50Q α-synuclein mutant : environment meets genetics / Villar-Piqué, Anna (University Medical Centre Göottingen. Department of Neurodegeneration and Restorative Research) ; Rossetti, Giulia (Jülich Forschungszentrum. Institut für Neurowissenschaften und Medizin) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Carloni, Paolo (Jülich Forschungszentrum. Institut für Neurowissenschaften und Medizin) ; Fernández, Claudio O. (Max Planck Laboratory for Structural Biology, Chemistry and Molecular Biophysics of Rosario) ; Outeiro, Tiago Fleming (University Medical Centre Göottingen. Department of Neurodegeneration and Restorative Research) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
Copper is one of the metals described to bind the Parkinson disease-related protein α-synuclein (aSyn), and to promote its aggregation. Although histidine at position 50 in the aSyn sequence is one of the most studied copper-anchoring sites, its precise role in copper binding and aSyn aggregation is still unclear. [...]
2017 - 10.1080/19420889.2016.1270484
Communicative & integrative Biology, Vol. 10, no. 1 (2017) , e127048  
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15 p, 4.8 MB The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation / Lázaro, Diana F. (Universitätsmedizin Göttingen) ; Dias, Mariana Castro (Universitätsmedizin Göttingen) ; 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) ; Madaleno, Carolina Silva (Universidade Nova de Lisboa. Centro de Estudos de Doenças Crónicas) ; Tenreiro, Sandra (Universidade Nova de Lisboa. Centro de Estudos de Doenças Crónicas) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Outeiro, Tiago Fleming (Max-Planck-Gesellschaft)
α-synuclein (aSyn) is associated with both sporadic and familial forms of Parkinson's disease (PD), the second most common neurodegenerative disorder after Alzheimer's disease. In particular, multiplications and point mutations in the gene encoding for aSyn cause familial forms of PD. [...]
2016 - 10.1186/s40478-016-0402-8
Acta neuropathologica communications, Vol. 4 (2016) , art. 128  

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