Resultados globales: 7 registros encontrados en 0.02 segundos.
Artículos, Encontrados 6 registros
Documentos de investigación, Encontrados 1 registros
Artículos Encontrados 6 registros  
1.
15 p, 4.1 MB Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity / Carija, Anita (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pinheiro, Francisca (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pujols, Jordi (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 F. (Max Planck Institute for Experimental Medicine) ; Navarro Cantero, Susanna (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  
2.
12 p, 3.6 MB ZPD-2, a small compound that inhibits α-synuclein amyloid aggregation and its seeded polymerization / Peña Díaz, Samuel (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pujols, Jordi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Conde Giménez, María (Universidad de Zaragoza. Instituto Universitario de Investigación de Biocomputación y Física de Sistemas Complejos) ; Čarija, Anita (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Dalfo, Esther (Universitat Autònoma de Barcelona. Facultat de Medicina) ; García, Jesús (Institut de Recerca Biomèdica) ; Navarro Cantero, Susanna (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pinheiro, Francisca (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Santos Suárez, Jaime (Universitat Autonoma de Barcelona. Departament de Bioquimica i Biologia Molecular) ; Salvatella, Xavier (Institut de Recerca Biomèdica) ; Sancho, Javier (Universidad de Zaragoza. Instituto Universitario de Investigación de Biocomputación y Física de Sistemas Complejos) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
α-Synuclein (α-Syn) forms toxic intracellular protein inclusions and transmissible amyloid structures in Parkinson's disease (PD). Preventing α-Syn self-assembly has become one of the most promising approaches in the search for disease-modifying treatments for this neurodegenerative disorder. [...]
2019 - 10.3389/fnmol.2019.00306
Frontiers in molecular neuroscience, Vol. 12 (Dec. 2019) , art. 306  
3.
20 p, 6.2 MB Computational assessment of bacterial protein structures indicates a selection against aggregation / Carija, Anita (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pinheiro, Francisca (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
The aggregation of proteins compromises cell fitness, either because it titrates functional proteins into non-productive inclusions or because it results in the formation of toxic assemblies. Accordingly, computational proteome-wide analyses suggest that prevention of aggregation upon misfolding plays a key role in sequence evolution. [...]
2019 - 10.3390/cells8080856
Cells, Vol. 8 (2019) , p. 1-20  
4.
13 p, 1.1 MB Protein aggregation into insoluble deposits protects from oxidative stress / Carija, Anita (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro Cantero, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biomedicina Molecular) ; Sánchez de Groot, Natalia (Centre de Regulació Genòmica) ; Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Protein misfolding and aggregation have been associated with the onset of neurodegenerative disorders. Recent studies demonstrate that the aggregation process can result in a high diversity of protein conformational states, however the identity of the specific species responsible for the cellular damage is still unclear. [...]
2017 - 10.1016/j.redox.2017.03.027
Redox biology, Vol. 12 (Aug. 2017) , p. 699-711  
5.
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 (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biomedicina 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 Biologia Molecular) ; Outeiro, Tiago F. (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  
6.
5 p, 351.1 KB Data on correlation between Aβ42 structural aggregation propensity and toxicity in bacteria / Carija, Anita (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Protein aggregation and amyloid formation is a hallmark of an increasing number of human disorders. Because protein aggregation is deleterious for the cell physiology and results in a decrease in overall cell fitness, it is thought that natural selection acts to purify aggregating proteins during evolution. [...]
2016 - 10.1016/j.dib.2016.02.017
Data in brief, Vol. 7 (february 2016) , p. 143-147  

Documentos de investigación Encontrados 1 registros  
1.
168 p, 8.7 MB A Multidisciplinary insight into the determinants of protein aggregation / Čarija, Anita, autor. ; Ventura Zamora, Salvador, supervisor acadèmic. ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
Els trastorns neurodegeneratius crònics, condicions mèdiques que afecten a la població principalment a la seva darrera etapa de vida, representen un problema molt important a la societat moderna. Per això, trobar nous mètodes de diagnòstic i teràpies per tractar aquestes patologies representa un objectiu que cada vegada es presenta com més urgent. [...]
Chronic neurodegenerative disorders, the medical conditions that strike primarily mid- to late-life population, represent a major issue of modern society. Therefore, finding new diagnostic and therapeutic approaches to treat these disorders is a goal of increasing urgency. [...]

[Bellaterra] : Universitat Autònoma de Barcelona, 2018.  

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