Results overview: Found 6 records in 0.01 seconds.
Articles, 6 records found
Articles 6 records found  
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.
2 p, 509.8 KB Inducing α-synuclein compaction : a new strategy for inhibiting α-synuclein aggregation? / Pinheiro, Francisca (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
2019 - 10.4103/1673-5374.259608
Neural Regeneration Research, Vol. 14, issue 11 (Nov. 2019) , p. 1897-1898  
3.
13 p, 1.1 MB Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity / Sant'Anna, Ricardo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Gallego Alonso, Pablo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Robinson, Lei Z. (Scripps Research Institute) ; Pereira-Henriques, Alda (Instituto de Ciências Biomédicas de Abel Salazar) ; Ferreira, Nelson (Instituto de Ciências Biomédicas de Abel Salazar) ; Pinheiro, Francisca (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Esperante, Sebastián (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Huertas, Oscar (SOM-Biotech) ; Almeida, Maria Rosário (Instituto de Ciências Biomédicas de Abel Salazar) ; Reixach, Natàlia (Scripps Research Institute) ; Insa, Raul (SOM-Biotech) ; Velazquez-Campoy, Adrián (Universidad de Zaragoza. Departamento de Bioquímica y Biología Celular y Molecular) ; Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Reig, Núria (SOM-Biotech) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Transthyretin (TTR) is a plasma homotetrameric protein implicated in fatal systemic amyloidoses. TTR tetramer dissociation precedes pathological TTR aggregation. Native state stabilizers are promising drugs to treat TTR amyloidoses. [...]
2016 - 10.1038/ncomms10787
Nature communications, Vol. 7 (2016) , art. 10787  
4.
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  
5.
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  
6.
12 p, 12.3 MB High-throughput screening methodology to identify alpha-synuclein aggregation inhibitors / Pujols, Jordi (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Peña Díaz, Samuel (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Conde-Giménez, María (Universidad de Zaragoza. Instituto Universitario de Investigación de Biocomputación y Física de Sistemas Complejos) ; Pinheiro, Francisca (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Sancho, Javier (Universidad de Zaragoza. Instituto Universitario de Investigación de Biocomputación y Física de Sistemas Complejos) ; Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
An increasing number of neurodegenerative diseases are being found to be associated with the abnormal accumulation of aggregated proteins in the brain. In Parkinson's disease, this process involves the aggregation of alpha-synuclein (α-syn) into intraneuronal inclusions. [...]
2017 - 10.3390/ijms18030478
International journal of molecular sciences, Vol. 18 (March 2017) , art. 478  

See also: similar author names
2 Pinheiro, F.
1 Pinheiro, Fernanda
1 Pinheiro, Fernanda Paula
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