Resultados globales: 35 registros encontrados en 0.02 segundos.
Artículos, Encontrados 31 registros
Documentos de investigación, Encontrados 4 registros
Artículos Encontrados 31 registros  1 - 10siguientefinal  ir al registro:
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.
3 p, 161.8 KB Editorial : protein solubility and aggregation in bacteria / Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
The Editorial on the research topic protein solubility and aggregation in bacteria.
2016 - 10.3389/fmicb.2016.01178
Frontiers in microbiology, Vol. 7 (July 2016) , art. 1178  
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.
13 p, 5.2 MB Discovering putative prion-like proteins in Plasmodium falciparum : a computational and experimental analysis / Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Sánchez de Groot, Natalia (Centre de Regulació Genòmica) ; Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sant'Anna, Ricardo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Biosca, Arnau (Institut de Bioenginyeria de Catalunya) ; Fernàndez Busquets, Xavier (Institut de Bioenginyeria de Catalunya) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Prions are a singular subset of proteins able to switch between a soluble conformation and a self-perpetuating amyloid state. Traditionally associated with neurodegenerative diseases, increasing evidence indicates that organisms exploit prion-like mechanisms for beneficial purposes. [...]
2018 - 10.3389/fmicb.2018.01737
Frontiers in microbiology, Vol. 9 (Aug. 2018) , art. 1737  
5.
12 p, 1.6 MB The rho termination factor of Clostridium botulinum contains a prion-like domain with a highly amyloidogenic core / Pallarès i Goitiz, Irantzu (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)
Prion-like proteins can switch between a soluble intrinsically disordered conformation and a highly ordered amyloid assembly. This conformational promiscuity is encoded in specific sequence regions, known as prion domains (PrDs). [...]
2016 - 10.3389/fmicb.2015.01516
Frontiers in microbiology, Vol. 6 (Jan. 2016) , art. 1516  
6.
16 p, 3.8 MB Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria / Macedo, Bruno (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sant'Anna, Ricardo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro Cantero, Susanna (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Cordeiro, Yraima (Universidade Federal do Rio de Janeiro. Faculdade de Farmácia) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Background: An increasing number of proteins are being shown to assemble into amyloid structures that lead to pathological states. Among them, mammalian prions outstand due to their ability to transmit the pathogenic conformation, becoming thus infectious. [...]
2015 - 10.1186/s12934-015-0361-y
Microbial cell factories, Vol. 14 (2015) , art. 174  
7.
13 p, 7.9 MB Computational analysis of candidate prion-like proteins in bacteria and their role / Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sánchez de Groot, Natalia (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Prion proteins were initially associated with diseases such as Creutzfeldt Jakob and transmissible spongiform encephalopathies. However, deeper research revealed them as versatile tools, exploited by the cells to execute fascinating functions, acting as epigenetic elements or building membrane free compartments in eukaryotes. [...]
2015 - 10.3389/fmicb.2015.01123
Frontiers in microbiology, Vol. 6 (Oct. 2015) , art. 1123  
8.
17 p, 651.1 KB Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains / Espinosa Angarica, Vladimir (Universidad de Zaragoza. Departamento de Bioquímica y Biología Molecular y Celular) ; Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sancho, Javier (Universidad de Zaragoza. Departamento de Bioquímica y Biología Molecular y Celular) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
Background: prion proteins conform a special class among amyloids due to their ability to transmit aggregative folds. Prions are known to act as infectious agents in neurodegenerative diseases in animals, or as key elements in transcription and translation processes in yeast. [...]
2013 - 10.1186/1471-2164-14-316
BMC genomics, Vol. 14 (2013) , art. 316  
9.
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  
10.
12 p, 4.2 MB In silico characterization of human prion-like proteins : beyond neurological diseases / Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Paladin, Lisanna (Università di Padua. Dipartimento di Scienze Biomediche) ; Juan Blanco, Teresa (Institut de Recerca Biomèdica) ; Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Aloy, Patrick (Institució Catalana de Recerca i Estudis Avançats (ICREA)) ; Tosatto, Silvio C.E. (Università di Padua. Dipartimento di Scienze Biomediche) ; Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammalian neurodegenerative diseases. However, a growing body of evidence suggests that this mechanism could be behind the regulation of processes such as transcription and translation in multiple species. [...]
2019 - 10.3389/fphys.2019.00314
Frontiers in physiology, Vol. 10 (March 2019) , art. 314  

Artículos : Encontrados 31 registros   1 - 10siguientefinal  ir al registro:
Documentos de investigación Encontrados 4 registros  
1.
1 p, 10.8 MB Deciphering hIAPP : a novel way to cure diabetes / Ruiz López, Iñigo ; Pallarés 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.
1 p, 410.9 KB DJ-1, a possible therapeutic target against Parkinson's disease / Oliva Vilarnau, Núria ; Yuste Mateos, Víctor J., (Víctor José), dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Universitat Autònoma de Barcelona. Facultat de Biociències
2015
Grau en Biotecnologia [815]  
3.
171 p, 3.7 MB Analysis of different evolutionary strategies to prevent protein aggregation / Graña Montes, Ricardo ; Ventura, Salvador, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
En els darrers 15 anys, l'estudi de l'agregació de proteïnes ha evolucionat de ser una part de la química de proteïnes que tradicionalment generava poc interès, a convertir-se en una àrea d'investigació dinàmica que ha ampliat el seu abast a diferents camps de recerca incloenthi la bioquímica, la biotecnologia, la nanotecnologia y la biomedicina. [...]
In the last 15 years, the study of protein aggregation has evolved from a mostly neglected topic of protein chemistry to a highly dynamic research area which has expanded its implications through different fields including biochemistry, biotechnology, nanotechnology and biomedicine. [...]

[Barcelona] : Universitat Autònoma de Barcelona, 2014  
4.
199 p, 6.0 MB Characterization of intracellular protein aggregates / Villar i Piqué, Anna ; Ventura, Salvador, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
Durant les últimes dècades, l'agregació de proteïnes ha esdevingut un tema d'investigació molt dinàmic que s'estén transversalment per diferents camps de recerca, incloent la bioquímica, la biotecnologia, la biomedicina i la nanotecnologia. [...]
During the last decades, protein aggregation has become a dynamic research topic extending across distinct investigation fields, including biochemistry, biotechnology, biomedicine and nanotechnology. [...]

[Barcelona] : Universitat Autònoma de Barcelona, 2013  

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