Resultados globales: 7 registros encontrados en 0.02 segundos.
Artículos, Encontrados 6 registros
Documentos de investigación, Encontrados 1 registros
Artículos Encontrados 6 registros  
1.
7 p, 1.8 MB PrionW : a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores / Zambrano, Rafael (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Conchillo-Solé, Óscar (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Illa, Ricard (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biomedicina Molecular) ; Rousseau, Frederic (KU Leuven. Department for Cellular and Molecular Medicine) ; Schymkowitz, Joost (KU Leuven. Department for Cellular and Molecular Medicine) ; Sabate, Raimon (Universitat de Barcelona. Departament de Fisicoquímica) ; Daura i Ribera, Xavier (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura i Zamora, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Prions are a particular type of amyloids with the ability to self-perpetuate and propagate in vivo. Prion-like conversion underlies important biological processes but is also connected to human disease. [...]
2015 - 10.1093/nar/gkv490
Nucleic acids research, Vol. 43 (2015) , Web Server issue W331–W337  
2.
9 p, 627.3 KB What makes a protein sequence a prion ? / Sabaté, Raimon (Universitat de Barcelona. Departament de Fisicoquímica) ; Rousseau, Frederic (KU Leuven. Department for Cellular and Molecular Medicine) ; Schymkowitz, Joost (KU Leuven. Departement for Cellular and Molecular Medicine) ; Ventura i Zamora, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Typical amyloid diseases such as Alzheimer's and Parkinson's were thought to exclusively result from de novo aggregation, but recently it was shown that amyloids formed in one cell can cross-seed aggregation in other cells, following a prion-like mechanism. [...]
2015 - 10.1371/journal.pcbi.1004013
PLoS computational biology, Vol. 11, Issue 1 (Jan. 2015) , art. e1004013  
3.
10 p, 5.7 MB Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion / Sabaté, Raimon (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ventura i Zamora, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecularar) ; Espargaró Colomé, Alba (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Saupe, Sven J. (Université Victor Segalen. Laboratoire de Génétique Moléculaire des Champignons (Burdeus, França))
The formation of amyloid aggregates is related to the onset of a number of human diseases. Recent studies provide compelling evidence for the existence of related fibrillar structures in bacterial inclusion bodies (IBs). [...]
2009 - 10.1186/1475-2859-8-56
Microbial cell factories, Vol. 8, N. 56 (October 2009) , p. 1-10  
4.
11 p, 1.6 MB Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors / Villar Piqué, Anna (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ventura i Zamora, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Espargaró Colomé, Alba (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sabaté, Raimon (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sánchez de Groot, Natalia (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Background: The amyloid-β peptide (Aβ42) is the main component of the inter-neuronal amyloid plaques characteristic of Alzheimer's disease (AD). The mechanism by which Aβ42 and other amyloid peptides assemble into insoluble neurotoxic deposits is still not completely understood and multiple factors have been reported to trigger their formation. [...]
2012 - 10.1186/1475-2859-11-55
Microbial cell factories, Vol. 11, N. 55 (May 2012) , p. 1-11  
5.
12 p, 2.5 MB Yeast prions form infectious amyloid inclusion bodies in bacteria / Espargaró Colomé, Alba (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura i Zamora, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Villar Piqué, Anna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Sabaté, Raimon (Universitat de Barcelona. Departament de Fisicoquímica)
Background: Prions were first identified as infectious proteins associated with fatal brain diseases in mammals. However, fungal prions behave as epigenetic regulators that can alter a range of cellular processes. [...]
2012 - 10.1186/1475-2859-11-89
Microbial cell factories, Vol. 11, N. 89 (June 2012) , p. 1-12
2 documentos
6.
9 p, 6.8 MB Amyloid-like protein inclusions in tobacco transgenic plants / Villar-Piqué, Anna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Sabaté Lagunas, Raimon (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Lopera Ortega, Oriol (Centre de Recerca en Agrigenòmica) ; Gibert Amat, Jordi (Centre de Recerca en Agrigenòmica) ; Torné, Josep M. (Centre de Recerca en Agrigenòmica) ; Santos, Mireya (Centre de Recerca en Agrigenòmica) ; Ventura Zamora, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
The formation of insoluble protein deposits in human tissues is linked to the onset of more than 40 different disorders, ranging from dementia to diabetes. In these diseases, the proteins usually self-assemble into ordered β-sheet enriched aggregates known as amyloid fibrils. [...]
2010 - 10.1371/journal.pone.0013625
PLoS one, Vol. 5, Issue 10 (October 2010) , p. e13625  

Documentos de investigación Encontrados 1 registros  
1.
182 p, 7.8 MB Modelos proteicos para el estudio de la agregación amiloide in vitro e in vivo / Espargaró Colomé, Alba ; Ventura Pedret, Salvador, dir. ; Sabaté Lagunas, Raimon, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular
Durante los últimos años la agregación proteica se ha convertido en un tema de elevada importancia en biología, biotecnología y medicina. Un número creciente de evidencias demuestran fehacientemente que el mal plegamiento de proteínas y su agregación, muchas veces en forma de fibras amiloides, conlleva la formación de depósitos celulares insolubles que son los responsables finales de un creciente número de enfermedades humanas. [...]
In recent years, protein aggregation has become a topic of great importance in biology, biotechnology and medicine areas. A growing body of evidences show conclusively that the protein misfolding and aggregation, often in the form of amyloid fibrils, leading to the formation of insoluble cellular deposits that are ultimately responsible for an increasing number of human diseases. [...]

[Barcelona] : Universitat Autònoma de Barcelona, 2013  

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5 Sabaté, Raimon
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