Resultados globales: 20 registros encontrados en 0.02 segundos.
Artículos, Encontrados 14 registros
Documentos de investigación, Encontrados 6 registros
Artículos Encontrados 14 registros  1 - 10siguiente  ir al registro:
1.
18 p, 3.6 MB hnRNPDL phase separation is regulated by alternative splicing and disease-causing mutations accelerate its aggregation / Batlle Carreras, Cristina (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Yang, Peiguo (St. Jude Children's Research Hospital. Department of Cell and Molecular Biology) ; Coughlin, Maura (St. Jude Children's Research Hospital. Department of Cell and Molecular Biology) ; Messing, James (Howard Hughes Medical Institute) ; Pesarrodona Roches, Mireia (Institut de Recerca Biomèdica) ; Szulc, Elzbieta (Institut de Recerca Biomèdica) ; Salvatella, Xavier (Institut de Recerca Biomèdica) ; Kim, Hong Joo (St. Jude Children's Research Hospital. Department of Cell and Molecular Biology) ; Taylor, J. Paul (Howard Hughes Medical Institute) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Prion-like proteins form multivalent assemblies and phase separate into membraneless organelles. Heterogeneous ribonucleoprotein D-like (hnRNPDL) is a RNA-processing prion-like protein with three alternative splicing (AS) isoforms, which lack none, one, or both of its two disordered domains. [...]
2020 - 10.1016/j.celrep.2019.12.080
Cell reports, Vol. 30, issue 4 (Jan. 2020) , p. 1117-1128  
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.
16 p, 9.5 MB Characterization of Soft Amyloid Cores in Human Prion-Like Proteins / Batlle Carreras, Cristina (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sánchez de Groot, Natalia (Centre de Regulació Genòmica) ; Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro Cantero, Susanna (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Prion-like behaviour is attracting much attention due to the growing evidences that amyloid-like self-assembly may reach beyond neurodegeneration and be a conserved functional mechanism. The best characterized functional prions correspond to a subset of yeast proteins involved in translation or transcription. [...]
2017 - 10.1038/s41598-017-09714-z
Scientific reports, Vol. 7 (2017) , art. 12134  
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.
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  
7.
14 p, 3.5 MB The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria / Navarro Cantero, Susanna (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Marinelli, Patrizia (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Diaz-Caballero, Marta (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Background: rhe formation of protein inclusions is connected to the onset of many human diseases. Human RNA binding proteins containing intrinsically disordered regions with an amino acid composition resembling those of yeast prion domains, like TDP-43 or FUS, are being found to aggregate in different neurodegenerative disorders. [...]
2015 - 10.1186/s12934-015-0284-7
Microbial cell factories, Vol. 14 (2015) , art. 102  
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, 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  
10.
33 p, 2.7 MB Development of a new largely scalable in vitro prion propagation method for the production of infectious recombinant prions for high resolution structural studies / Eraña, Hasier (ATLAS Molecular Pharma S. L.) ; Charco, Jorge M. (CIC bioGUNE) ; Di Bari, Michele Angelo (CIC bioGUNE) ; Díaz-Domínguez, Carlos M. (Istituto Superiore di Sanità. Department of Veterinary Public Health and Food Safety.) ; López-Moreno, R. (CIC bioGUNE) ; Vidal, Enric (Universitat Autònoma de Barcelona. Centre de Recerca en Sanitat Animal (CReSA)) ; González-Miranda, E. (CIC bioGUNE) ; Pérez-Castro, Miguel A. (CIC bioGUNE) ; García-Martínez, Sandra (ATLAS Molecular Pharma S. L.) ; Bravo, Susana Belén (Proteomics Lab. IDIS) ; Fernández-Borges, N. (CIC bioGUNE) ; Geijo, Maria V. (NEIKER-Instituto Vasco de Investigación y Desarrollo Agrario) ; D'Agostino, C. (Department of Veterinary Public Health and Food Safety. Istituto Superiore di Sanità) ; Garrido, J. (NEIKER-Instituto Vasco de Investigación y Desarrollo Agrario) ; Bian, J. (Colorado State University. Prion Research Center (PRC).) ; König, A. (Heinrich-Heine-Universität Düsseldorf. Physikalische Biologie.) ; Uluca-Yazgi, B. (Heinrich-Heine-Universität Düsseldorf. Physikalische Biologie.) ; Sabate, R. (Universitat de Barcelona. Institute of Nanoscience and Nanotechnology (IN2UB).) ; Khaychuk, V. (Colorado State University. Prion Research Center (PRC).) ; Vanni, Ilaria (Istituto Superiore di Sanità. Department of Veterinary Public Health and Food Safety.) ; Telling, G.C. (Colorado State University. Prion Research Center (PRC).) ; Heise, Henrike (Heinrich-Heine-Universität Düsseldorf. Physikalische Biologie.) ; Nonno, Romolo (Istituto Superiore di Sanità. Department of Veterinary Public Health and Food Safety.) ; Requena, J.R. (Universidad de Santiago de Compostela. CIMUS Biomedical Research Institute.) ; Castilla, Joaquín (IKERBasque. Basque Foundation for Science)
The resolution of the three-dimensional structure of infectious prions at the atomic level is pivotal to understand the pathobiology of Transmissible Spongiform Encephalopathies (TSE), but has been long hindered due to certain particularities of these proteinaceous pathogens. [...]
2019 - 10.1371/journal.ppat.1008117
PLoS pathogens, Vol. 15 Núm. 10 (2019) , p. e1008117  

Artículos : Encontrados 14 registros   1 - 10siguiente  ir al registro:
Documentos de investigación Encontrados 6 registros  
1.
1 p, 1.3 MB Immunology of prion neuroinvasion : importance of secondary lymphoid organs in the early stages / Bayó Llorens, Cristina ; Villaverde Corrales, Antonio, dir. (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ; Universitat Autònoma de Barcelona. Facultat de Biociències
2017
Grau en Microbiologia [816]  
2.
1 p, 3.6 MB Prion-like proteins, phase separation and neurodegenerative disorders / Gil García, Marcos ; Ventura, Salvador, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Facultat de Biociències
2016
Grau en Bioquímica [814]  
3.
1 p, 1.3 MB New proteins with prion-like domains involved in neurodegenerative disease / Domingo Pelegrin, Marina ; Ventura, Salvador, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Facultat de Biociències
2014
Grau en Bioquímica [814]  
4.
1 p, 2.5 MB Identification of new neurodegenerative diseases / Diaz-Caballero, Marta ; Ventura, Salvador, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Facultat de Biociències
2014
Grau en Bioquímica [814]  
5.
1 p, 3.8 MB Finding proteins with prion-like domains and their involvement in neurodegenerative diseases : FUS and HNRNPD / Carmona Ule, Nuria ; Ventura, Salvador, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Facultat de Biociències
2014
Grau en Biotecnologia [815]  
6.
1 p, 1.6 MB The role of prion-like proteins in human diseases : TAF15 and HNRPDL / Ventura Molina, Júlia ; Ventura, Salvador, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Facultat de Biociències
2014
Grau en Biotecnologia [815]  

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