Resultats globals: 61 registres trobats en 0.11 segons.
Articles, 54 registres trobats
Contribucions a jornades i congressos, 1 registres trobats
Documents de recerca, 6 registres trobats
Articles 54 registres trobats  1 - 10següentfinal  anar al registre:
1.
15 p, 2.9 MB MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation / Batlle Carreras, Cristina (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Calvo, Isabel (Institut de Ciència i Tecnologia de Barcelona. Institut de Recerca en Biomedicina) ; Iglesias, Valentin (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; J. Lynch, Cian (Institut de Ciència i Tecnologia de Barcelona. Institut de Recerca en Biomedicina) ; Gil-Garcia, Marcos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Serrano, Manuel (Institut de Ciència i Tecnologia de Barcelona. Institut de Recerca en Biomedicina) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
A disordered to β-sheet transition was thought to drive the functional switch of Q/N-rich prions, similar to pathogenic amyloids. However, recent evidence indicates a critical role for coiled-coil (CC) regions within yeast prion domains in amyloid formation. [...]
2021 - 10.1038/s42003-021-01930-8
Communications Biology, Vol. 4 (March 2021) , art. 414  
2.
21 p, 5.3 MB Pathological ATX3 Expression Induces Cell Perturbations in E. coli as Revealed by Biochemical and Biophysical Investigations / Ami, Diletta (University of Milano-Bicocca. Department of Biotechnologies and Biosciences) ; Mereghetti, Paolo (Bioinformatics Consultant) ; Falvo, Jacopo (University of Milano-Bicocca. Department of Biotechnologies and Biosciences) ; Catelani, Tiziano (University of Milano-Bicocca. Department of Biotechnologies and Biosciences) ; Visentin, Cristina (Università degli Studi di Milano. Department of Biosciences) ; Tortora, Paolo (University of Milano-Bicocca. Department of Biotechnologies and Biosciences) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Natalello, Antonino (University of Milano-Bicocca. Departament of Biotechnology and Biosciences) ; Regonesi, Maria Elena (Università di Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ; Sciandrone, Barbara (University of Milano-Bicocca. Department of Biotechnologies and Biosciences)
Amyloid aggregation of human ataxin-3 (ATX3) is responsible for spinocerebellar ataxia type 3, which belongs to the class of polyglutamine neurodegenerative disorders. It is widely accepted that the formation of toxic oligomeric species is primarily involved in the onset of the disease. [...]
2021 - 10.3390/ijms22020943
International journal of molecular sciences, Vol. 22, Issue 2 (January 2021) , art. 943  
3.
10 p, 1.3 MB Title : insoluble proteins catch heterologous soluble proteins into inclusion bodies by intermolecular interaction of aggregating peptides / Carratalá, Jose Vicente (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Cisneros, Andrés (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Hellman, Elijah (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ferrer Miralles, Neus (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia
Protein aggregation is a biological event observed in expression systems in which the recombinant protein is produced under stressful conditions surpassing the homeostasis of the protein quality control system. [...]
2021 - 10.1186/s12934-021-01524-3
Microbial cell factories, Vol. 20 (February 2021)  
4.
12 p, 2.4 MB Inhibition of α-synuclein aggregation and mature fibril disassembling with a minimalistic compound, ZPDm / Peña Díaz, Samuel (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pujols, Jordi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pinheiro, Francisca (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Santos, Jaime (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro, Susanna (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Conde Gimenez, María (Universidad de Zaragoza. Instituto Aragonés de Investigaciones Sanitarias) ; García, Jesús (Institut de Recerca Biomèdica de Lleida) ; Salvatella, Xavier (Institució Catalana de Recerca i Estudis Avançats) ; Dalfo Capella, Esther (Universitat Autònoma de Barcelona. Facultat de Medicina) ; Sancho, Javier (Universidad de Zaragoza. Instituto Aragonés de Investigaciones Sanitarias) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
Synucleinopathies are a group of disorders characterized by the accumulation of α-Synuclein amyloid inclusions in the brain. Preventing α-Synuclein aggregation is challenging because of the disordered nature of the protein and the stochastic nature of fibrillogenesis, but, at the same time, it is a promising approach for therapeutic intervention in these pathologies. [...]
2020 - 10.3389/fbioe.2020.588947
Frontiers in Bioengineering and Biotechnology, Vol. 8 (October 2020) , art. 588947  
5.
10 p, 3.4 MB Rational design of small molecules able to inhibit α-synuclein amyloid aggregation for the treatment of Parkinson's disease / Vittorio, Serena (Università degli Studi di Messina Viale Palatucci. Dipartimento di Scienze Chimiche, Biologiche, Farmaceutiche e Ambientali) ; Adornato, Ilenia (Università degli Studi di Messina Viale Palatucci. Dipartimento di Scienze Chimiche, Biologiche, Farmaceutiche e Ambientali) ; Gitto, Rosaria (Università degli Studi di Messina Viale Palatucci. Dipartimento di Scienze Chimiche, Biologiche, Farmaceutiche e Ambientali) ; Peña Díaz, Samuel (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; De Luca, Laura (Università degli Studi di Messina Viale Palatucci. Dipartimento di Scienze Chimiche, Biologiche, Farmaceutiche e Ambientali) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
Parkinson's disease is one of the most common neurodegenerative disorders in elderly age. One of the mechanisms involved in the neurodegeneration appears related to the aggregation of the presynaptic protein alpha synuclein (α-syn) into toxic oligomers and fibrils. [...]
2020 - 10.1080/14756366.2020.1816999
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol. 35, Issue 1 (September 2020) , p. 1727-1735  
6.
11 p, 1.4 MB Computational prediction of protein aggregation : advances in proteomics, conformation-specific algorithms and biotechnological applications / Santos, Jaime (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pujols, Jordi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Iglesias, Valentin (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Protein aggregation is a widespread phenomenon that stems from the establishment of non-native intermolecular contacts resulting in protein precipitation. Despite its deleterious impact on fitness, protein aggregation is a generic property of polypeptide chains, indissociable from protein structure and function. [...]
2020 - 10.1016/j.csbj.2020.05.026
Computational and Structural Biotechnology Journal, Vol. 18 (June 2020) , p. 1403-1413  
7.
15 p, 4.1 MB Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity / Carija, Anita (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pinheiro, Francisca (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pujols, Jordi (Universitat Autònoma de Barcelona. 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, Susanna (Universitat Autònoma de Barcelona. 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  
8.
18 p, 3.6 MB hnRNPDL phase separation is regulated by alternative splicing and disease-causing mutations accelerate its aggregation / Batlle Carreras, Cristina (Universitat Autònoma de Barcelona. 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 de Lleida) ; Szulc, Elzbieta (Institut de Recerca Biomèdica de Lleida) ; Salvatella, Xavier (Institut de Recerca Biomèdica de Lleida) ; 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  
9.
3 p, 161.8 KB Editorial : protein solubility and aggregation in bacteria / Ventura, Salvador (Universitat Autònoma de Barcelona. 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  
10.
13 p, 1.1 MB Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity / Sant'Anna, Ricardo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Gallego Alonso, Pablo (Universitat Autònoma de Barcelona. 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 (Porto, Portugal)) ; Ferreira, Nelson (Instituto de Ciências Biomédicas de Abel Salazar (Porto, Portugal)) ; Pinheiro, Francisca (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Esperante, Sebastián (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Huertas, Oscar (SOM-Biotech) ; Almeida, Maria Rosário (Instituto de Ciências Biomédicas de Abel Salazar (Porto, Portugal)) ; 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  

Articles : 54 registres trobats   1 - 10següentfinal  anar al registre:
Contribucions a jornades i congressos 1 registres trobats  
1.
51 p, 394.4 KB On the measurement of multidimensional poverty in multiple domain contexts / Permanyer, Iñaki
We develop the measurement of multidimensional poverty for the case in which the different dimensions taken into account are partitioned in several domains-an issue with crucial implications for the identification and aggregation of the poor which has been neglected in the literature. [...]
2016
Meeting of the Society for Social Choice and Welfare. Lund (Suècia), 13è : 2016  

Documents de recerca 6 registres trobats  
1.
1 p, 2.4 MB The amyloid state, an unexploited resource / Fornt Suñé, Marc ; Universitat Autònoma de Barcelona. Facultat de Biociències
2020
Grau en Bioquímica [814]  
2.
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]  
3.
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 de Biologia Molecular) ; Universitat Autònoma de Barcelona. Facultat de Biociències
2015
Grau en Biotecnologia [815]  
4.
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  
5.
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  
6.
39 p, 341.1 KB Heterogeneous dynamics, aggregation and the persistence of economic shocks / Mayoral, Laura ; Universitat Autònoma de Barcelona. Unitat de Fonaments de l'Anàlisi Econòmica ; Institut d'Anàlisi Econòmica
It has been recently emphasized that, if individuals have heterogeneous dynamics, estimates of shock persistence based on aggregate data are significatively higher than those derived from its disaggregate counterpart. [...]
2009 (Working papers ; 786.09)  

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