Results overview: Found 17 records in 0.01 seconds.
Articles, 15 records found
Research literature, 1 records found
Course materials, 1 records found
Articles 15 records found  1 - 10next  jump to record:
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.
12 p, 5.4 MB The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers / Taglialegna, Agustina (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Agrobiotecnología) ; Matilla-Cuenca, Leticia (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Agrobiotecnología) ; Dorado-Morales, Pedro (Universidad Pública de Navarra. Departamento de Salud) ; 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) ; Garnett, James A. (Centre for Host Microbiome Interactions. Dental institute. King's College London) ; Lasa, Iñigo (Universidad Pública de Navarra. Departamento de Salud) ; Valle, Jaione (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Agrobiotecnología)
Functional amyloids are considered as common building block structures of the biofilm matrix in different bacteria. In previous work, we have shown that the staphylococcal surface protein Bap, a member of the Biofilm-Associated Proteins (BAP) family, is processed and the fragments containing the N-terminal region become aggregation-prone and self-assemble into amyloid-like structures. [...]
2020 - 10.1038/s41522-020-0125-2
npj biofilms and microbiomes, Vol. 6, issue 1 (2020) , art. 15  
3.
34 p, 4.2 MB Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals / Taglialegna, Agustina (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Agrobiotecnología) ; 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) ; Garnett, James A. (Queen Mary University of London. School of Biological and Chemical Sciences) ; Matthews, Steve (Imperial College London. Department of Life Sciences) ; Penades, José R. (University of Glasgow. College of Medical, Veterinary and Life Sciences) ; Lasa, Iñigo (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Agrobiotecnología) ; Valle, Jaione (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Agrobiotecnología)
Biofilms are communities of bacteria that grow encased in an extracellular matrix that often contains proteins. The spatial organization and the molecular interactions between matrix scaffold proteins remain in most cases largely unknown. [...]
2016 - 10.1371/journal.ppat.1005711
PLoS pathogens, Vol. 12, issue 6 (June 2016) , p. e1005711  
4.
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  
5.
13 p, 4.4 MB Dissecting the contribution of Staphylococcus aureus α-phenol-soluble modulins to biofilm amyloid structure / Marinelli, Patrizia (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Navarro Cantero, Susanna (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
The opportunistic pathogen Staphylococcus aureus is recognized as one of the most frequent causes of biofilm-associated infections. The recently discovered phenol soluble modulins (PSMs) are small α-helical amphipathic peptides that act as the main molecular effectors of staphylococcal biofilm maturation, promoting the formation of an extracellular fibril structure with amyloid-like properties. [...]
2016 - 10.1038/srep34552
Scientific reports, Vol. 6 (2016) , art. 34552  
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.
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.
11 p, 2.1 MB Aggregation propensity of neuronal receptors : potential implications in neurodegenerative disorders / Navarro Cantero, Susanna (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Diaz-Caballero, Marta (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Illa, Ricard (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biomedicina Molecular) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Misfolding and aggregation of proteins in tissues is linked to the onset of a diverse set of human neurodegenerative disorders, including Alzheimer's and Parkinson's diseases. In these pathologies proteins usually aggregate into highly ordered and β-sheet enriched amyloid fibrils. [...]
2015 - 10.4155/fso.15.39
Future science OA, Vol. 1, issue 2 (2015) , art. FSO39  
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.
10 p, 1.3 MB Characterization of Amyloid Cores in Prion Domains / Sant'Anna, Ricardo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Fernández Gallegos, Ma. Rosario (María Rosario) (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Batlle Carreras, Cristina (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Navarro Cantero, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Sánchez de Groot, Natalia (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Serpell, Louise (University of Sussex. School of Life Sciences) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Amyloids consist of repetitions of a specific polypeptide chain in a regular cross-β-sheet conformation. Amyloid propensity is largely determined by the protein sequence, the aggregation process being nucleated by specific and short segments. [...]
2016 - 10.1038/srep34274
Scientific reports, Vol. 6 (2016) , art. 34274  

Articles : 15 records found   1 - 10next  jump to record:
Research literature 1 records found  
1.
215 p, 7.5 MB From sequence to structure : determinants of functional and non-functional protein aggregation / Marinelli, Patrizia ; Ventura, Salvador, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Navarro Cantero, Susanna, dir (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
El estudio de la agregación proteica representa un campo de investigación desafiante que abarca tanto el área biomédica como la biotecnológica. El creciente número de enfermedades humanas asociadas a la acumulación de agregados amiloides, así como la formación de depósitos intracelulares durante la producción recombinante de proteínas terapéuticas en modelos celulares ha impulsado la investigación para comprender y desarrollar estrategias contra la agregación de proteínas. [...]
The study of protein aggregation represents a challenging research field which embraces from biomedical to biotechnological areas. The growing number of human diseases associated to the deposition of amyloid aggregates as well as the formation of intracellular protein deposits during the recombinant production of therapeutic proteins in cell factories has pushed the research to understand and develop strategies against protein aggregation. [...]

Bellaterra : Universitat Autònoma de Barcelona, 2015  

Course materials 1 records found  
1.
4 p, 28.4 KB Bioquímica dels teixits [20166] / Arús i Caraltó, Carles ; Navarro Cantero, Susanna ; Universitat Autònoma de Barcelona. Facultat de Biociències
2007-08
Llicenciat en Bioquímica [477]  

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