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10 p, 1.3 MB |
Characterization of Amyloid Cores in Prion Domains
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Sant'Anna, Ricardo (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
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, Susana (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
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2.
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17 p, 3.4 MB |
Protein environment : A crucial triggering factor in josephin domain aggregation: The role of 2,2,2-trifluoroethanol
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Visentin, Cristina (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Grasso, Gianvito (Università della Svizzera italiana. Istituto Dalle Molle di Studi sull'Intelligenza Artificiale (IDSIA)) ;
Regonesi, Maria Elena (Università di Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ;
Deriu, Marco Agostino (Università della Svizzera italiana. Istituto Dalle Molle di Studi sull'Intelligenza Artificiale (IDSIA)) ;
Tortora, Paolo (Università di Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
The protein ataxin-3 contains a polyglutamine stretch that triggers amyloid aggregation when it is expanded beyond a critical threshold. This results in the onset of the spinocerebellar ataxia type 3. [...]
2018 - 10.3390/ijms19082151
International Journal of Molecular Sciences, Vol. 19, Núm. 8 (August 2018) , art. 2151
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3.
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13 p, 2.6 MB |
The disordered C-terminus of yeast hsf1 contains a cryptic low-complexity amyloidogenic region
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Pujols, Jordi (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Santos Suárez, Jaime (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Universitat Autònoma de Barcelona.
Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí"
Response mechanisms to external stress rely on networks of proteins able to activate specific signaling pathways to ensure the maintenance of cell proteostasis. Many of the proteins mediating this kind of response contain intrinsically disordered regions, which lack a defined structure, but still are able to interact with a wide range of clients that modulate the protein function. [...]
2018 - 10.3390/ijms19051384
International Journal of Molecular Sciences, Vol. 19, Núm. 5 (May 2018) , p. 1384
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4.
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3 p, 438.3 KB |
Proteïnes prions ajuden els bacteris a sobreviure
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Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Els prions s'han associat tradicionalment amb greus malalties neurològiques, però aquestes proteïnes, en la seva forma funcional, també poden ser beneficioses pels organismes que els porten. Investigadors del Departament de Bioquímica i Biologia Molecular de la UAB han identificat recentment el primer prió en un bacteri en un estudi realitzat amb tècniques d'anàlisi computacional. [...]
2017
UAB divulga, Desembre 2017, p. 1-3
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5.
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10 p, 1.2 MB |
A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation
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Marinelli, Patrizia (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Graña Montes, Ricardo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Bañó-Polo, Manuel (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Fernández Gallegos, Ma. Rosario (María Rosario) (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Papaleo, Elena (Kræftens Bekæmpelse) ;
Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Oxidatively modified forms of proteins accumulate during aging. Oxidized protein conformers might act as intermediates in the formation of amyloids in age-related disorders. However, it is not known whether this amyloidogenic conversion requires an extensive protein oxidative damage or it can be promoted just by a discrete, localized post-translational modification of certain residues. [...]
2017 - 10.1016/j.redox.2017.10.022
Redox Biology, Vol. 14 (April 2018) , p. 566-575
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4 p, 393.4 KB |
Copper(II) and the pathological H50Q α-synuclein mutant : environment meets genetics
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Villar-Piqué, Anna (University Medical Centre Göottingen. Department of Neurodegeneration and Restorative Research) ;
Rossetti, Giulia (Jülich Forschungszentrum. Institut für Neurowissenschaften und Medizin) ;
Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Carloni, Paolo (Jülich Forschungszentrum. Institut für Neurowissenschaften und Medizin) ;
Fernández, Claudio O. (Max Planck Laboratory for Structural Biology, Chemistry and Molecular Biophysics of Rosario) ;
Outeiro, Tiago Fleming (University Medical Centre Göottingen. Department of Neurodegeneration and Restorative Research) ;
Universitat Autònoma de Barcelona.
Departament de Bioquímica i Biologia Molecular
Copper is one of the metals described to bind the Parkinson disease-related protein α-synuclein (aSyn), and to promote its aggregation. Although histidine at position 50 in the aSyn sequence is one of the most studied copper-anchoring sites, its precise role in copper binding and aSyn aggregation is still unclear. [...]
2017 - 10.1080/19420889.2016.1270484
Communicative & integrative Biology, Vol. 10, no. 1 (2017) , e127048
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8.
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12 p, 12.3 MB |
High-throughput screening methodology to identify alpha-synuclein aggregation inhibitors
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Pujols, Jordi (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Peña Díaz, Samuel (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Conde-Giménez, María (Universidad de Zaragoza. Instituto Universitario de Investigación de Biocomputación y Física de Sistemas Complejos) ;
Pinheiro, Francisca (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Sancho, Javier (Universidad de Zaragoza. Instituto Universitario de Investigación de Biocomputación y Física de Sistemas Complejos) ;
Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
An increasing number of neurodegenerative diseases are being found to be associated with the abnormal accumulation of aggregated proteins in the brain. In Parkinson's disease, this process involves the aggregation of alpha-synuclein (α-syn) into intraneuronal inclusions. [...]
2017 - 10.3390/ijms18030478
International journal of molecular sciences, Vol. 18 (March 2017) , art. 478
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9.
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2 p, 47.1 KB |
DisProt 7.0 : a major update of the database of disordered proteins
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Piovesan, Damiano (Università di Padova. Dipartimento di Scienze Biomediche) ;
Tabaro, Francesco (Università di Padova. Dipartimento di Scienze Biomediche) ;
Mičetić, Ivan (Università di Padova. Dipartimento di Scienze Biomediche) ;
Necci, Marco (Università di Padova. Dipartimento di Scienze Biomediche) ;
Quaglia, Federica (Università di Padova. Dipartimento di Scienze Biomediche) ;
Oldfield, Christopher J. (Indiana University School of Medicine) ;
Aspromonte, Maria Cristina (Università di Padova. Dipartimento di Salute della Donna e del Bambino) ;
Davey, Norman E. (Conway Institute of Biomolecular & Biomedical Research) ;
Davidović, Radoslav (Univerzitet u Beogradu. Vinca Institut za Nuklearne Nauke) ;
Dosztányi, Zsuzsanna (Magyar Tudományos Akadémia) ;
Elofsson, Arne (Stockholms universitet) ;
Gasparini, Alessandra (Università di Padova. Dipartimento di Salute della Donna e del Bambino) ;
Hatos, András (Università di Padova. Dipartimento di Scienze Biomediche) ;
Kajava, Andrey V. (Université Montpellier) ;
Kalmar, Lajos (University of Cambridge. Department of Veterinary Medicine) ;
Leonardi, Emanuela (Università di Padova. Dipartimento di Salute della Donna e del Bambino) ;
Lazar, Tamas (Vlaams Instituut voor Biotechnologie) ;
Macedo-Ribeiro, Sandra (Universidade do Porto) ;
Macossay-Castillo, Mauricio (Vlaams Instituut voor Biotechnologie) ;
Meszaros, Attila (Magyar Tudományos Akadémia) ;
Minervini, Giovanni (Università di Padova. Dipartimento di Scienze Biomediche) ;
Murvai, Nikoletta (Magyar Tudományos Akadémia) ;
Pujols, Jordi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Roche, Daniel B. (Université Montpellier) ;
Salladini, Edoardo (Université d'Aix-Marseille) ;
Schad, Eva (Magyar Tudományos Akadémia) ;
Schramm, Antoine (Université d'Aix-Marseille) ;
Szabo, Beata (Magyar Tudományos Akadémia) ;
Tantos, Agnes (Magyar Tudományos Akadémia) ;
Tonello, Fiorella (CNR Institute of Neurosceince, I-35121 Padova, Italy) ;
Tsirigos, Konstantinos D. (Stockholms universitet) ;
Veljković, Nevena (Univerzitet u Beogradu. Vinca Institut za Nuklearne Nauke) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Vranken, Wim (Interuniversity Institute of Bioinformatics in Brussels) ;
Warholm, Per (Stockholms universitet) ;
Uversky, Vladimir N. (University of South Florida. Department of Molecular Medicine) ;
Dunker, A. Keith (Indiana University School of Medicine) ;
Longhi, Sonia (Université d'Aix-Marseille) ;
Tompa, Peter (Vlaams Instituut voor Biotechnologie) ;
Tosatto, Silvio C.E. (Università di Padova. Dipartimento di Scienze Biomediche)
2016 - 10.1093/nar/gkw1279
Nucleic acids research, Vol. 45 (Dec. 2017) , D1123-D1124
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10.
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15 p, 4.8 MB |
The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation
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Lázaro, Diana F. (Universitätsmedizin Göttingen) ;
Dias, Mariana Castro (Universitätsmedizin Göttingen) ;
Carija, Anita (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biomedicina Molecular) ;
Madaleno, Carolina Silva (Universidade Nova de Lisboa. Centro de Estudos de Doenças Crónicas) ;
Tenreiro, Sandra (Universidade Nova de Lisboa. Centro de Estudos de Doenças Crónicas) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Outeiro, Tiago F. (Max-Planck-Gesellschaft)
α-synuclein (aSyn) is associated with both sporadic and familial forms of Parkinson's disease (PD), the second most common neurodegenerative disorder after Alzheimer's disease. In particular, multiplications and point mutations in the gene encoding for aSyn cause familial forms of PD. [...]
2016 - 10.1186/s40478-016-0402-8
Acta neuropathologica communications, Vol. 4 (2016) , art. 128
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