|
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.
|
|
|
3.
|
|
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
|
|
|
4.
|
|
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
|
|
|
5.
|
|
8 p, 674.6 KB |
DisProt : intrinsic protein disorder annotation in 2020
/
Hatos, Andras (University of Padova. Department of Biomedical Sciences) ;
Hajdu-Soltész, Borbála (MTA-ELTE Lendület Bioinformatics Research Group. Department of Biochemistry. Eötvös Loránd University) ;
Monzon, Alexander M. (Department of Biomedical Sciences. University of Padova) ;
Palopoli, Nicolas (Departamento de Ciencia y Tecnología. Universidad Nacional de Quilmes-CONICET) ;
Álvarez, Lucía (Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Biotecnológicas IIBIO. Universidad Nacional de San Martín) ;
Aykac-Fas, Burcu (Computational Biology Laboratory. Danish Cancer Society Research Center) ;
Bassot, Claudio (Department of Biochemistry and Biophysics and Science for Life Laboratory. Stockholm University. Box 1031) ;
Benítez, Guillermo I. (Departamento de Ciencia y Tecnología. Universidad Nacional de Quilmes-CONICET) ;
Bevilacqua, Martina (Department of Biomedical Sciences. University of Padova) ;
Chasapi, Anastasia (Biological Computation and Process Laboratory. Chemical Process and Energy Resources Institute. Centre for Research and Technology Hellas) ;
Chemes, Lucía (Departamento de Fisiología y Biología Molecular y Celular (DFBMC). Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires) ;
Davey, NormanE. (Division of Cancer Biology. Institute of Cancer Research) ;
Davidović, Radoslav (Laboratory for Bioinformatics and Computational Chemistry. Institute of Nuclear Sciences Vinca. University of Belgrade) ;
Dunker, A. Keith (Center for Computational Biology and Bioinformatics. Indiana University School of Medicine) ;
Elofsson, Arne (Department of Biochemistry and Biophysics and Science for Life Laboratory. Stockholm University. Box 1031) ;
Gobeill, Julien (Swiss Institute of Bioinformatics and HES-SO\HEG) ;
Foutel, Nicolás S.G. (Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Biotecnológicas IIBIO. Universidad Nacional de San Martín) ;
Sudha, Govindarajan (Department of Biochemistry and Biophysics and Science for Life Laboratory. Stockholm University. Box 1031) ;
Guharoy, Mainak (VIB-VUB Center for Structural Biology. Flanders Institute for Biotechnology (VIB)) ;
Horvath, Tamas (Institute of Enzymology. Research Centre for Natural Sciences. Hungarian Academy of Sciences) ;
Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Kajava, Andrey V. (Institut de Biologie Computationnelle(IBC)) ;
Kovacs, Orsolya P. (Institute of Enzymology. Research Centre for Natural Sciences. Hungarian Academy of Sciences) ;
Lamb, John (Department of Biochemistry and Biophysics and Science for Life Laboratory. Stockholm University. Box 1031) ;
Lambrughi, Matteo (Computational Biology Laboratory. Danish Cancer Society Research Center) ;
Lazar, Tamas (VIB-VUB Center for Structural Biology. Flanders Institute for Biotechnology (VIB)) ;
Leclercq, Jeremy Y. (Centre de Recherche en Biologie Cellulaire de Montpellier (CRBM). UMR 5237 CNRS. Université Montpellier) ;
Leonardi, Emanuela (Fondazione Istituto di Ricerca Pediatrica (IRP). Città della Speranza) ;
MacEdo-Ribeiro, Sandra (Instituto de Biologia Molecular e Celular (IBMC). Instituto de Investigação e Inovação em Saúde (i3S). Universidade Do Porto) ;
MacOssay-Castillo, Mauricio (VIB-VUB Center for Structural Biology. Flanders Institute for Biotechnology (VIB)) ;
Maiani, Emiliano (Computational Biology Laboratory. Danish Cancer Society Research Center) ;
Manso, José A. (Instituto de Biologia Molecular e Celular (IBMC). Instituto de Investigação e Inovação em Saúde (i3S). Universidade Do Porto) ;
Marino-Buslje, Cristina (Bioinformatics Unit. Fundación Instituto Leloir) ;
Martínez-Pérez, Elisabeth (Bioinformatics Unit. Fundación Instituto Leloir) ;
Mészáros, Bálint (MTA-ELTE Lendület Bioinformatics Research Group. Department of Biochemistry. Eötvös Loránd University) ;
Mičetić, Ivan (Department of Biomedical Sciences. University of Padova) ;
Minervini, Giovanni (Department of Biomedical Sciences. University of Padova) ;
Murvai, Nikoletta (Institute of Enzymology. Research Centre for Natural Sciences. Hungarian Academy of Sciences) ;
Necci, Marco (Department of Biomedical Sciences. University of Padova) ;
Ouzounis, Christos A. (Biological Computation and Process Laboratory. Chemical Process and Energy Resources Institute. Centre for Research and Technology Hellas) ;
Pajkos, Mátyás (MTA-ELTE Lendület Bioinformatics Research Group. Department of Biochemistry. Eötvös Loránd University) ;
Paladin, Lisanna (Department of Biomedical Sciences. University of Padova) ;
Pancsa, Rita (Institute of Enzymology. Research Centre for Natural Sciences. Hungarian Academy of Sciences) ;
Papaleo, Elena (Translational Disease Systems Biology. Faculty of Health and Medical Sciences. Novo Nordisk Foundation Center. Protein Research University of Copenhagen) ;
Parisi, Gustavo (Departamento de Ciencia y Tecnología. Universidad Nacional de Quilmes-CONICET) ;
Pasche, Emilie (Swiss Institute of Bioinformatics and HES-SO\HEG) ;
Barbosa Pereira, Pedro J. (Instituto de Biologia Molecular e Celular (IBMC). Instituto de Investigação e Inovação em Saúde (i3S). Universidade Do Porto) ;
Promponas, Vasilis J. (Bioinformatics Research Laboratory. Department of Biological Sciences. University of Cyprus) ;
Pujols, Jordi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Quaglia, Federica (Department of Biomedical Sciences. University of Padova) ;
Ruch, Patrick (Swiss Institute of Bioinformatics and HES-SO\HEG) ;
Salvatore, Marco (Department of Biochemistry and Biophysics and Science for Life Laboratory. Stockholm University. Box 1031) ;
Schad, Eva (Institute of Enzymology. Research Centre for Natural Sciences. Hungarian Academy of Sciences) ;
Szabo, Beata (Institute of Enzymology. Research Centre for Natural Sciences. Hungarian Academy of Sciences) ;
Szaniszló, Tamás (MTA-ELTE Lendület Bioinformatics Research Group. Department of Biochemistry. Eötvös Loránd University) ;
Tamana, Stella (Bioinformatics Research Laboratory. Department of Biological Sciences. University of Cyprus) ;
Tantos, Agnes (Institute of Enzymology. Research Centre for Natural Sciences. Hungarian Academy of Sciences) ;
Veljkovic, Nevena (Laboratory for Bioinformatics and Computational Chemistry. Institute of Nuclear Sciences Vinca. University of Belgrade) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Vranken, Wim (Interuniversity Institute of Bioinformatics in Brussels (IB2). ULB-VUB) ;
Dosztányi, Zsuzsanna (MTA-ELTE Lendület Bioinformatics Research Group. Department of Biochemistry. Eötvös Loránd University) ;
Tompa, Peter (Institute of Enzymology. Research Centre for Natural Sciences. Hungarian Academy of Sciences) ;
Tosatto, Silvio C.E. (CNR Institute of Neurosceince) ;
Piovesan, Daminao (Department of Biomedical Sciences. University of Padova)
The Database of Protein Disorder (DisProt, URL: https://disprot. org) provides manually curated annotations of intrinsically disordered proteins from the literature. Here we report recent developments with DisProt (version 8), including the doubling of protein entries, a new disorder ontology, improvements of the annotation format and a completely new website. [...]
2020 - 10.1093/nar/gkz975
Nucleic acids research, Vol. 48, issue D1 (Jan. 2020) , p. D269-D276
|
|
|
6.
|
|
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
|
|
|
7.
|
|
|
8.
|
|
|
9.
|
|
13 p, 1.1 MB |
Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity
/
Sant'Anna, Ricardo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Gallego Alonso, Pablo (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) ;
Ferreira, Nelson (Instituto de Ciências Biomédicas de Abel Salazar) ;
Pinheiro, Francisca (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Esperante, Sebastián (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Huertas, Oscar (SOM-Biotech) ;
Almeida, Maria Rosário (Instituto de Ciências Biomédicas de Abel Salazar) ;
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
|
|
|
10.
|
|
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
|
|
visitante ::
identificación
alerta personal vía correo electrónico o subscríbase al 
canal RSS.
