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1.
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11 p, 2.5 MB |
The small aromatic compound SynuClean-D inhibits the aggregation and seeded polymerization of multiple α-synuclein strains
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Peña Díaz, Samuel (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Pujols Pujol, Jordi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Vasili, Eftychia (Max Planck Institute for Experimental Medicine) ;
Pinheiro, Francisca (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Santos, Jaime (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Manglano-Artuñedo, Zoe (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Outeiro, Tiago Fleming (Scientific Employee With a Honorary Contract. Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE)) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Parkinson's disease is a neurodegenerative disorder characterized by the loss of dopaminergic neurons in the substantia nigra, as well as the accumulation of intraneuronal proteinaceous inclusions known as Lewy bodies and Lewy neurites. [...]
2022 -  10.1016/j.jbc.2022.101902
Journal of biological chemistry, Vol. 298, Issue 5 (May 2022) , art. 101902
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2.
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14 p, 4.4 MB |
α-Helical peptidic scaffolds to target α-synuclein toxic species with nanomolar affinity
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Santos, Jaime (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Gracia González, Pablo (Universidad de Zaragoza. Instituto de Biocomputación y Física de Sistemas Complejos) ;
Navarro, Susanna (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Peña Díaz, Samuel (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Pujols Pujol, Jordi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Cremades, Nunilo (Universidad de Zaragoza. Instituto de Biocomputación y Física de Sistemas Complejos) ;
Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
α-Synuclein aggregation is a key driver of neurodegeneration in Parkinson's disease and related syndromes. Accordingly, obtaining a molecule that targets α-synuclein toxic assemblies with high affinity is a long-pursued objective. [...]
2021 - 10.1038/s41467-021-24039-2
Nature communications, Vol. 12 (June 2021) , art. 3752
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3.
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14 p, 2.8 MB |
Critical assessment of protein intrinsic disorder prediction
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Necci, Marco (University of Padua. Department of Biomedical Sciences) ;
Piovesan, Damiano (University of Padua. Department of Biomedical Sciences) ;
Hoque, M. T. (University of New Orleans. Computer Science) ;
Walsh, Ian (Agency for Science, Technology and Research. Bioprocessing Technology Institute) ;
Iqbal, Sumaiya (Broad Institute of MIT and Harvard. Center for Psychiatric Research) ;
Vendruscolo, Michele (University of Cambridge. Centre for Misfolding Diseases. Department of Chemistry) ;
Sormanni, Pietro (University of Cambridge. Centre for Misfolding Diseases. Department of Chemistry) ;
Wang, Chen (Columbia University. Department of Medicine) ;
Raimondi, Daniele (ESAT-STADIUS. KU Leuven) ;
Sharma, Ronesh (Fiji National University) ;
Zhou, Yaoqi (Griffith University. Institute for Glycomics and School of Information and Communication Technology) ;
Litfin, Thomas (Griffith University. Institute for Glycomics and School of Information and Communication Technology) ;
Galzitskaya, Oxxana Valerianovna (Russian Academy of Sciences. Institute of Theoretical and Experimental Biophysics) ;
Lobanov, Michail Yu (Russian Academy of Sciences. Institute of Protein Research) ;
Vranken, Wim (Vrije Universiteit Brussel. Interuniversity Institute of Bioinformatics in Brussels) ;
Wallner, Björn (Linköping University. Department of Physics, Chemistry and Biology) ;
Mirabello, Claudio (Linköping University. Department of Physics, Chemistry and Biology) ;
Malhis, Nawar (University of British Columbia. Michael Smith Laboratories) ;
Dosztányi, Zsuzsanna (Eötvös Loránd University. Department of Biochemistry) ;
Erdős, Gábor (Eötvös Loránd University. Department of Biochemistry) ;
Mészáros, Bálint (European Molecular Biology Laboratory. Structural and Computational Biology Unit) ;
Gao, Jianzhao (Nankai University. School of Mathematical Sciences and LPMC) ;
Wang, Kui (Nankai University. School of Mathematical Sciences and LPMC) ;
Hu, Gang (Nankai University. School of Statistics and Data Science) ;
Wu, Zhonghua (Nankai University. School of Mathematical Sciences and LPMC) ;
Sharma, Alok (University of the South Pacific. School of Engineering and Physics) ;
Hanson, Jack (Griffith University. School of Engineering and Built Environment. Signal Processing Laboratory Griffith University. School of Engineering and Built Environment. Signal Processing Laboratory Signal Processing Laboratory. School of Engineering and Built Environment. Griffith University) ;
Callebaut, Isabelle (Sorbonne Université. Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie. Muséum National d'Histoire Naturelle) ;
Bitard-Feildel, Tristan (Sorbonne Université. Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie. Muséum National d'Histoire Naturelle) ;
Orlando, Gabriele (VIB-KU Leuven. Switch Laboratorium.) ;
Peng, Zhenling (Tianjin University. Center for Applied Mathematics) ;
Xu, Jinbo (Toyota Technological Institute at Chicago) ;
Wang, Sheng (Toyota Technological Institute at Chicago) ;
Jones, David T. (University College London) ;
Cozzetto, Domenico (University College London) ;
Meng, Fanchi (University of Alberta. Department of Electrical and Computer Engineering) ;
Yan, Jing (University of Alberta. Department of Electrical and Computer Engineering) ;
Gsponer, Jörg (University of British Columbia. Michael Smith Laboratories) ;
Cheng, Jianlin (University of Missouri. Department of Electrical Engineering and Computer Science) ;
Wu, Tianqi (University of Missouri. Department of Electrical Engineering and Computer Science) ;
Kurgan, Lukasz (Virginia Commonwealth University. Department of Computer Science) ;
Promponas, Vasilis J. (University of Cyprus. Department of Biological Sciences. Bioinformatics Research Laboratory) ;
Tamana, Stella (University of Cyprus. Department of Biological Sciences. Bioinformatics Research Laboratory) ;
Marino-Buslje, Cristina (Fundación Instituto Leloir (Buenos Aires, Argentina)) ;
Martínez-Pérez, Elisabeth (Fundación Instituto Leloir (Buenos Aires, Argentina)) ;
Chasapi, Anastasia (Centre for Research & Technology Hellas. Chemical Process & Energy Resources Institute) ;
Ouzounis, Christos (Centre for Research & Technology Hellas. Chemical Process & Energy Resources Institute) ;
Dunker, A. Keith (Indiana University School of Medicine. Center for Computational Biology and Bioinformatics) ;
Kajava, Andrey V (University of Montpellier. Centre de Recherche en Biologie cellulaire de Montpellier) ;
Leclercq, Jeremy Y. (University of Montpellier. Centre de Recherche en Biologie cellulaire de Montpellier) ;
Aykac-Fas, Burcu (Danish Cancer Society Research Center) ;
Lambrughi, Matteo (Danish Cancer Society Research Center) ;
Maiani, Emiliano (Danish Cancer Society Research Center) ;
Papaleo, Elena (Danish Cancer Society Research Center) ;
Chemes, Lucía Beatriz (Universidad Nacional de San Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Biotecnológicas) ;
Álvarez, Lucía (Universidad Nacional de San Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Biotecnológicas) ;
González-Foutel, Nicolás S. (Universidad Nacional de San Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Biotecnológicas) ;
Iglesias, Valentin (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Pujols Pujol, Jordi (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") ;
Palopoli, Nicolas (Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología) ;
Benítez, Guillermo I (Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología) ;
Parisi, Gustavo (Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología) ;
Bassot, Claudio (Stockholm University. Department of Biochemistry and Biophysics and Science for Life Laboratory) ;
Elofsson, Arne (Stockholm University. Department of Biochemistry and Biophysics and Science for Life Laboratory) ;
Govindarajan, Sudha (Stockholm University. Department of Biochemistry and Biophysics and Science for Life Laboratory) ;
Lamb, John (Stockholm University. Department of Biochemistry and Biophysics and Science for Life Laboratory) ;
Salvatore, Marco (Copenhagen University. Department of Biology) ;
Hatos, András (Università di Padova. Dipartimento di Scienze Biomediche) ;
Monzon, Alexander Miguel (Università di Padova. Dipartimento di Scienze Biomediche) ;
Bevilacqua, Martina (Università di Padova. Dipartimento di Scienze Biomediche) ;
Mičetić, Ivan (Università di Padova. Dipartimento di Scienze Biomediche) ;
Minervini, Giovanni (Università di Padova. Dipartimento di Scienze Biomediche) ;
Paladin, Lisanna (Università di Padova. Dipartimento di Scienze Biomediche) ;
Quaglia, Federica (Università di Padova. Dipartimento di Scienze Biomediche) ;
Leonardi, Emanuela (Università di Padova) ;
Davey, Norman E. (The Institute of Cancer Research. Chelsea) ;
Horvath, Tamas (Research Centre for Natural Sciences. Institute of Enzymology) ;
Kovacs, Orsolya Panna (Research Centre for Natural Sciences. Institute of Enzymology) ;
Murvai, Nikoletta (Research Centre for Natural Sciences. Institute of Enzymology) ;
Pancsa, Rita (Research Centre for Natural Sciences. Institute of Enzymology) ;
Schad, Eva (Research Centre for Natural Sciences. Institute of Enzymology) ;
Szabo, Beata (Research Centre for Natural Sciences. Institute of Enzymology) ;
Tantos, Agnes (Research Centre for Natural Sciences. Institute of Enzymology) ;
Macedo-Ribeiro, Sandra (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ;
Manso, Jose Antonio (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ;
Barbosa Pereira, Pedro José (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ;
Davidović, Radoslav (University of Belgrade. Vinča Institute of Nuclear Sciences - National Institute of thе Republic of Serbia.) ;
Veljkovic, Nevena (University of Belgrade. Vinča Institute of Nuclear Sciences - National Institute of thе Republic of Serbia.) ;
Hajdu-Soltész, Borbála (Eötvös Loránd University. Department of Biochemistry) ;
Pajkos, Mátyás (Eötvös Loránd University. Department of Biochemistry) ;
Szaniszló, Tamás (Eötvös Loránd University. Department of Biochemistry) ;
Guharoy, Mainak (Vrije Universiteit Brussel. Structural Biology Brussels) ;
Lazar, Tamas (Vrije Universiteit Brussel. Structural Biology Brussels) ;
Macossay-Castillo, Mauricio (Vrije Universiteit Brussel. Structural Biology Brussels) ;
Tompa, Peter (Vrije Universiteit Brussel. Structural Biology Brussels) ;
Tosatto, Silvio (University of Padua. Department of Biomedical Sciences)
Intrinsically disordered proteins, defying the traditional protein structure-function paradigm, are a challenge to study experimentally. Because a large part of our knowledge rests on computational predictions, it is crucial that their accuracy is high. [...]
2021 - 10.1038/s41592-021-01117-3
Nature Methods, Vol. 18 (May 2021) , p. 472-481
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4.
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285 p, 10.3 MB |
Connection between protein disorder, folding and aggregation : Physiological and Pathological implications
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Pujols Pujol, Jordi ;
Avilés, Francesc X, dir. ;
Ventura Zamora, Salvador, dir.
Les Proteïnes o Regions Intrínsecament Desordenades (IDPs, IDRs) son una classe de polipèptids que són incapaços d'adoptar una estructura tridimensional definida en el seu estat natiu. La seva funció depèn de la flexibilitat estructural i de la fluctuació entre un conjunt de conformacions diferents. [...]
Las proteínas o Regiones Intrínsecamente Desordenadas (IDPs, IDRs) son una clase de polipéptidos incapaces de adoptar una estructura tridimensional definida en su estado nativo. Su función depende de la flexibilidad estructural y de la fluctuación entre un conjunto de diferentes conformaciones. [...]
Intrinsically Disordered Proteins (IDPs) and Regions (IDRs) are a class of polypeptides that lack defined three-dimensional structures. Instead, they populate a dynamic ensemble of flexible conformers that endorse them with unique properties to interact with multiple partners and mediate in signal transduction. [...]
2021
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5.
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12 p, 2.4 MB |
Inhibition of α-synuclein aggregation and mature fibril disassembling with a minimalistic compound, ZPDm
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Peña Díaz, Samuel (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Pujols Pujol, 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 Giménez, 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, 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
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6.
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11 p, 1.4 MB |
Computational prediction of protein aggregation : advances in proteomics, conformation-specific algorithms and biotechnological applications
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Santos, Jaime (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Pujols Pujol, 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
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7.
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15 p, 4.1 MB |
Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity
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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 Pujol, 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 Fleming (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
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8.
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8 p, 674.6 KB |
DisProt : intrinsic protein disorder annotation in 2020
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Hatos, András (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 (Centre for Research and Technology Hellas (Tessalònica, Grècia)) ;
Chemes, Lucía Beatriz (Universidad de Buenos Aires. Departamento de Fisiología y Biología Molecular y Celular) ;
Davey, Norman E. (Institute of Cancer Research (Londres, Regne Unit)) ;
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 (Universitat Autònoma de Barcelona. 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 National de la Recherche Scientifique (França). Centre de Recherche en Biologie Cellulaire de 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 (Fundación Instituto Leloir (Buenos Aires, Argentina)) ;
Martínez-Pérez, Elisabeth (Fundación Instituto Leloir (Buenos Aires, Argentina)) ;
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. (Centre for Research and Technology Hellas (Tessalònica, Grècia)) ;
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 José (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 Pujol, Jordi (Universitat Autònoma de Barcelona. 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 (CNR Institute of Neurosceince) ;
Piovesan, Damiano (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
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9.
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16 p, 3.8 MB |
Disulfide driven folding for a conditionally disordered protein
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Fraga, Hugo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Pujols Pujol, Jordi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Gil Garcia, Marcos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Roque Córdova, Alicia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Bernardo-Seisdedos, Ganeko (CIC BioGUNE) ;
Santambrogio, Carlo (University of Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ;
Bech-Serra, Joan-Josep (Vall d'Hebron Institut d'Oncologia) ;
Canals, Francesc (Vall d'Hebron Institut d'Oncologia) ;
Bernadó, Pau (Centre de biochimie Structurale (Montpellier)) ;
Grandori, Rita (University of Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ;
Millet, Oscar (CIC BioGUNE) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Conditionally disordered proteins are either ordered or disordered depending on the environmental context. The substrates of the mitochondrial intermembrane space (IMS) oxidoreductase Mia40 are synthesized on cytosolic ribosomes and diffuse as intrinsically disordered proteins to the IMS, where they fold into their functional conformations; behaving thus as conditionally disordered proteins. [...]
2017 - 10.1038/s41598-017-17259-4
Scientific reports, Vol. 7 (2017) , art. 16994
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10.
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12 p, 3.6 MB |
ZPD-2, a small compound that inhibits α-synuclein amyloid aggregation and its seeded polymerization
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Peña Díaz, Samuel (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Pujols Pujol, Jordi (Universitat Autònoma de Barcelona. 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) ;
Carija, Anita (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Dalfo, Esther (Universitat Autònoma de Barcelona. Facultat de Medicina) ;
García, Jesús (Institut de Recerca Biomèdica de Lleida) ;
Navarro, Susanna (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. Departament de Bioquímica i de Biologia Molecular) ;
Salvatella, Xavier (Institut de Recerca Biomèdica de Lleida) ;
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
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