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Articles 13 registres trobats  1 - 10següent  anar al registre:
1.
12 p, 2.4 MB Inhibition of α-synuclein aggregation and mature fibril disassembling with a minimalistic compound, ZPDm / Peña Díaz, Samuel (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pujols, Jordi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pinheiro, Francisca (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Santos, Jaime (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pallarès i Goitiz, Irantzu (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro Cantero, Susana (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 (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  
2.
11 p, 1.4 MB Computational prediction of protein aggregation : advances in proteomics, conformation-specific algorithms and biotechnological applications / Santos, Jaime (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pujols, Jordi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pallarès i Goitiz, Irantzu (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (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  
3.
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, Susana (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  
4.
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 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 (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  
5.
16 p, 3.8 MB Disulfide driven folding for a conditionally disordered protein / Fraga, Hugo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pujols, Jordi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Gil-Garcia, Marcos (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 (Nature Publishing Group), Vol. 7 (2017) , art. 16994  
6.
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 de Lleida) ; Navarro Cantero, Susana (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pinheiro, Francisca (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  
7.
15 p, 1.8 MB C-mannosylation supports folding and enhances stability of thrombospondin repeats / Shcherbakova, Aleksandra (Medizinische Hochschule Hannover. Institut für Klinische Biochemie) ; Preller, Matthias (Medizinische Hochschule Hannover. Institut für Biophysikalische Chemie) ; Taft, Manuel H. (Medizinische Hochschule Hannover. Institut für Biophysikalische Chemie) ; Pujols, Jordi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Tiemann, Birgit (Medizinische Hochschule Hannover. Institut für Klinische Biochemie) ; Buettner, Falk F.R. (Medizinische Hochschule Hannover. Institut für Klinische Biochemie) ; Bakker, Hans (Medizinische Hochschule Hannover. Institut für Klinische Biochemie)
Previous studies demonstrated importance of C-mannosylation for efficient protein secretion. To study its impact on protein folding and stability, we analyzed both C-mannosylated and non-C-mannosylated thrombospondin type 1 repeats (TSRs) of netrin receptor UNC-5. [...]
2019 - 10.7554/eLife.52978
eLife, Vol. 8 (Dec. 2019) , art. e52978  
8.
8 p, 2.9 MB Aggrescan3D (A3D) 2.0 : prediction and engineering of protein solubility / Kuriata, Aleksander (Centrum Nauk Biologiczno-Chemicznych Uniwersytetu Warszawskiego) ; Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pujols, Jordi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Kurcinski, Mateusz (Centrum Nauk Biologiczno-Chemicznych Uniwersytetu Warszawskiego) ; Kmiecik, Sebastian (Centrum Nauk Biologiczno-Chemicznych Uniwersytetu Warszawskiego) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Protein aggregation is a hallmark of a growing number of human disorders and constitutes a major bottleneck in the manufacturing of therapeutic proteins. Therefore, there is a strong need of in-silico methods that can anticipate the aggregative properties of protein variants linked to disease and assist the engineering of soluble protein-based drugs. [...]
2019 - 10.1093/nar/gkz321
Nucleic acids research, Vol. 47, issue W1 (July 2019) , p. W300-W307  
9.
13 p, 2.6 MB The disordered C-terminus of yeast hsf1 contains a cryptic low-complexity amyloidogenic region / Pujols, Jordi (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Santos, Jaime (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de 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  
10.
12 p, 12.3 MB High-throughput screening methodology to identify alpha-synuclein aggregation inhibitors / Pujols, Jordi (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Peña Díaz, Samuel (Universitat Autònoma de Barcelona. Departament de Bioquímica i de 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 de Biologia Molecular) ; Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i de 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  

Articles : 13 registres trobats   1 - 10següent  anar al registre:
Documents de recerca 1 registres trobats  
1.
1 p, 1.4 MB HSP90-kinase recognition : role of kinase domain stability in interactions strenght / Pujols i Pujol, Jordi ; Ventura, Salvador, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Facultat de Biociències
2013
Grau en Bioquímica [814]  

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