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Artículos Encontrados 127 registros  inicioanterior34 - 43siguientefinal  ir al registro: La búsqueda tardó 0.02 segundos. 
34.
12 p, 5.2 MB Functionalized Prion-Inspired Amyloids for Biosensor Applications / Díaz-Caballero, Marta (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro, Susanna (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")
Protein amyloid nanofibers provide a biocompatible platform for the development of functional nanomaterials. However, the functionalities generated up to date are still limited. Typical building blocks correspond to aggregation-prone proteins and peptides, which must be modified by complex and expensive reactions post-assembly. [...]
2021 - 10.1021/acs.biomac.1c00222
Biomacromolecules, Vol. 22, Issue 7 (July 2021) , p. 2822-2833  
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35.
15 p, 2.9 MB Cryptic amyloidogenic regions in intrinsically disordered proteins : Function and disease association / Santos, Jaime (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Iglesias, Valentin (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")
The amyloid conformation is considered a fundamental state of proteins and the propensity to populate it a generic property of polypeptides. Multiple proteome-wide analyses addressed the presence of amyloidogenic regions in proteins, nurturing our understanding of their nature and biological implications. [...]
2021 - 10.1016/j.csbj.2021.07.019
Computational and Structural Biotechnology Journal, Vol. 19 (July 2021) , p. 4192-4206  
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36.
14 p, 2.8 MB Critical assessment of protein intrinsic disorder prediction / 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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37.
18 p, 1.3 MB Prion-like proteins : from computational approaches to proteome-wide analysis / Gil Garcia, Marcos (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") ; 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")
Prions are self-perpetuating proteins able to switch between a soluble state and an aggregated-and-transmissible conformation. These proteinaceous entities have been widely studied in yeast, where they are involved in hereditable phenotypic adaptations. [...]
2021 - 10.1002/2211-5463.13213
FEBS Open Bio, Vol. 11, Issue 9 (September 2021) , p. 2400-2417  
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38.
14 p, 2.5 MB Disease-associated mutations impacting BC-loop flexibility trigger long-range transthyretin tetramer destabilization and aggregation / Esperante, Sebastián A. (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Varejão, Nathalia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Pinheiro, Francisca (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sant'Anna, Ricardo (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Luque-Ortega, Juan Román (Centro de Investigaciones Biológicas (Madrid)) ; Alfonso, Carlos (Centro de Investigaciones Biológicas (Madrid)) ; Sora, Valentina (Technical University of Denmark. Cancer Systems Biology, Health and Technology Department) ; Papaleo, Elena (Technical University of Denmark. Cancer Systems Biology, Health and Technology Department) ; Rivas, Germán (Centro de Investigaciones Biológicas (Madrid)) ; Reverter i Cendrós, David (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)
Hereditary transthyretin amyloidosis (ATTR) is an autosomal dominant disease characterized by the extracellular deposition of the transport protein transthyretin (TTR) as amyloid fibrils. Despite the progress achieved in recent years, understanding why different TTR residue substitutions lead to different clinical manifestations remains elusive. [...]
2021 - 10.1016/j.jbc.2021.101039
Journal of biological chemistry, Vol. 297, Issue 3 (September 2021) , art. 101039  
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39.
11 p, 2.4 MB Multifunctional antibody-conjugated coiled-coil protein nanoparticles for selective cell targeting / Gil Garcia, Marcos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Departament de Bioquímica i de Biologia Molecular)
Nanostructures decorated with antibodies (Abs) are applied in bioimaging and therapeutics. However, most covalent conjugation strategies affect Abs functionality. In this study, we aimed to create protein-based nanoparticles to which intact Abs can be attached through tight, specific, and noncovalent interactions. [...]
2021 - 10.1016/j.actbio.2021.06.040
Acta Biomaterialia, Vol. 131 (September 2021) , p. 472-482  
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40.
15 p, 2.9 MB MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation / Batlle Carreras, Cristina (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Calvo, Isabel (Institut de Recerca Biomèdica) ; Iglesias, Valentin (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; J. Lynch, Cian (Institut de Recerca Biomèdica) ; Gil Garcia, Marcos (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Serrano, Manuel (Institut de Recerca Biomèdica) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
A disordered to β-sheet transition was thought to drive the functional switch of Q/N-rich prions, similar to pathogenic amyloids. However, recent evidence indicates a critical role for coiled-coil (CC) regions within yeast prion domains in amyloid formation. [...]
2021 - 10.1038/s42003-021-01930-8
Communications Biology, Vol. 4 (March 2021) , art. 414  
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41.
9 p, 1.1 MB Atomistic fibrillar architectures of polar prion-inspired heptapeptides / Peccati, Francesca (Centro de Investigación Cooperativa en Biociencias. Basque Research and Technology Alliance) ; Díaz-Caballero, Marta (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") ; Rodríguez Santiago, Luis (Universitat Autònoma de Barcelona. Departament de Química) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sodupe Roure, Mariona (Universitat Autònoma de Barcelona. Departament de Química) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular ; Universitat Autònoma de Barcelona. Departament de Química
This article provides the computational prediction of the atomistic architectures resulting from self-assembly of the polar heptapeptide sequences NYNYNYN, SYSYSYS and GYGYGYG. Using a combination of molecular dynamics and a newly developed tool for non-covalent interaction analysis, we uncover the properties of a new class of bionanomaterials, including hydrogen-bonded polar zippers, and the relationship between peptide composition, fibril geometry and weak interaction networks. [...]
2020 - 10.1039/d0sc05638c
Chemical science, Vol. 11, Issue 48 (December 2020) , p. 13143-13151  
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42.
18 p, 1.7 MB MIRRAGGE - Minimum Information Required for Reproducible AGGregation Experiments / Martins, Pedro M. (Universidade do Porto. Instituto de Ciências Biomédicas Abel Salazar) ; Navarro, Susanna (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Silva, Alexandra (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ; Pinto, Maria F. (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ; Sárkány, Zsuzsa (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ; Figueiredo, Francisco (Universidade do Porto. Instituto de Ciências Biomédicas Abel Salazar) ; Barbosa Pereira, Pedro José (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ; Pinheiro, Francisca (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Bednarikova, Zuzana (Slovak Academy of Sciences. Department of Biophysics) ; Burdukiewicz, Michal (Warsaw University of Technology. Faculty of Mathematics and Information Science) ; Galzitskaya, Oxxana V. (Russian Academy of Sciences. Institute of Theoretical and Experimental Biophysics) ; Gazova, Zuzana (Slovak Academy of Sciences. Department of Biophysics) ; Gomes, Cláudio M. (Universidade de Lisboa. Departamento de Química e Bioquímica) ; Pastore, Annalisa (King's College London. Maurice Wohl Clinical Neuroscience Institute) ; Serpell, Louise C. (University of Sussex. School of Life Sciences) ; Skrabana, Rostislav (Slovak Academy of Sciences. Institute of Neuroimmunology) ; Smirnovas, Vytautas (Vilnius University. Institute of Biotechnology) ; Ziaunys, Mantas (Vilnius University. Institute of Biotechnology) ; Otzen, Daniel E. (Aarhus University. Department of Molecular Biology and Genetics) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Macedo-Ribeiro, Sandra (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
Reports on phase separation and amyloid formation for multiple proteins and aggregation-prone peptides are recurrently used to explore the molecular mechanisms associated with several human diseases. [...]
2020 - 10.3389/fnmol.2020.582488
Frontiers in molecular neuroscience, Vol. 13 (November 2020) , art. 582488  
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43.
21 p, 5.3 MB Pathological ATX3 Expression Induces Cell Perturbations in E. coli as Revealed by Biochemical and Biophysical Investigations / Ami, Diletta (University of Milano-Bicocca. Department of Biotechnologies and Biosciences) ; Mereghetti, Paolo (Bioinformatics Consultant) ; Falvo, Jacopo (University of Milano-Bicocca. Department of Biotechnologies and Biosciences) ; Catelani, Tiziano (University of Milano-Bicocca. Department of Biotechnologies and Biosciences) ; Visentin, Cristina (Università degli Studi di Milano. Department of Biosciences) ; Tortora, Paolo (University of Milano-Bicocca. Department of Biotechnologies and Biosciences) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Natalello, Antonino (University of Milano-Bicocca. Departament of Biotechnology and Biosciences) ; Regonesi, Maria Elena (Università di Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ; Sciandrone, Barbara (University of Milano-Bicocca. Department of Biotechnologies and Biosciences)
Amyloid aggregation of human ataxin-3 (ATX3) is responsible for spinocerebellar ataxia type 3, which belongs to the class of polyglutamine neurodegenerative disorders. It is widely accepted that the formation of toxic oligomeric species is primarily involved in the onset of the disease. [...]
2021 - 10.3390/ijms22020943
International journal of molecular sciences, Vol. 22, Issue 2 (January 2021) , art. 943  
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Artículos : Encontrados 127 registros   inicioanterior34 - 43siguientefinal  ir al registro:
Vea también: autores con nombres similares
7 Ventura, S.
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