Resultados globales: 31 registros encontrados en 0.02 segundos.
Artículos, Encontrados 27 registros
Contribuciones a jornadas y congresos, Encontrados 1 registros
Documentos de investigación, Encontrados 3 registros
Artículos Encontrados 27 registros  1 - 10siguientefinal  ir al registro:
1.
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  
2.
16 p, 9.5 MB Characterization of Soft Amyloid Cores in Human Prion-Like Proteins / Batlle Carreras, Cristina (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sánchez de Groot, Natalia (Centre de Regulació Genòmica) ; Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro Cantero, Susanna (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Prion-like behaviour is attracting much attention due to the growing evidences that amyloid-like self-assembly may reach beyond neurodegeneration and be a conserved functional mechanism. The best characterized functional prions correspond to a subset of yeast proteins involved in translation or transcription. [...]
2017 - 10.1038/s41598-017-09714-z
Scientific reports, Vol. 7 (2017) , art. 12134  
3.
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  
4.
12 p, 1.6 MB The rho termination factor of Clostridium botulinum contains a prion-like domain with a highly amyloidogenic core / Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Prion-like proteins can switch between a soluble intrinsically disordered conformation and a highly ordered amyloid assembly. This conformational promiscuity is encoded in specific sequence regions, known as prion domains (PrDs). [...]
2016 - 10.3389/fmicb.2015.01516
Frontiers in microbiology, Vol. 6 (Jan. 2016) , art. 1516  
5.
13 p, 7.9 MB Computational analysis of candidate prion-like proteins in bacteria and their role / Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sánchez de Groot, Natalia (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Prion proteins were initially associated with diseases such as Creutzfeldt Jakob and transmissible spongiform encephalopathies. However, deeper research revealed them as versatile tools, exploited by the cells to execute fascinating functions, acting as epigenetic elements or building membrane free compartments in eukaryotes. [...]
2015 - 10.3389/fmicb.2015.01123
Frontiers in microbiology, Vol. 6 (Oct. 2015) , art. 1123  
6.
12 p, 4.2 MB In silico characterization of human prion-like proteins : beyond neurological diseases / Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Paladin, Lisanna (Università di Padua. Dipartimento di Scienze Biomediche) ; Juan Blanco, Teresa (Institut de Recerca Biomèdica) ; Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Aloy, Patrick (Institució Catalana de Recerca i Estudis Avançats (ICREA)) ; Tosatto, Silvio C.E. (Università di Padua. Dipartimento di Scienze Biomediche) ; Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammalian neurodegenerative diseases. However, a growing body of evidence suggests that this mechanism could be behind the regulation of processes such as transcription and translation in multiple species. [...]
2019 - 10.3389/fphys.2019.00314
Frontiers in physiology, Vol. 10 (March 2019) , art. 314  
7.
5 p, 900.2 KB AMYCO : evaluation of mutational impact on prion-like proteins aggregation propensity / Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Conchillo-Solé, Óscar (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Batlle Carreras, Cristina (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Background: around 1% of human proteins are predicted to contain a disordered and low complexity prion-like domain (PrLD). Mutations in PrLDs have been shown promote a transition towards an aggregation-prone state in several diseases. [...]
2019 - 10.1186/s12859-019-2601-3
BMC bioinformatics, Vol. 20 (2019) , art. 24  
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.
17 p, 261.9 KB Entre lo formal y lo no formal : un análisis desde la formación permanente del profesorado / Souto-Seijo, Alba (Universidade da Coruña) ; Estévez, Iris (Universidade da Coruña) ; Iglesias Fustes, Verónica (Universidade da Coruña) ; González-Sanmamed, Mercedes (Universidade da Coruña)
Una de las características más relevantes de la sociedad actual es que el aprendizaje no se desarrolla de forma lineal ni en espacios concretos, por lo que no se puede limitar a los parámetros de la modalidad formal. [...]
Una de les característiques més rellevants de la societat actual és el fet que l'aprenentatge no es desenvolupa de forma lineal ni en espais concrets. Això fa que no es pugui limitar als paràmetres de la modalitat formal. [...]
One of the most relevant characteristics of today's society is that learning does not take place in a linear way or in specific spaces, so it cannot be limited to the parameters of the formal modality. [...]

2020 - 10.5565/rev/educar.1095
Educar, Vol. 56 Núm. 1 (2020) , p. 91-107 (Monográfico)  
10.
20 p, 6.2 MB Computational assessment of bacterial protein structures indicates a selection against aggregation / Carija, Anita (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pinheiro, Francisca (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
The aggregation of proteins compromises cell fitness, either because it titrates functional proteins into non-productive inclusions or because it results in the formation of toxic assemblies. Accordingly, computational proteome-wide analyses suggest that prevention of aggregation upon misfolding plays a key role in sequence evolution. [...]
2019 - 10.3390/cells8080856
Cells, Vol. 8 (2019) , p. 1-20  

Artículos : Encontrados 27 registros   1 - 10siguientefinal  ir al registro:
Contribuciones a jornadas y congresos Encontrados 1 registros  
1.
10 p, 89.4 KB Neel Doff ou la rupture de l'omerta : une dénonciation de la société et des mœurs du XIXème siècle / Iglesias Pruvost, Virginia (Université de Grenade)
Neel Doff (1858-1942) est une écrivaine prolétarienne belge, d'expression française, quasiment inconnue. Dans sa trilogie de forte inspiration autobiographique, composée de Jours de famine, Keetje et Keetje trottin, elle entend dévoiler les souffrances des miséreux, d'autant plus s'il s'agit de femmes. [...]
2012
Colloque de l'Asociación de Profesores de Francés de la Universidad Española. Barcelona-Bellaterra, 21r : 2012  

Documentos de investigación Encontrados 3 registros  
1.
460 p, 5.0 MB El Desarrollo de la educación literaria en aprendientes iniciales de ELE : una propuesta didáctica llevada a las aulas / García Iglesias, Mª Victoria, autor. ; Real Mercadal, Neus, supervisor acadèmic. ; Regueiro, Marisa, supervisor acadèmic. ; Universitat Autònoma de Barcelona. Departament de Didàctica de la Llengua i la Literatura i de les Ciències Socials
Esta tesis doctoral recoge una investigación que se propuso llevar la literatura a las aulas de primero de secundaria bilingüe para extranjeros. La intervención en el aula se materializó a través de un curso que aúna el estudio de la lengua y la literatura bajo una metodología integradora que favorece las repercusiones didácticas en el proceso global de aprendizaje del Español como Lengua Extranjera (ELE). [...]
This doctoral thesis presents an investigation that was proposed to take the literature to the first class of bilingual secondary for foreigners. The intervention in the classroom was materialized through a course that combines the study of language and literature under an integrative methodology that favors the didactic repercussions in the overall learning process of Spanish as a Foreign Language (SFL). [...]

[Barcelona] : Universitat Autònoma de Barcelona, 2017.  
2.
148 p, 16.4 MB CAFM nanoscale electrical properties and reliability of HfO₂ based gate dielectrics in electron devices : impact of the polycrystallization and resistive switching / Iglesias Santiso, Vanessa ; Porti i Pujal, Marc, dir. (Universitat Autònoma de Barcelona. Departament d'Enginyeria Electrònica) ; Universitat Autònoma de Barcelona. Departament d'Enginyeria Electrònica
La evolución de los dispositivos MOS ha conllevado una reducción de tamaño de los mismos con el fin de mejorar sus prestaciones. Sin embargo, este continuo escalado se ha topado con un límite físico: la delgada capa aislante de SiO2 (entre otros), que fuerza la búsqueda de nuevas alternativas que permitan abastecer al exigente mercado tecnológico. [...]
The evolution of MOS devices has involved an important shrinking in the transistor size with the aim of improve their benefits. However, this continuous miniaturization has found its physical limits in the thin SiO2 dielectric layer with current sizes at nanometric scale. [...]

[Barcelona] : Universitat Autònoma de Barcelona, 2013  
3.
47 p, 1.6 MB Transporte de animales de compañía / Santos Sempere, Laura de los. ; Tojo Iglesias, Victoriano José
2010. (Treballs de l'assignatura Deontologia Veterinària.)  

Vea también: autores con nombres similares
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