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Artículos, Encontrados 17 registros
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Artículos Encontrados 17 registros  1 - 10siguiente  ir al registro:
1.
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  
2.
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, I. (Agency for Science, Technology and Research. Bioprocessing Technology Institute) ; Iqbal, S. (Broad Institute of MIT and Harvard. Center for Psychiatric Research) ; Vendruscolo, M. (University of Cambridge. Centre for Misfolding Diseases. Department of Chemistry) ; Sormanni, P. (University of Cambridge. Centre for Misfolding Diseases. Department of Chemistry) ; Wang, C. (Columbia University. Department of Medicine) ; Raimondi, D. (ESAT-STADIUS. KU Leuven) ; Sharma, R. (Fiji National University) ; Zhou, Y. (Griffith University. Institute for Glycomics and School of Information and Communication Technology) ; Litfin, T. (Griffith University. Institute for Glycomics and School of Information and Communication Technology) ; Galzitskaya, Oxxana V (Russian Academy of Sciences. Institute of Theoretical and Experimental Biophysics) ; Lobanov, M.Y. (Russian Academy of Sciences. Institute of Protein Research) ; Vranken, W. (Vrije Universiteit Brussel. Interuniversity Institute of Bioinformatics in Brussels) ; Wallner, B. (Linköping University. Department of Physics, Chemistry and Biology) ; Mirabello, C. (Linköping University. Department of Physics, Chemistry and Biology) ; Malhis, N. (University of British Columbia. Michael Smith Laboratories) ; Dosztányi, Z. (Eötvös Loránd University. Department of Biochemistry) ; Erdős, G. (Eötvös Loránd University. Department of Biochemistry) ; Mészáros, B. (European Molecular Biology Laboratory. Structural and Computational Biology Unit) ; Gao, J. (Nankai University. School of Mathematical Sciences and LPMC) ; Wang, K. (Nankai University. School of Mathematical Sciences and LPMC) ; Hu, G. (Nankai University. School of Statistics and Data Science) ; Wu, Z. (Nankai University. School of Mathematical Sciences and LPMC) ; Sharma, A. (University of the South Pacific. School of Engineering and Physics) ; Hanson, J. (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, I. (Sorbonne Université. Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie. Muséum National d'Histoire Naturelle) ; Bitard-Feildel, T. (Sorbonne Université. Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie. Muséum National d'Histoire Naturelle) ; Orlando, G. (VIB-KU Leuven. Switch Laboratorium.) ; Peng, Z. (Tianjin University. Center for Applied Mathematics) ; Xu, J. (Toyota Technological Institute at Chicago) ; Wang, S. (Toyota Technological Institute at Chicago) ; Jones, D.T. (University College London) ; Cozzetto, D. (University College London) ; Meng, F. (University of Alberta. Department of Electrical and Computer Engineering) ; Yan, J. (University of Alberta. Department of Electrical and Computer Engineering) ; Gsponer, J. (University of British Columbia. Michael Smith Laboratories) ; Cheng, J. (University of Missouri. Department of Electrical Engineering and Computer Science) ; Wu, T. (University of Missouri. Department of Electrical Engineering and Computer Science) ; Kurgan, L. (Virginia Commonwealth University. Department of Computer Science) ; Promponas, V.J. (University of Cyprus. Department of Biological Sciences. Bioinformatics Research Laboratory) ; Tamana, S. (University of Cyprus. Department of Biological Sciences. Bioinformatics Research Laboratory) ; Marino-Buslje, C. (Fundación Instituto Leloir (Buenos Aires, Argentina)) ; Martínez-Pérez, E. (Fundación Instituto Leloir (Buenos Aires, Argentina)) ; Chasapi, Anastasia (Centre for Research & Technology Hellas. Chemical Process & Energy Resources Institute) ; Ouzounis, C. (Centre for Research & Technology Hellas. Chemical Process & Energy Resources Institute) ; Dunker, A.K. (Indiana University School of Medicine. Center for Computational Biology and Bioinformatics) ; Kajava, A.V. (University of Montpellier. Centre de Recherche en Biologie cellulaire de Montpellier) ; Leclercq, J.Y. (University of Montpellier. Centre de Recherche en Biologie cellulaire de Montpellier) ; Aykac-Fas, B. (Danish Cancer Society Research Center) ; Lambrughi, M. (Danish Cancer Society Research Center) ; Maiani, Emiliano (Danish Cancer Society Research Center) ; Papaleo, E. (Danish Cancer Society Research Center) ; Chemes, L.B. (Universidad Nacional de San Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Biotecnológicas) ; Álvarez, L. (Universidad Nacional de San Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Biotecnológicas) ; González-Foutel, N.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, 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, N. (Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología) ; Benítez, G.I. (Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología) ; Parisi, G. (Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología) ; Bassot, Claudio (Stockholm University. Department of Biochemistry and Biophysics and Science for Life Laboratory) ; Elofsson, A. (Stockholm University. Department of Biochemistry and Biophysics and Science for Life Laboratory) ; Govindarajan, S. (Stockholm University. Department of Biochemistry and Biophysics and Science for Life Laboratory) ; Lamb, J. (Stockholm University. Department of Biochemistry and Biophysics and Science for Life Laboratory) ; Salvatore, M. (Copenhagen University. Department of Biology) ; Hatos, A. (University of Padua. Department of Biomedical Sciences) ; Monzon, A.M. (University of Padua. Department of Biomedical Sciences) ; Bevilacqua, M. (University of Padua. Department of Biomedical Sciences) ; Mičetić, I. (University of Padua. Department of Biomedical Sciences) ; Minervini, G. (University of Padua. Department of Biomedical Sciences) ; Paladin, L. (University of Padua. Department of Biomedical Sciences) ; Quaglia, F. (University of Padua. Department of Biomedical Sciences) ; Leonardi, E. (University of Padova - Pediatric Research Institute. Città della Speranza. Department of Woman and Child Health) ; Davey, N. (The Institute of Cancer Research. Chelsea) ; Horvath, T. (Research Centre for Natural Sciences. Institute of Enzymology) ; Kovacs, O.P. (Research Centre for Natural Sciences. Institute of Enzymology) ; Murvai, Nikoletta (Research Centre for Natural Sciences. Institute of Enzymology) ; Pancsa, R. (Research Centre for Natural Sciences. Institute of Enzymology) ; Schad, Eva (Research Centre for Natural Sciences. Institute of Enzymology) ; Szabo, B. (Research Centre for Natural Sciences. Institute of Enzymology) ; Tantos, A. (Research Centre for Natural Sciences. Institute of Enzymology) ; Macedo-Ribeiro, S. (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ; Manso, J.A. (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ; Pereira, P.J.B. (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ; Davidović, R. (University of Belgrade. Vinča Institute of Nuclear Sciences - National Institute of thе Republic of Serbia.) ; Veljkovic, N. (University of Belgrade. Vinča Institute of Nuclear Sciences - National Institute of thе Republic of Serbia.) ; Hajdu-Soltész, B. (Eötvös Loránd University. Department of Biochemistry) ; Pajkos, M. (Eötvös Loránd University. Department of Biochemistry) ; Szaniszló, T. (Eötvös Loránd University. Department of Biochemistry) ; Guharoy, M. (Vrije Universiteit Brussel. Structural Biology Brussels) ; Lazar, T. (Vrije Universiteit Brussel. Structural Biology Brussels) ; Macossay-Castillo, M. (Vrije Universiteit Brussel. Structural Biology Brussels) ; Tompa, P. (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  
3.
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  
4.
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 Ciència i Tecnologia de Barcelona. Institut de Recerca en Biomedicina) ; Iglesias, Valentin (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; J. Lynch, Cian (Institut de Ciència i Tecnologia de Barcelona. Institut de Recerca en Biomedicina) ; Gil-Garcia, Marcos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Serrano, Manuel (Institut de Ciència i Tecnologia de Barcelona. Institut de Recerca en Biomedicina) ; 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
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  
5.
12 p, 1.4 MB DispHred : a server to predict pH-dependent order-disorder transitions in intrinsically disordered proteins / Santos, Jaime (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") ; Pintado Grima, Carlos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Santos-Suárez, Juan (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") ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
The natively unfolded nature of intrinsically disordered proteins (IDPs) relies on several physicochemical principles, of which the balance between a low sequence hydrophobicity and a high net charge appears to be critical. [...]
2020 - 10.3390/ijms21165814
International journal of molecular sciences, Vol. 21, Issue 16 (August 2020) , art. 5814  
6.
11 p, 1.4 MB Computational prediction of protein aggregation : advances in proteomics, conformation-specific algorithms and biotechnological applications / Santos, Jaime (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pujols, 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  
7.
8 p, 674.6 KB DisProt : intrinsic protein disorder annotation in 2020 / 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 (Departamento de Fisiología y Biología Molecular y Celular (DFBMC). Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires) ; 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 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 (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  
8.
16 p, 9.5 MB Characterization of Soft Amyloid Cores in Human Prion-Like Proteins / Batlle Carreras, Cristina (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sánchez de Groot, Natalia (Centre de Regulació Genòmica) ; Iglesias, Valentin (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") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de 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 (Nature Publishing Group), Vol. 7 (2017) , art. 12134  
9.
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 de Biologia Molecular) ; Sánchez de Groot, Natalia (Centre de Regulació Genòmica) ; Iglesias, Valentin (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sant'Anna, Ricardo (Universitat Autònoma de Barcelona. 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  
10.
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 de Biologia Molecular) ; Iglesias, Valentin (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)
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  

Artículos : Encontrados 17 registros   1 - 10siguiente  ir al registro:
Documentos de investigación Encontrados 1 registros  
1.
194 p, 7.0 MB Bioinformatic analysis on the determinants of protein aggregation and conformational conversion / Iglesias Mas, Valentín ; Ventura Zamora, Salvador, dir.
L'agregació de proteïnes ha passat de ser gairebé una curiositat biofísica sense major interès a un dels camps més actius de la recerca, especialment des que es va esbrinar que podia ser la causa de diverses malalties en humans. [...]
La agregación de proteínas ha pasado de ser prácticamente una curiosidad biofísica sin mayor interés a uno de los campos más activos de la investigación, especialmente desde que se dilucidó como el causante de diversas enfermedades en humanos. [...]
Protein aggregation has moved from being an almost neglected biophysical curiosity to a central research field mostly due to aggregating proteins causing debilitating conditions in humans. The aggregation propensity of polypeptidic sequences is primarily dictated by their amino acid sequence, which delimits the possible interactions between amino acids. [...]
Universitat Autònoma de Barcelona. Programa de Doctorat en Bioquímica, Biologia Molecular i Biomedicina.

2021  

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