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Articles, 11 records found
Articles 11 records found  1 - 10next  jump to record:
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, Oscar (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.
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  
10.
14 p, 2.0 MB PH-dependent aggregation in intrinsically disordered proteins is determined by charge and lipophilicity / Santos Suárez, Jaime (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Iglesias, Valentin (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Mangiagalli, Marco (Department of Biotechnology and Biosciences, University of Milano-Bicocca) ; Santos-Suárez, Juan (Galicia Supercomputing Center (CESGA)) ; Brocca, Stefania (Department of Biotechnology and Biosciences, University of Milano-Bicocca) ; Pallarès,Irantzu (Institut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Protein aggregation is associated with an increasing number of human disorders and premature aging. Moreover, it is a central concern in the manufacturing of recombinant proteins for biotechnological and therapeutic applications. [...]
2020 - 10.3390/cells9010145
Cells, Vol. 9 (2020)  

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4 Iglesias, V.
16 Iglesias, Valentín
1 Iglesias, Verónica
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