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12 p, 2.9 MB |
Cryo-EM structure of hnRNPDL-2 fibrils, a functional amyloid associated with limb-girdle muscular dystrophy D3
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Garcia-Pardo, Javier (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Bartolomé-Nafría, Andrea (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Chaves-Sanjuan, Antonio (Università degli Studi di Milano. Dipartimento di Bioscienze) ;
Gil Garcia, Marcos (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Visentin, Cristina (Università degli Studi di Milano. Dipartimento di Bioscienze) ;
Bolognesi, Martino (Università degli Studi di Milano. CRC Fondazione Romeo e Enrica Invernizzi and NOLIMITS) ;
Ricagno, Stefano (Policlinico San Donato. Institute of Molecular and Translational Cardiology, I.R.C.C.S.) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
hnRNPDL is a ribonucleoprotein (RNP) involved in transcription and RNA-processing that hosts missense mutations causing limb-girdle muscular dystrophy D3 (LGMD D3). Mammalian-specific alternative splicing (AS) renders three natural isoforms, hnRNPDL-2 being predominant in humans. [...]
2023 -  10.1038/s41467-023-35854-0
Nature communications, Vol. 14 (January 2023) , art. 239
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17 p, 5.7 MB |
An integrated multi-omics approach identifies the landscape of interferon-α-mediated responses of human pancreatic beta cells
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Colli, M. L. (ULB Center for Diabetes Research. Medical Faculty. Université Libre de Bruxelles) ;
Ramos-Rodríguez, M. (Institut Germans Trias i Pujol. Hospital Universitari Germans Trias i Pujol) ;
Nakayasu, E. S. (Biological Sciences Division. Pacific Northwest National Laboratory) ;
Alvelos, M. I. (ULB Center for Diabetes Research. Medical Faculty. Université Libre de Bruxelles) ;
Lopes, M. (ULB Center for Diabetes Research. Medical Faculty. Université Libre de Bruxelles) ;
Hill, J. L. E. (Institute of Biomedical & Clinical Science. University of Exeter Medical School) ;
Turatsinze, J. V. (ULB Center for Diabetes Research. Medical Faculty. Université Libre de Bruxelles) ;
Coomans de Brachène, A. (ULB Center for Diabetes Research. Medical Faculty. Université Libre de Bruxelles) ;
Russell, M. A. (Institute of Biomedical & Clinical Science. University of Exeter Medical School) ;
Raurell Vila, Helena (Institut Germans Trias i Pujol. Hospital Universitari Germans Trias i Pujol) ;
Castela, A. (ULB Center for Diabetes Research. Medical Faculty. Université Libre de Bruxelles) ;
Juan-Mateu, J. (ULB Center for Diabetes Research. Medical Faculty. Université Libre de Bruxelles) ;
Webb-Robertson, B. J. M. (Biological Sciences Division. Pacific Northwest National Laboratory) ;
Krogvold, L. (Oslo University Hospital (Oslo, Noruega)) ;
Dahl-Jorgensen, K. (Oslo University Hospital (Oslo, Noruega)) ;
Marselli, L. (Department of Clinical and Experimental Medicine. Islet Cell Laboratory. University of Pisa) ;
Marchetti, P. (Department of Clinical and Experimental Medicine. Islet Cell Laboratory. University of Pisa) ;
Richardson, S. J. (Institute of Biomedical & Clinical Science. University of Exeter Medical School) ;
Morgan, N. G. (Institute of Biomedical & Clinical Science. University of Exeter Medical School) ;
Metz, T. O. (Biological Sciences Division. Pacific Northwest National Laboratory) ;
Pasquali, Lorenzo (Institut Germans Trias i Pujol. Institut de Recerca contra la Leucèmia Josep Carreras) ;
Eizirik, D. L. (Indiana Biosciences Research Institute) ;
Universitat Autònoma de Barcelona
Interferon-α (IFNα), a type I interferon, is expressed in the islets of type 1 diabetic individuals, and its expression and signaling are regulated by T1D genetic risk variants and viral infections associated with T1D. [...]
2020 - 10.1038/s41467-020-16327-0
Nature communications, Vol. 11 Núm. 1 (january 2020) , p. 2584
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28 p, 6.3 MB |
PTBP1-Mediated Alternative Splicing Regulates the Inflammatory Secretome and the Pro-tumorigenic Effects of Senescent Cells
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Georgilis, Athena (Imperial College London) ;
Klotz, Sabrina (Eberhard Karls University Tübingen) ;
Hanley, Christopher J. (University of Southampton) ;
Herranz, Nicolas (Imperial College London) ;
Weirich, Benedikt (German Cancer Research Centre (DKFZ)) ;
Morancho, Beatriz (Vall d'Hebron Institut d'Oncologia) ;
Leote, Ana Carolina (Universidade de Lisboa) ;
D'Artista, Luana (Eberhard Karls University Tübingen) ;
Gallage, Suchira (German Cancer Research Centre (DKFZ)) ;
Seehawer, Marco (Eberhard Karls University Tübingen) ;
Carroll, Thomas (Imperial College London) ;
Dharmalingam, Gopuraja (Imperial College London) ;
Wee, Keng Boon (Bioinformatics Institute) ;
Mellone, Marco (University of Southampton) ;
Pombo, Joaquim (Imperial College London) ;
Heide, Danijela (German Cancer Research Centre (DKFZ)) ;
Guccione, Ernesto (Institute of Molecular and Cell Biology (Singapore)) ;
Arribas, Joaquín V (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Barbosa-Morais, Nuno L. (Universidade de Lisboa) ;
Heikenwälder, Mathias (German Cancer Research Centre (DKFZ)) ;
Thomas, Gareth J. (University of Southampton) ;
Zender, Lars (German Cancer Research Center (DKFZ)) ;
Gil, Jesús (Imperial College London)
Oncogene-induced senescence is a potent tumor-suppressive response. Paradoxically, senescence also induces an inflammatory secretome that promotes carcinogenesis and age-related pathologies. Consequently, the senescence-associated secretory phenotype (SASP) is a potential therapeutic target. [...]
2018 - 10.1016/j.ccell.2018.06.007
Cancer Cell, Vol. 34 (july 2018) , p. 85-102.e9
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18 p, 3.6 MB |
hnRNPDL phase separation is regulated by alternative splicing and disease-causing mutations accelerate its aggregation
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Batlle Carreras, Cristina (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Yang, Peiguo (St. Jude Children's Research Hospital (Memphis, Estats Units d'Amèrica)) ;
Coughlin, Maura (St. Jude Children's Research Hospital (Memphis, Estats Units d'Amèrica)) ;
Messing, James (Howard Hughes Medical Institute) ;
Pesarrodona Roches, Mireia (Institut de Recerca Biomèdica de Lleida) ;
Szulc, Elzbieta (Institut de Recerca Biomèdica de Lleida) ;
Salvatella, Xavier (Institut de Recerca Biomèdica de Lleida) ;
Kim, Hong Joo (St. Jude Children's Research Hospital (Memphis, Estats Units d'Amèrica)) ;
Taylor, J. Paul (Howard Hughes Medical Institute) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Prion-like proteins form multivalent assemblies and phase separate into membraneless organelles. Heterogeneous ribonucleoprotein D-like (hnRNPDL) is a RNA-processing prion-like protein with three alternative splicing (AS) isoforms, which lack none, one, or both of its two disordered domains. [...]
2020 - 10.1016/j.celrep.2019.12.080
Cell reports, Vol. 30, issue 4 (Jan. 2020) , p. 1117-1128
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12 p, 1.0 MB |
Site-Specific mRNA Cleavage for Selective and Quantitative Profiling of Alternative Splicing with Label-Free Optical Biosensors
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Huertas, César S. (Institut Català de Nanociència i Nanotecnologia) ;
Bonnal, Sophie (Universitat Pompeu Fabra) ;
Soler Aznar, Maria (Institut Català de Nanociència i Nanotecnologia) ;
Escuela, Alfonso M. (Universidad de Las Palmas de Gran Canaria) ;
Valcárcel, Juan (Universitat Pompeu Fabra) ;
Lechuga, Laura M (Institut Català de Nanociència i Nanotecnologia)
Alternative splicing of mRNA precursors is a key process in gene regulation, contributing to the diversity of proteomes by the alternative selection of exonic sequences. Alterations in this mechanism are associated with most cancers, enhancing their proliferation and survival, and can be employed as cancer biomarkers. [...]
2019 - 10.1021/acs.analchem.9b03898
Analytical chemistry, Vol. 91, Issue 23 (December 2019) , p. 15138-15146
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21 p, 6.7 MB |
Identification and characterization of new isoforms of human fas apoptotic inhibitory molecule (FAIM)
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Coccia, Elena (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Calleja Yagüe, Isabel (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Planells Ferrer, Laura (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Sanuy, Blanca (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Sanz, Belen (Centro Nacional de Investigaciones Oncológicas) ;
López-Soriano, Joaquín (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Moubarak, Rana S. (Department of Pathology. NYU Langone Medical Center) ;
Munell Casadesus, Francina (Hospital Universitari Vall d'Hebron. Institut de Recerca) ;
Barneda Zahonero, Bruna (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Comella i Carnicé, Joan Xavier 1963- (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Pérez-García, M. Jose (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Fas Apoptosis Inhibitory Molecule (FAIM) is an evolutionarily highly conserved death receptor antagonist, widely expressed and known to participate in physiological and pathological processes. Two FAIM transcript variants have been characterized to date, namely FAIM short (FAIM-S) and FAIM long (FAIM-L). [...]
2017 - 10.1371/journal.pone.0185327
PloS one, Vol. 12 Núm. 10 (october 2017) , p. e0185327
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