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8 p, 4.8 MB |
Protein features instruct the secretion dynamics from metal-supported synthetic amyloids
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Parladé Molist, Eloi (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Sanchez, Julieta M (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
López-Laguna, Hèctor (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Unzueta Elorza, Ugutz (Institut d'Investigació Biomèdica Sant Pau) ;
Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Vázquez Gómez, Esther (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia)
Hexahistidine-tagged proteins can be clustered by divalent cations into self-containing, dynamic protein depots at the microscale, which under physiological conditions leak functional protein. While such protein granules show promise in clinics as time-sustained drug delivery systems, little is known about how the nature of their components, that is, the protein and the particular cation used as cross-linker, impact on the disintegration of the material and on its secretory performance. [...]
2023 - 10.1016/j.ijbiomac.2023.126164
International journal of biological macromolecules, Vol. 250 (October 2023) , art. 126164
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12 p, 2.0 MB |
The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies
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Sánchez, Julieta María (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Carratalá, José Vicente (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Serna, Naroa (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Unzueta Elorza, Ugutz (Institut d'Investigació Biomèdica Sant Pau) ;
Nolan, Verónica (Universidad Nacional de Córdoba. Departamento de Química) ;
Sánchez Chardi, Alejandro (Universitat Autònoma de Barcelona. Servei de Microscòpia) ;
Voltà-Durán, Eric (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
López-Laguna, Hèctor (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Ferrer-Miralles, Neus (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Vázquez Gómez, Esther (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Institut Germans Trias i Pujol. Institut de Recerca contra la Leucèmia Josep Carreras
The coordination between histidine-rich peptides and divalent cations supports the formation of nano- and micro-scale protein biomaterials, including toxic and non-toxic functional amyloids, which can be adapted as drug delivery systems. [...]
2022 - 10.3390/pharmaceutics14030602
Pharmaceutics, Vol. 14, Issue 3 (March 2022) , art. 602
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21 p, 5.3 MB |
Pathological ATX3 Expression Induces Cell Perturbations in E. coli as Revealed by Biochemical and Biophysical Investigations
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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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62 p, 1.5 MB |
Bacterial inclusion bodies are industrially exploitable amyloids
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de Marco, Ario (University of Nova Gorica. Laboratory for Environmental and Life Sciences (Slovenia)) ;
Ferrer-Miralles, Neus (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Garcia-Fruitos, Elena (Institut de Recerca i Tecnologia Agroalimentàries) ;
Mitraki, Anna (University of Crete. Department of Materials Science and Technology (Greece)) ;
Peternel, Spela (Lupinica (Slovenia)) ;
Rinas, Ursula (Leibniz University of Hannover. Technical Chemistry and Life Science (Germany)) ;
Trujillo-Roldán, Mauricio A. (Universidad Nacional Autónoma de México. Instituto de Investigaciones Biomédicas) ;
Valdez-Cruz, Norma A. (Universidad Nacional Autónoma de México. Instituto de Investigaciones Biomédicas) ;
Vázquez Gómez, Esther (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Universitat Autònoma de Barcelona.
Departament de Genètica i de Microbiologia
Understanding the structure, functionalities and biology of functional amyloids is an issue of emerging interest. Inclusion bodies, namely protein clusters formed in recombinant bacteria during protein production processes, have emerged as unanticipated, highly tunable models for the scrutiny of the physiology and architecture of functional amyloids. [...]
2019 - 10.1093/femsre/fuy038
FEMS Microbiology Reviews, Vol. 43, Issue 1 (January 2019) , p. 53-72
7 documents
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10 p, 2.9 MB |
Prion domains as a driving force for the assembly of functional nanomaterials
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Wang, Weiqiang (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")
Amyloids display a highly ordered fibrillar structure. Many of these assemblies appear associated with human disease. However, the controllable, stable, tunable, and robust nature of amyloid fibrils can be exploited to build up remarkable nanomaterials with a wide range of applications in biomedicine and biotechnology. [...]
2020 - 10.1080/19336896.2020.1785659
Prion, Vol. 14, issue 1 (2020) , p. 170-179
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16 p, 3.8 MB |
Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria
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Macedo, Bruno (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") ;
Navarro, Susanna (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Cordeiro, Yraima (Universidade Federal do Rio de Janeiro. Faculdade de Farmácia) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Background: An increasing number of proteins are being shown to assemble into amyloid structures that lead to pathological states. Among them, mammalian prions outstand due to their ability to transmit the pathogenic conformation, becoming thus infectious. [...]
2015 - 10.1186/s12934-015-0361-y
Microbial cell factories, Vol. 14 (2015) , art. 174
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