|
1.
|
|
12 p, 5.7 MB |
Protein-only Nanoparticles for T Cell Expansion and Activation
/
Fornt Suñé, Marc (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Lázaro Bermejo, Gonzalo (Universitat Autònoma de Barcelona. Departament de Biologia Cel·lular, de Fisiologia i d'Immunologia) ;
Gil Garcia, Marcos (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Aran, Andrea (Universitat Autònoma de Barcelona. Departament de Biologia Cel·lular, de Fisiologia i d'Immunologia) ;
Garcia Pardo, Javier (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ;
Martí, Mercè (Universitat Autònoma de Barcelona. Departament de Biologia Cel·lular, de Fisiologia i d'Immunologia) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
The in vitro expansion and activation of T cells utilizing synthetic nanosized artificial antigen presenting cells (aAPCs) have emerged as a promising technique for cancer treatment. Although diverse nanomaterials have been explored as aAPC scaffolds, protein-only nanoparticles have been largely overlooked, despite their high designability and biocompatibility. [...]
2024 -  10.1021/acsanm.4c00698
ACS applied nano materials, Vol. 7 Núm. 6 (22 2024) , p. 6669-6680
|
|
|
2.
|
|
|
3.
|
|
12 p, 2.9 MB |
Cryo-EM structure of hnRNPDL-2 fibrils, a functional amyloid associated with limb-girdle muscular dystrophy D3
/
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
|
|
|
4.
|
|
172 p, 7.7 MB |
Design of improved therapeutic proteins and novel protein-based nanomaterials
/
Gil Garcia, Marcos ;
Ventura Zamora, Salvador, dir.
Les proteïnes estan involucrades en innombrables processos biològics com catàlisis, transport, regulació, defensa i estructura cel·lular. Per a poder dur a terme aquestes funcions, la gran majoria d'elles necessiten plegar-se en una estructura 3D definida. [...]
Las proteínas están involucradas en innumerables procesos biológicos como catálisis, transporte, regulación, defensa y estructura celular. Para poder llevar a cabo estas funciones, la gran mayoría de ellas necesitan plegarse en una estructura 3D definida. [...]
Proteins are involved in a myriad of biological processes such as catalysis, transport, regulation, defense, and providing structure to the cell. Most proteins need to fold into a defined 3D structure to perform such functions. [...]
2022
|
|
|
5.
|
|
|
6.
|
|
|
7.
|
|
|
8.
|
|
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 Recerca Biomèdica) ;
Iglesias, Valentin (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
J. Lynch, Cian (Institut de Recerca Biomèdica) ;
Gil Garcia, Marcos (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Serrano, Manuel (Institut de Recerca Biomèdica) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
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
|
|
|
9.
|
|
16 p, 2.9 MB |
Coiled-coil inspired functional inclusion bodies
/
Gil Garcia, Marcos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Navarro, Susanna (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")
Recombinant protein expression in bacteria often leads to the formation of intracellular insoluble protein deposits, a major bottleneck for the production of soluble and active products. However, in recent years, these bacterial protein aggregates, commonly known as inclusion bodies (IBs), have been shown to be a source of stable and active protein for biotechnological and biomedical applications. [...]
2020 - 10.1186/s12934-020-01375-4
Microbial cell factories, Vol. 19 (June 2020) , art. 117
|
|
|
10.
|
|
16 p, 3.8 MB |
Disulfide driven folding for a conditionally disordered protein
/
Fraga, Hugo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Pujols Pujol, Jordi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Gil Garcia, Marcos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Roque Córdova, Alicia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Bernardo-Seisdedos, Ganeko (CIC BioGUNE) ;
Santambrogio, Carlo (University of Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ;
Bech-Serra, Joan-Josep (Vall d'Hebron Institut d'Oncologia) ;
Canals, Francesc (Vall d'Hebron Institut d'Oncologia) ;
Bernadó, Pau (Centre de biochimie Structurale (Montpellier)) ;
Grandori, Rita (University of Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ;
Millet, Oscar (CIC BioGUNE) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Conditionally disordered proteins are either ordered or disordered depending on the environmental context. The substrates of the mitochondrial intermembrane space (IMS) oxidoreductase Mia40 are synthesized on cytosolic ribosomes and diffuse as intrinsically disordered proteins to the IMS, where they fold into their functional conformations; behaving thus as conditionally disordered proteins. [...]
2017 - 10.1038/s41598-017-17259-4
Scientific reports, Vol. 7 (2017) , art. 16994
|
|
visitant ::
identificació
alerta personal via correu electrònic o subscribiu-vos al 
canal RSS.
