Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Marta Díaz-Caballero"'
Autor:
Susanna Navarro, Salvador Ventura, Francesc Teixidor, Francesca Peccati, Marta Díaz-Caballero, Miquel Nuez-Martínez, Mariona Sodupe, Luis Rodríguez-Santiago
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
instname
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
There is an increasing interest in synthetic systems that can execute bioinspired chemical reactions without requiring the complex structures that characterize enzymes in their components. The hierarchical self-assembly of peptides provides a means t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::152f43e4716c89547aadcd69c61a1552
http://hdl.handle.net/10261/239692
http://hdl.handle.net/10261/239692
Publikováno v:
Biomacromolecules
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
Altres ajuts: acords transformatius de la UAB Protein amyloid nanofibers provide a biocompatible platform for the development of functional nanomaterials. However, the functionalities generated up to date are still limited. Typical building blocks co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::056ba27110b7a8cf36bb8ebc57b775f1
https://ddd.uab.cat/record/250434
https://ddd.uab.cat/record/250434
Publikováno v:
Biomacromolecules. 21(6)
Amyloids are associated with human disease. However, they are also exploited by nature for functional purposes. Functional amyloids have inspired amyloid-based biomaterials for different nanotechnologies. Early soluble species in the fibrillation pat
Publikováno v:
Prion. 12:266-272
Protein misfolding and aggregation into highly ordered fibrillar structures have been traditionally associated with pathological processes. Nevertheless, nature has taken advantage of the particular properties of amyloids for functional purposes, lik
Combining Structural Aggregation Propensity and Stability Predictions To Redesign Protein Solubility
Autor:
Marcos Gil-Garcia, Salvador Ventura, Michał H. Jamróz, Nathalia Varejão, Sebastian Kmiecik, Manuel Bañó-Polo, Aleksander Kuriata, David Reverter, Marta Díaz-Caballero, Jara Lascorz, Bertrand Morel, Susanna Navarro
Publikováno v:
Molecular Pharmaceutics. 15:3846-3859
The aggregation propensity of each particular protein seems to be shaped by evolution according to its natural abundance in the cell. The production and downstream processing of recombinant polypeptides implies attaining concentrations that are order
Publikováno v:
ACS Nano. 12:5394-5407
Nature provides copious examples of self-assembling supramolecular nanofibers. Among them, amyloid structures have found amazing applications as advanced materials in fields such as biomedicine and nanotechnology. Prions are a singular subset of prot
Publikováno v:
Microbial Cell Factories
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
Background The formation of protein inclusions is connected to the onset of many human diseases. Human RNA binding proteins containing intrinsically disordered regions with an amino acid composition resembling those of yeast prion domains, like TDP-4
Aggregation propensity of neuronal receptors : potential implications in neurodegenerative disorders
Publikováno v:
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
Future Science OA
Universitat Autònoma de Barcelona
Future Science OA
Misfolding and aggregation of proteins in tissues is linked to the onset of a diverse set of human neurodegenerative disorders, including Alzheimer's and Parkinson's diseases. In these pathologies proteins usually aggregate into highly ordered and β
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c8955d9b1215b800210ba44b3d7c146
https://ddd.uab.cat/record/225162
https://ddd.uab.cat/record/225162