UAB Digital Repository of Documents 5 records found  Search took 0.01 seconds. 
1.
13 p, 4.4 MB Dissecting the contribution of Staphylococcus aureus α-phenol-soluble modulins to biofilm amyloid structure / Marinelli, Patrizia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Navarro, Susanna (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
The opportunistic pathogen Staphylococcus aureus is recognized as one of the most frequent causes of biofilm-associated infections. The recently discovered phenol soluble modulins (PSMs) are small α-helical amphipathic peptides that act as the main molecular effectors of staphylococcal biofilm maturation, promoting the formation of an extracellular fibril structure with amyloid-like properties. [...]
2016 - 10.1038/srep34552
Scientific reports, Vol. 6 (2016) , art. 34552  
2.
14 p, 3.5 MB The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria / Navarro, Susanna (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Marinelli, Patrizia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Díaz-Caballero, Marta (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Background: rhe 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-43 or FUS, are being found to aggregate in different neurodegenerative disorders. [...]
2015 - 10.1186/s12934-015-0284-7
Microbial cell factories, Vol. 14 (2015) , art. 102  
3.
10 p, 1.2 MB A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation / Marinelli, Patrizia (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) ; Graña Montes, Ricardo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Bañó-Polo, Manuel (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Fernández Gallegos, María Rosario (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Papaleo, Elena (Kræftens Bekæmpelse) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Oxidatively modified forms of proteins accumulate during aging. Oxidized protein conformers might act as intermediates in the formation of amyloids in age-related disorders. However, it is not known whether this amyloidogenic conversion requires an extensive protein oxidative damage or it can be promoted just by a discrete, localized post-translational modification of certain residues. [...]
2017 - 10.1016/j.redox.2017.10.022
Redox biology, Vol. 14 (April 2018) , p. 566-575  
4.
15 p, 1.8 MB Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF Domain / Marinelli, Patrizia ; Castillo Cano, Virginia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Amyloid fibril formation is implicated in different human diseases. The transition between native α-helices and nonnative intermolecular β-sheets has been suggested to be a trigger of fibrillation in different conformational diseases. [...]
2013 - 10.3390/ijms140917830
International journal of molecular sciences, Vol. 14 Núm. 9 (August 2013) , p. 17830-17844  
5.
215 p, 7.5 MB From sequence to structure : determinants of functional and non-functional protein aggregation / Marinelli, Patrizia ; Ventura, Salvador, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Navarro, Susanna, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
El estudio de la agregación proteica representa un campo de investigación desafiante que abarca tanto el área biomédica como la biotecnológica. El creciente número de enfermedades humanas asociadas a la acumulación de agregados amiloides, así como la formación de depósitos intracelulares durante la producción recombinante de proteínas terapéuticas en modelos celulares ha impulsado la investigación para comprender y desarrollar estrategias contra la agregación de proteínas. [...]
The study of protein aggregation represents a challenging research field which embraces from biomedical to biotechnological areas. The growing number of human diseases associated to the deposition of amyloid aggregates as well as the formation of intracellular protein deposits during the recombinant production of therapeutic proteins in cell factories has pushed the research to understand and develop strategies against protein aggregation. [...]

Bellaterra : Universitat Autònoma de Barcelona, 2015  

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