Resultats globals: 3 registres trobats en 0.02 segons.
Articles, 2 registres trobats
Documents de recerca, 1 registres trobats
Articles 2 registres trobats  
1.
10 p, 1.2 MB A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation / Marinelli, Patrizia (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Graña Montes, Ricardo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Bañó-Polo, Manuel (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Fernández Gallegos, Ma. Rosario (María Rosario) (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Papaleo, Elena (Kræftens Bekæmpelse) ; Ventura i Zamora, Salvador (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  
2.
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 Biologia Molecular) ; Ventura i Zamora, 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  

Documents de recerca 1 registres trobats  
1.
215 p, 7.5 MB From sequence to structure : determinants of functional and non-functional protein aggregation / Marinelli, Patrizia ; Ventura i Zamora, Salvador, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Navarro Cantero, Susanna, dir (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i 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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