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Resultats globals: 2 registres trobats en 0.04 segons.
Articles, 2 registres trobats
Articles 2 registres trobats  
1.
15 p, 1.9 MB The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain / Castillo Cano, Virginia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Chiti, Fabrizio (Università di Firenze. Dipartimento di Scienze Biochimiche) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Background: Protein aggregation is linked to the onset of an increasing number of human nonneuropathic (either localized or systemic) and neurodegenerative disorders. In particular, misfolding of native α-helical structures and their self-assembly into nonnative intermolecular β-sheets has been proposed to trigger amyloid fibril formation in Alzheimer's and Parkinson's diseases. [...]
2013 - 10.1371/journal.pone.0058297
PloS one, Vol. 8 issue 3 (2013) , art. e58297  
Registre complet - Creative Commons
2.
16 p, 1.6 MB Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases / Castillo Cano, Virginia (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")
Protein aggregation underlies a wide range of human disorders. The polypeptides involved in these pathologies might be intrinsically unstructured or display a defined 3D-structure. Little is known about how globular proteins aggregate into toxic assemblies under physiological conditions, where they display an initially folded conformation. [...]
2009 - 10.1371/journal.pcbi.1000476
PLOS Computational Biology, Vol. 5, Issue 8 (August 2009) , p. e1000476  
Registre complet - Creative Commons

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