Data on correlation between Aβ42 structural aggregation propensity and toxicity in bacteria
Carija, Anita (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)

Date:	2016
Abstract:	Protein aggregation and amyloid formation is a hallmark of an increasing number of human disorders. Because protein aggregation is deleterious for the cell physiology and results in a decrease in overall cell fitness, it is thought that natural selection acts to purify aggregating proteins during evolution. This data article contains complementary figures and results related to the research article entitled "Selection against toxic aggregation-prone protein sequences in bacteria" (Navarro et al. , 2014) . Here, we used the AGGRESCAN3D (A3D) server, a novel in house predictor that forecasts protein aggregation properties in protein structures to illustrate a striking correlation between the structure-based predictions of aggregation propensities for Alzheimer's Aβ42 peptide variants and their previously reported deleterious effects in bacteria.
Grants:	Ministerio de Economía y Competitividad BFU2013-44763-P
Rights:	Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.
Language:	Anglès
Document:	Article ; recerca ; Versió publicada
Published in:	Data in brief, Vol. 7 (february 2016) , p. 143-147, ISSN 2352-3409

DOI: 10.1016/j.dib.2016.02.017
PMID: 27408907

5 p, 351.1 KB

The record appears in these collections:
Articles > Research articles
Articles > Published articles