Increased Aggregation Is More Frequently Associated to Human Disease-Associated Mutations Than to Neutral Polymorphisms
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Title
Increased Aggregation Is More Frequently Associated to Human Disease-Associated Mutations Than to Neutral Polymorphisms
Authors
Keywords
Protein domains, Mutation databases, Protein aggregation, Globular proteins, Pathogens, Protein structure, Intrinsically disordered proteins, Thermodynamics
Journal
PLoS Computational Biology
Volume 11, Issue 9, Pages e1004374
Publisher
Public Library of Science (PLoS)
Online
2015-09-05
DOI
10.1371/journal.pcbi.1004374
References
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- (2012) Della C. David Frontiers in Genetics
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