A bioinformatics method for identifying Q/N-rich prion-like domains in proteins.

Academic Article

Abstract

  • Numerous proteins contain domains that are enriched in glutamine and asparagine residues, and aggregation of some of these proteins has been linked to both prion formation in yeast and a number of human diseases. Unfortunately, predicting whether a given glutamine/asparagine-rich protein will aggregate has proven difficult. Here we describe a recently developed algorithm designed to predict the aggregation propensity of glutamine/asparagine-rich proteins. We discuss the basis for the algorithm, its limitations, and usage of recently developed online and downloadable versions of the algorithm.
  • Authors

  • Ross, Eric D
  • MacLea, Kyle
  • Anderson, Charles
  • Ben-Hur, Asa
  • Status

    Publication Date

  • 2013
  • Published In

    Keywords

  • Algorithms
  • Asparagine
  • Computational Biology
  • Glutamine
  • Humans
  • Internet
  • Prions
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae
  • Sequence Analysis, Protein
  • Software
  • Digital Object Identifier (doi)

    Pubmed Id

  • 23719919
  • Start Page

  • 219
  • End Page

  • 228
  • Volume

  • 1017