Tracking protein aggregate interactions

Christina J. Sigurdson, Jason C. Bartz, K. Peter R Nilsson

Research output: Contribution to journalComment/debate

1 Citation (Scopus)

Abstract

Amyloid fibrils share a structural motif consisting of highly ordered β-sheets aligned perpendicular to the fibril axis. 1,2 At each fibril end, β-sheets provide a template for recruiting and converting monomers. 3 Different amyloid fibrils often co-occur in the same individual, yet whether a protein aggregate aids or inhibits the assembly of a heterologous protein is unclear. In prion disease, diverse prion aggregate structures, known as strains, are thought to be the basis of disparate disease phenotypes in the same species expressing identical prion protein sequences. 4-7 Here we explore the interactions reported to occur when two distinct prion strains occur together in the central nervous system.

Original languageEnglish
Pages (from-to)52-55
Number of pages4
JournalPrion
Volume5
Issue number2
DOIs
StatePublished - Apr 2011

Fingerprint

Prions
Amyloid
Prion Diseases
Central Nervous System
Neurology
Phenotype
Monomers
Proteins
Protein Aggregates
Prion Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cell Biology
  • Infectious Diseases
  • Cellular and Molecular Neuroscience

Cite this

Tracking protein aggregate interactions. / Sigurdson, Christina J.; Bartz, Jason C.; Nilsson, K. Peter R.

In: Prion, Vol. 5, No. 2, 04.2011, p. 52-55.

Research output: Contribution to journalComment/debate

Sigurdson, CJ, Bartz, JC & Nilsson, KPR 2011, 'Tracking protein aggregate interactions', Prion, vol. 5, no. 2, pp. 52-55. https://doi.org/10.4161/pri.5.2.16173
Sigurdson, Christina J. ; Bartz, Jason C. ; Nilsson, K. Peter R. / Tracking protein aggregate interactions. In: Prion. 2011 ; Vol. 5, No. 2. pp. 52-55.
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