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Tracking protein aggregate interactions
University of California San Diego.
Creighton University.
Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry. Linköping University, The Institute of Technology.ORCID iD: 0000-0002-5582-140X
2011 (English)In: PRION, ISSN 1933-6896, Vol. 5, no 2, 52-55 p.Article in journal (Refereed) Published
Abstract [en]

Amyloid fibrils share a structural motif consisting of highly ordered beta-sheets aligned perpendicular to the fibril axis.(1,2) At each fibril end, beta-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.

Place, publisher, year, edition, pages
Landes Bioscience , 2011. Vol. 5, no 2, 52-55 p.
Keyword [en]
prion; prions; strain; TSE; interaction; amyloid; LCP; neurodegeneration; aggregation
National Category
Engineering and Technology
URN: urn:nbn:se:liu:diva-69920DOI: 10.4161/pri.5.2.16173ISI: 000292724200002OAI: diva2:433194
Available from: 2011-08-09 Created: 2011-08-08 Last updated: 2014-04-08

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Nilsson, Peter
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Organic ChemistryThe Institute of Technology
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