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Transition of the prion protein from a structured cellular form (PrPC) to the infectious scrapie agent (PrPSc)


Baral, Pravas K; Yin, Jiang; Aguzzi, Adriano; James, Michael N G (2019). Transition of the prion protein from a structured cellular form (PrPC) to the infectious scrapie agent (PrPSc). Protein Science, 28(12):2055-2063.

Abstract

Prion diseases in mammals are caused by a conformational transition of the cellular prion protein from its native conformation (PrPC ) to a pathological isoform called "prion protein scrapie" (PrPSc ). A molecular level of understanding of this conformational transition will be helpful in unveiling the disease etiology. Experimental structural biological techniques (NMR and X-ray crystallography) have been used to unravel the atomic level structural information for the prion and its binding partners. More than one hundred three-dimensional structures of the mammalian prions have been deposited in the protein databank. Structural studies on the prion protein and its structural transitions will deepen our understanding of the molecular basis of prion pathogenesis and will provide valuable guidance for future structure-based drug discovery endeavors.

Abstract

Prion diseases in mammals are caused by a conformational transition of the cellular prion protein from its native conformation (PrPC ) to a pathological isoform called "prion protein scrapie" (PrPSc ). A molecular level of understanding of this conformational transition will be helpful in unveiling the disease etiology. Experimental structural biological techniques (NMR and X-ray crystallography) have been used to unravel the atomic level structural information for the prion and its binding partners. More than one hundred three-dimensional structures of the mammalian prions have been deposited in the protein databank. Structural studies on the prion protein and its structural transitions will deepen our understanding of the molecular basis of prion pathogenesis and will provide valuable guidance for future structure-based drug discovery endeavors.

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Additional indexing

Item Type:Journal Article, refereed, further contribution
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Scopus Subject Areas:Life Sciences > Biochemistry
Life Sciences > Molecular Biology
Uncontrolled Keywords:Biochemistry, Molecular Biology
Language:English
Date:1 December 2019
Deposited On:20 Dec 2019 11:09
Last Modified:27 Dec 2020 08:13
Publisher:Wiley-Blackwell Publishing, Inc.
ISSN:0961-8368
OA Status:Closed
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1002/pro.3735
PubMed ID:31583788
Project Information:
  • : FunderSNSF
  • : Grant ID31003A_179040
  • : Project TitleThe prion protein in health and disease
  • : FunderH2020
  • : Grant ID670958
  • : Project TitleFunction and malfunction of the prion protein

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