Glycosaminoglycan sulfation determines the biochemical properties of prion protein aggregates-Reference-Cited by-同舟云学术

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Glycosaminoglycan sulfation determines the biochemical properties of prion protein aggregates

Published:2015-02-20 Issue:7 Volume:25 Page:745-755
ISSN:1460-2423
Container-title:Glycobiology
language:en
Short-container-title:

Author:

Ellett Laura J,Coleman Bradley M,Shambrook Mitch C,Johanssen Vanessa A,Collins Steven J,Masters Colin L,Hill Andrew F,Lawson Victoria A

Publisher

Oxford University Press (OUP)

Subject

Biochemistry

Link

http://academic.oup.com/glycob/article-pdf/25/7/745/16786881/cwv014.pdf

Reference64 articles.

1. Binding of bovine prion protein to heparin: A fluorescence polarization study;Andrievskaia;Arch Biochem Biophys,2007

2. Prion rods contain an inert polysaccharide scaffold;Appel;Biol Chem,1999

3. Divergent heparin-induced fibrillation pathways of a prion amyloidogenic determinant;Bazar;Chembiochem,2010

4. Cellular heparan sulfate participates in the metabolism of prions;Ben-Zaken;J Biol Chem,2003

5. In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc);Bocharova;J Mol Biol,2005

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1. Genetic insights into drug targets for sporadic Creutzfeldt-Jakob disease: Integrative multi-omics analysis;Neurobiology of Disease;2024-09

2. Neuronal Ndst1 depletion accelerates prion protein clearance and slows neurodegeneration in prion infection;PLOS Pathogens;2023-09-25

3. NeuronalNdst1depletion accelerates prion protein clearance and slows neurodegeneration in prion infection;2023-06-20

4. Comparative analysis of heparin affecting the biochemical properties of chicken and murine prion proteins;PLOS ONE;2021-02-18

5. Liquid–liquid phase separation of full-length prion protein initiates conformational conversion in vitro;Journal of Biological Chemistry;2021-01

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