(Q57014255)

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In silico studies and fluorescence binding assays of potential anti-prion compounds reveal an important binding site for prion inhibition from PrPC to PrPSc

scientific article published on 15 July 2014

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10 March 2020

In silico studies and fluorescence binding assays of potential anti-prion compounds reveal an important binding site for prion inhibition from PrP(C) to PrP(Sc) (English)

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10 March 2020

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Nataraj S Pagadala

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10 March 2020

Rolando Perez Pineiro

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10 March 2020

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10 March 2020

Jack Tuszyński

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10 March 2020

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Nataraj S. Pagadala

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Rolando Perez-Pineiro

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Jack A. Tuszynski

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15 July 2014

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10 March 2020

European Journal of Medicinal Chemistry

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10 March 2020

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10 March 2020

118-131

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10 March 2020

Structural Domains and Main-Chain Flexibility in Prion Proteins†

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Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics

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The conversion of helix H2 to beta-sheet is accelerated in the monomer and dimer of the prion protein upon T183A mutation

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The antimalarials quinacrine and chloroquine induce weak lysosomal storage of sulphated glycosaminoglycans in cell culture and in vivo

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Checking the pH-induced conformational transition of prion protein by molecular dynamics simulations: effect of protonation of histidine residues

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The oligomerization properties of prion protein are restricted to the H2H3 domain

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Identifiers

10.1016/J.EJMECH.2014.07.045

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25042003%20AND%20SRC:MED&resulttype=core&format=json

10 March 2020

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25042003%20AND%20SRC:MED&resulttype=core&format=json

10 March 2020

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