Copper alters aggregation behavior of prion protein and induces novel interactions between its N- and C-terminal regions.
about
Solvent microenvironments and copper binding alters the conformation and toxicity of a prion fragmentUtilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.PrP overdrive: does inhibition of α-cleavage contribute to PrP(C) toxicity and prion disease?Cellular prion protein and NMDA receptor modulation: protecting against excitotoxicity.Insect cell-derived cofactors become fully functional after proteinase K and heat treatment for high-fidelity amplification of glycosylphosphatidylinositol-anchored recombinant scrapie and BSE prion proteins.Octarepeat region flexibility impacts prion function, endoproteolysis and disease manifestationDynamic Clustering of the Bacterial Sensory Kinase BaeSPrP charge structure encodes interdomain interactionsCopper-induced structural conversion templates prion protein oligomerization and neurotoxicity.Zinc drives a tertiary fold in the prion protein with familial disease mutation sites at the interfaceInteraction between Prion Protein's Copper-Bound Octarepeat Domain and a Charged C-Terminal Pocket Suggests a Mechanism for N-Terminal Regulation.A new paradigm for enzymatic control of α-cleavage and β-cleavage of the prion protein.The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling ModulesCharacterization of biometal profiles in neurological disorders.Expression of Tyrosine Hydroxylase is Negatively Regulated Via Prion Protein.Dopamine induces the accumulation of insoluble prion protein and affects autophagic flux.Biophysical and morphological studies on the dual interaction of non-octarepeat prion protein peptides with copper and nucleic acids.Substitutions of PrP N-terminal histidine residues modulate scrapie disease pathogenesis and incubation time in transgenic mice.Epitope scanning indicates structural differences in brain-derived monomeric and aggregated mutant prion proteins related to genetic prion diseases.
P2860
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P2860
Copper alters aggregation behavior of prion protein and induces novel interactions between its N- and C-terminal regions.
description
2011 nî lūn-bûn
@nan
2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Copper alters aggregation beha ...... its N- and C-terminal regions.
@ast
Copper alters aggregation beha ...... its N- and C-terminal regions.
@en
type
label
Copper alters aggregation beha ...... its N- and C-terminal regions.
@ast
Copper alters aggregation beha ...... its N- and C-terminal regions.
@en
prefLabel
Copper alters aggregation beha ...... its N- and C-terminal regions.
@ast
Copper alters aggregation beha ...... its N- and C-terminal regions.
@en
P2093
P2860
P356
P1476
Copper alters aggregation beha ...... its N- and C-terminal regions.
@en
P2093
Abhay Kumar Thakur
Atul Kumar Srivastava
Chintalagiri Mohan Rao
Kandala Venkata Ramana Chary
Volety Srinivas
P2860
P304
38533-38545
P356
10.1074/JBC.M111.265645
P407
P577
2011-09-07T00:00:00Z