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A cationic tetrapyrrole inhibits toxic activities of the cellular prion protein.Interaction between Prion Protein's Copper-Bound Octarepeat Domain and a Charged C-Terminal Pocket Suggests a Mechanism for N-Terminal Regulation.The amyloid fold of Gad m 1 epitopes governs IgE binding.The prion protein family member Shadoo induces spontaneous ionic currents in cultured cells.Melanin or a Melanin-Like Substance Interacts with the N-Terminal Portion of Prion Protein and Inhibits Abnormal Prion Protein Formation in Prion-Infected Cells.Cation-π interactions in CREBBP bromodomain inhibition: an electrostatic model for small-molecule binding affinity and selectivity.Amyloid Assembly Endows Gad m 1 with Biomineralization Properties.
P2860
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P2860
description
2015 nî lūn-bûn
@nan
2015年の論文
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2015年論文
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2015年論文
@zh-hant
2015年論文
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2015年論文
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2015年論文
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2015年论文
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2015年论文
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2015年论文
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name
PrP charge structure encodes interdomain interactions
@ast
PrP charge structure encodes interdomain interactions
@en
type
label
PrP charge structure encodes interdomain interactions
@ast
PrP charge structure encodes interdomain interactions
@en
prefLabel
PrP charge structure encodes interdomain interactions
@ast
PrP charge structure encodes interdomain interactions
@en
P2093
P2860
P356
P1433
P1476
PrP charge structure encodes interdomain interactions
@en
P2093
Adriano Aguzzi
Ilia V Baskakov
Milagros Castellanos
Natallia Makarava
Rosa Sánchez
P2860
P2888
P356
10.1038/SREP13623
P407
P577
2015-09-01T00:00:00Z