Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers.
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Anti-prion drug mPPIg5 inhibits PrP(C) conversion to PrP(Sc)Nanoparticles as catalysts for protein fibrillation.Complex polyamines: unique prion disaggregating compounds.Dendrimers as therapeutic agents: a systematic review.Nanomaterials for reducing amyloid cytotoxicity.Membrane Disruption Mechanism of a Prion Peptide (106-126) Investigated by Atomic Force Microscopy, Raman and Electron Paramagnetic Resonance Spectroscopy.Nanomedicine for prion disease treatment: new insights into the role of dendrimersEffects of lipid composition and phase on the membrane interaction of the prion peptide 106-126 amide.Amidation and structure relaxation abolish the neurotoxicity of the prion peptide PrP106-126 in vivo and in vitro.Unexpected Biological Applications of Dendrimers and Specific Multivalency Activities
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P2860
Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年學術文章
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name
Amyloid aggregates of the prio ...... d by the action of dendrimers.
@en
Amyloid aggregates of the prio ...... d by the action of dendrimers.
@nl
type
label
Amyloid aggregates of the prio ...... d by the action of dendrimers.
@en
Amyloid aggregates of the prio ...... d by the action of dendrimers.
@nl
prefLabel
Amyloid aggregates of the prio ...... d by the action of dendrimers.
@en
Amyloid aggregates of the prio ...... d by the action of dendrimers.
@nl
P2093
P2860
P1433
P1476
Amyloid aggregates of the prio ...... d by the action of dendrimers.
@en
P2093
Heidi Gertz Pedersen
James Flink
Peter M H Heegaard
Ulrik Boas
P2860
P304
P356
10.1016/J.FEBSLET.2004.09.073
P407
P577
2004-11-01T00:00:00Z