Dissociation of recombinant prion protein fibrils into short protofilaments: implications for the endocytic pathway and involvement of the N-terminal domain.
about
Charge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids.Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and websPrP charge structure encodes interdomain interactionsMouse prion protein polymorphism Phe-108/Val-189 affects the kinetics of fibril formation and the response to seeding: evidence for a two-step nucleation polymerization mechanism.Novel insights into amylin aggregation.Direct observation of murine prion protein replication in vitro
P2860
Dissociation of recombinant prion protein fibrils into short protofilaments: implications for the endocytic pathway and involvement of the N-terminal domain.
description
2012 nî lūn-bûn
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2012年の論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年论文
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2012年论文
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name
Dissociation of recombinant pr ...... ment of the N-terminal domain.
@ast
Dissociation of recombinant pr ...... ment of the N-terminal domain.
@en
type
label
Dissociation of recombinant pr ...... ment of the N-terminal domain.
@ast
Dissociation of recombinant pr ...... ment of the N-terminal domain.
@en
prefLabel
Dissociation of recombinant pr ...... ment of the N-terminal domain.
@ast
Dissociation of recombinant pr ...... ment of the N-terminal domain.
@en
P2093
P2860
P356
P1433
P1476
Dissociation of recombinant pr ...... ment of the N-terminal domain.
@en
P2093
Michele A McGuirl
Roger A Moore
P2860
P304
P356
10.1021/BI300201E
P407
P577
2012-05-23T00:00:00Z