The polysaccharide scaffold of PrP 27-30 is a common compound of natural prions and consists of alpha-linked polyglucose.
about
Na+/K+-ATPase is present in scrapie-associated fibrils, modulates PrP misfolding in vitro and links PrP function and dysfunction.Uptake and degradation of protease-sensitive and -resistant forms of abnormal human prion protein aggregates by human astrocytes.The reconstitution of mammalian prion infectivity de novo.Branched chain mechanism of polymerization and ultrastructure of prion protein amyloid fibrils.The two faces of protein misfolding: gain- and loss-of-function in neurodegenerative diseases.A specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner.Structural requirements for efficient prion protein conversion: cofactors may promote a conversion-competent structure for PrP(C).In vitro conversion and seeded fibrillization of posttranslationally modified prion protein.
P2860
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P2860
The polysaccharide scaffold of PrP 27-30 is a common compound of natural prions and consists of alpha-linked polyglucose.
description
2005 nî lūn-bûn
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name
The polysaccharide scaffold of ...... s of alpha-linked polyglucose.
@en
The polysaccharide scaffold of ...... s of alpha-linked polyglucose.
@nl
type
label
The polysaccharide scaffold of ...... s of alpha-linked polyglucose.
@en
The polysaccharide scaffold of ...... s of alpha-linked polyglucose.
@nl
altLabel
The polysaccharide scaffold of ...... nsists of α-linked polyglucose
@en
prefLabel
The polysaccharide scaffold of ...... s of alpha-linked polyglucose.
@en
The polysaccharide scaffold of ...... s of alpha-linked polyglucose.
@nl
P2093
P2860
P50
P356
P1433
P1476
The polysaccharide scaffold of ...... s of alpha-linked polyglucose.
@en
P2093
Christian Dumpitak
Detlev Riesner
Nicole Weinmann
Sabine Metzger
P2860
P304
P356
10.1515/BC.2005.131
P577
2005-11-01T00:00:00Z