The structural intolerance of the PrP alpha-fold for polar substitution of the helix-3 methionines.
about
Sup35 methionine oxidation is a trigger for de novo [PSI(+)] prion formationSelenomethionine incorporation into amyloid sequences regulates fibrillogenesis and toxicityOxidation of Helix-3 methionines precedes the formation of PK resistant PrP.Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.PrP charge structure encodes interdomain interactionsAtomic force fluorescence microscopy in the characterization of amyloid fibril assembly and oligomeric intermediatesPolar substitutions in helix 3 of the prion protein produce transmembrane isoforms that disturb vesicle trafficking.Failure of prion protein oxidative folding guides the formation of toxic transmembrane forms.Impact of methionine oxidation as an initial event on the pathway of human prion protein conversion.
P2860
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P2860
The structural intolerance of the PrP alpha-fold for polar substitution of the helix-3 methionines.
description
2010 nî lūn-bûn
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2010年の論文
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name
The structural intolerance of ...... on of the helix-3 methionines.
@en
The structural intolerance of ...... on of the helix-3 methionines.
@nl
type
label
The structural intolerance of ...... on of the helix-3 methionines.
@en
The structural intolerance of ...... on of the helix-3 methionines.
@nl
prefLabel
The structural intolerance of ...... on of the helix-3 methionines.
@en
The structural intolerance of ...... on of the helix-3 methionines.
@nl
P50
P1476
The structural intolerance of ...... on of the helix-3 methionines.
@en
P2093
Ruth Gabizon
Silvia Lisa
P2888
P304
P356
10.1007/S00018-010-0363-1
P577
2010-05-09T00:00:00Z