A model for non-obligate oligomer formation in protein aggregration.
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A prion-like mechanism for the propagated misfolding of SOD1 from in silico modeling of solvated near-native conformersA mechanism for propagated SOD1 misfolding from frustration analysis of a G85R mutant protein assembly.Altered dynamics upon oligomerization corresponds to key functional sites.An in silico study of the effect of SOD1 electrostatic loop dynamics on amyloid‑like filament formation.
P2860
A model for non-obligate oligomer formation in protein aggregration.
description
2015 nî lūn-bûn
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2015年の論文
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2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
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2015年论文
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2015年论文
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name
A model for non-obligate oligomer formation in protein aggregration.
@ast
A model for non-obligate oligomer formation in protein aggregration.
@en
type
label
A model for non-obligate oligomer formation in protein aggregration.
@ast
A model for non-obligate oligomer formation in protein aggregration.
@en
prefLabel
A model for non-obligate oligomer formation in protein aggregration.
@ast
A model for non-obligate oligomer formation in protein aggregration.
@en
P2860
P1476
A model for non-obligate oligomer formation in protein aggregration.
@en
P2093
Eamonn F Healy
P2860
P304
P356
10.1016/J.BBRC.2015.08.052
P407
P50
P577
2015-08-14T00:00:00Z