The Aggregation Free Energy Landscapes of Polyglutamine Repeats.
about
Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.Aggregation landscapes of Huntingtin exon 1 protein fragments and the critical repeat length for the onset of Huntington's disease.A Free Energy Barrier Caused by the Refolding of an Oligomeric Intermediate Controls the Lag Time of Amyloid Formation by hIAPP.Monomeric Huntingtin Exon 1 Has Similar Overall Structural Features for Wild-Type and Pathological Polyglutamine Lengths.Distinct oligomerization and fibrillization dynamics of amyloid core sequences of amyloid-beta and islet amyloid polypeptide.Looking at the Disordered Proteins through the Computational Microscope.
P2860
The Aggregation Free Energy Landscapes of Polyglutamine Repeats.
description
2016 nî lūn-bûn
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2016年の論文
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年學術文章
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2016年學術文章
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name
The Aggregation Free Energy Landscapes of Polyglutamine Repeats.
@en
The Aggregation Free Energy Landscapes of Polyglutamine Repeats.
@nl
type
label
The Aggregation Free Energy Landscapes of Polyglutamine Repeats.
@en
The Aggregation Free Energy Landscapes of Polyglutamine Repeats.
@nl
prefLabel
The Aggregation Free Energy Landscapes of Polyglutamine Repeats.
@en
The Aggregation Free Energy Landscapes of Polyglutamine Repeats.
@nl
P2860
P356
P1476
The Aggregation Free Energy Landscapes of Polyglutamine Repeats.
@en
P2093
MinYeh Tsai
Weihua Zheng
P2860
P304
15197-15203
P356
10.1021/JACS.6B08665
P407
P577
2016-10-27T00:00:00Z