Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
about
Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90.Major depressive disorder: insight into candidate cerebrospinal fluid protein biomarkers from proteomics studies.Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.Pathogenic Mutations Induce Partial Structural Changes in the Native β-Sheet Structure of Transthyretin and Accelerate Aggregation.Distribution of Amyloid-Like and Oligomeric Species from Protein Aggregation Kinetics.Structure of Monomeric Transthyretin Carrying the Clinically Important T119M Mutation.FRET studies of various conformational states adopted by transthyretin.Kinetic and structural comparison of a protein's cotranslational folding and refolding pathways.NMR Measurements Reveal the Structural Basis of Transthyretin Destabilization by Pathogenic MutationsKinetic analysis of the multistep aggregation pathway of human transthyretin
P2860
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P2860
Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
Structural Changes Associated ...... Solution and Solid-State NMR.
@en
type
label
Structural Changes Associated ...... Solution and Solid-State NMR.
@en
prefLabel
Structural Changes Associated ...... Solution and Solid-State NMR.
@en
P2093
P2860
P1433
P1476
Structural Changes Associated ...... Solution and Solid-State NMR.
@en
P2093
Anvesh K R Dasari
David E Wemmer
Jeffery W Kelly
Kwang Hun Lim
P2860
P304
P356
10.1021/ACS.BIOCHEM.6B00164
P407
P577
2016-03-21T00:00:00Z