Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.
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MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors.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.Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.NMR Measurements Reveal the Structural Basis of Transthyretin Destabilization by Pathogenic MutationsKinetic analysis of the multistep aggregation pathway of human transthyretin
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Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 07 September 2016
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.
@en
Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.
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label
Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.
@en
Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.
@nl
prefLabel
Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.
@en
Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.
@nl
P2093
P2860
P50
P1433
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Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid
@en
P2093
Anvesh K R Dasari
David E Wemmer
Kwang Hun Lim
Peter E Wright
P2860
P304
P356
10.1021/ACS.BIOCHEM.6B00649
P407
P577
2016-09-07T00:00:00Z