Localized structural fluctuations promote amyloidogenic conformations in transthyretin.
about
Mechanisms of amyloid formation revealed by solution NMRThermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways.Uncovering the Mechanism of Aggregation of Human Transthyretin.Substoichiometric inhibition of transthyretin misfolding by immune-targeting sparsely populated misfolding intermediates: a potential diagnostic and therapeutic for TTR amyloidoses.Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.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.Transthyretin and BRICHOS: The Paradox of Amyloidogenic Proteins with Anti-Amyloidogenic Activity for Aβ in the Central Nervous System.Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein.Transthyretin Suppresses Amyloid-β Secretion by Interfering with Processing of the Amyloid-β Protein PrecursorFluorotryptophan Incorporation Modulates the Structure and Stability of Transthyretin in a Site-Specific Manner.Pathogenic Mutations Induce Partial Structural Changes in the Native β-Sheet Structure of Transthyretin and Accelerate Aggregation.Structure of Monomeric Transthyretin Carrying the Clinically Important T119M Mutation.Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies.FRET studies of various conformational states adopted by transthyretin.Q-Rich Yeast Prion [PSI+] Accelerates Aggregation of Transthyretin, a Non-Q-Rich Human Protein.Dynamics and Thermodynamics of Transthyretin Association from Molecular Dynamics Simulations.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
Localized structural fluctuations promote amyloidogenic conformations in transthyretin.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Localized structural fluctuations promote amyloidogenic conformations in transthyretin.
@ast
Localized structural fluctuations promote amyloidogenic conformations in transthyretin.
@en
type
label
Localized structural fluctuations promote amyloidogenic conformations in transthyretin.
@ast
Localized structural fluctuations promote amyloidogenic conformations in transthyretin.
@en
prefLabel
Localized structural fluctuations promote amyloidogenic conformations in transthyretin.
@ast
Localized structural fluctuations promote amyloidogenic conformations in transthyretin.
@en
P2860
P50
P1476
Localized structural fluctuations promote amyloidogenic conformations in transthyretin.
@en
P2093
Kwang Hun Lim
P2860
P304
P356
10.1016/J.JMB.2013.01.008
P407
P577
2013-01-11T00:00:00Z