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PMEL Amyloid Fibril Formation: The Bright Steps of PigmentationStructure and dynamics of amyloid-β segmental polymorphismsSolid-State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well-Ordered β-Sheet Core Amidst Structural HeterogeneityDistinct prion strains are defined by amyloid core structure and chaperone binding site dynamics.Characterization of prion-like conformational changes of the neuronal isoform of Aplysia CPEBMolecular origin of pH-dependent fibril formation of a functional amyloidPhysical and structural basis for polymorphism in amyloid fibrilsLysophospholipid-containing membranes modulate the fibril formation of the repeat domain of a human functional amyloid, pmel17.Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure informationOn the problem of resonance assignments in solid state NMR of uniformly ¹⁵N,¹³C-labeled proteins.Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue levelEfficient resonance assignment of proteins in MAS NMR by simultaneous intra- and inter-residue 3D correlation spectroscopy.Molecular structures of amyloid and prion fibrils: consensus versus controversyPMEL: a pigment cell-specific model for functional amyloid formationAmyloid-based nanosensors and nanodevices.Amyloidosis in alkaptonuria.Resonance assignment of the NMR spectra of disordered proteins using a multi-objective non-dominated sorting genetic algorithm.Cystatin-related epididymal spermatogenic subgroup members are part of an amyloid matrix and associated with extracellular vesicles in the mouse epididymal lumen.Critical Influence of Cosolutes and Surfaces on the Assembly of Serpin-Derived Amyloid Fibrils.Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Reversing the amyloid trend: Mechanism of fibril assembly and dissolution of the repeat domain from a human functional amyloid.Identification of an amyloid fibril forming segment of human Pmel17 repeat domain (RPT domain).A β-solenoid model of the Pmel17 repeat domain: insights to the formation of functional amyloid fibrils.Transition Dipoles from 1D and 2D Infrared Spectroscopy Help Reveal the Secondary Structures of Proteins: Application to Amyloids.What Does Solid-State NMR Tell Us about Amyloid Structures?
P2860
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P2860
description
2011 nî lūn-bûn
@nan
2011 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Segmental polymorphism in a functional amyloid.
@ast
Segmental polymorphism in a functional amyloid.
@en
type
label
Segmental polymorphism in a functional amyloid.
@ast
Segmental polymorphism in a functional amyloid.
@en
prefLabel
Segmental polymorphism in a functional amyloid.
@ast
Segmental polymorphism in a functional amyloid.
@en
P2860
P1433
P1476
Segmental polymorphism in a functional amyloid.
@en
P2093
Kan-Nian Hu
Ryan P McGlinchey
P2860
P304
P356
10.1016/J.BPJ.2011.09.051
P407
P577
2011-11-01T00:00:00Z