Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies. - Wikidata - awgldk - TriplyDB

Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies.

Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies.

http://www.wikidata.org/entity/Q42550081

about

D-strand perturbation and amyloid propensity in beta-2 microglobulin Conformational Conversion during Amyloid Formation at Atomic Resolution Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR.A general Monte Carlo/simulated annealing algorithm for resonance assignment in NMR of uniformly labeled biopolymers Solid-state NMR studies of metal-free SOD1 fibrillar structures.High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .4D solid-state NMR for protein structure determination.Polymorphism of β2-microglobulin amyloid fibrils manifested by ultrasonication-enhanced fibril formation in trifluoroethanol Distinct prion strains are defined by amyloid core structure and chaperone binding site dynamics.Physical and structural basis for polymorphism in amyloid fibrils Structural evolution of Iowa mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth High-field dynamic nuclear polarization with high-spin transition metal ions.Structural insights into functional and pathological amyloid.Structural insights into the pre-amyloid tetramer of β-2-microglobulin from covalent labeling and mass spectrometry Structured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites.Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions.Segmental polymorphism in a functional amyloid.pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils.High resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR.Efficient resonance assignment of proteins in MAS NMR by simultaneous intra- and inter-residue 3D correlation spectroscopy.Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.Both the cis-trans equilibrium and isomerization dynamics of a single proline amide modulate β2-microglobulin amyloid assembly.Conformational stability of mammalian prion protein amyloid fibrils is dictated by a packing polymorphism within the core region.Understanding the complex mechanisms of β2-microglobulin amyloid assembly.Distinguishing closely related amyloid precursors using an RNA aptamer.Ligand binding to distinct states diverts aggregation of an amyloid-forming protein.Chiral recognition in amyloid fiber growth.Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.Intermolecular alignment in β2-microglobulin amyloid fibrils.Direct observation of minimum-sized amyloid fibrils using solution NMR spectroscopy.Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy.Morphological differences between β(2) -microglobulin in fibrils and inclusion bodies.Domain swapping and amyloid fibril conformation.Immunoglobulin Light Chains Form an Extensive and Highly Ordered Fibril Involving the N- and C-Termini.Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.Pathogenic Mutations Induce Partial Structural Changes in the Native β-Sheet Structure of Transthyretin and Accelerate Aggregation.On the use of ultracentrifugal devices for sedimented solute NMR.SedNMR: a web tool for optimizing sedimentation of macromolecular solutes for SSNMR.A hypothetical hierarchical mechanism of the self-assembly of the Escherichia coli RNA polymerase σ(70) subunit.

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P2860

Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies.

http://www.wikidata.org/entity/Q42550081

description

2010 nî lūn-bûn

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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2010年论文

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2010年论文

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name

Magic angle spinning NMR analy ...... in two distinct morphologies.

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Magic angle spinning NMR analy ...... in two distinct morphologies.

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Magic angle spinning NMR analy ...... in two distinct morphologies.

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type

label

Magic angle spinning NMR analy ...... in two distinct morphologies.

@en

Magic angle spinning NMR analy ...... in two distinct morphologies.

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Magic angle spinning NMR analy ...... in two distinct morphologies.

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prefLabel

Magic angle spinning NMR analy ...... in two distinct morphologies.

@en

Magic angle spinning NMR analy ...... in two distinct morphologies.

@en-gb

Magic angle spinning NMR analy ...... in two distinct morphologies.

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Journal of the American Chemical Society

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Magic angle spinning NMR analy ...... in two distinct morphologies.

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Galia T Debelouchina

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Geoffrey W Platt

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Robert G Griffin

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P2860

Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation.

Structure of the cross-beta spine of amyloid-like fibrils

The structure and stability of an HLA-A*0201/octameric tax peptide complex with an empty conserved peptide-N-terminal binding site

The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transition

Crystal structure of monomeric human -2-microglobulin reveals clues to its amyloidogenic properties

Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy

beta2-microglobulin H31Y variant 3D structure highlights the protein natural propensity towards intermolecular aggregation

High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy

High-resolution crystal structure of beta2-microglobulin formed at pH 7.0

Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core

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scholarly article

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10.1021/JA102775U

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30

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Marvin J. Bayro

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2010-08-01T00:00:00Z

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45387490

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2919207

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