Structural complexity of a composite amyloid fibril. - sprookjes - yvandenbroek - TriplyDB

Structural complexity of a composite amyloid fibril.

Structural complexity of a composite amyloid fibril.

http://www.wikidata.org/entity/Q35302543

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Fibrillogenesis of huntingtin and other glutamine containing proteins Structural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the β-Sheet Core An Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase.Flexibility and Solvation of Amyloid-β Hydrophobic Core Fast Motions of Key Methyl Groups in Amyloid-β Fibrils.C-terminal domain swapping of SSB changes the size of the ssDNA binding site Demonstration of a common indole-based aromatic core in natural and synthetic eumelanins by solid-state NMR.Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.Physical and structural basis for polymorphism in amyloid fibrils Interplay of sequence, topology and termini charge in determining the stability of the aggregates of GNNQQNY mutants: a molecular dynamics study.Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue level Enhanced sensitivity by nonuniform sampling enables multidimensional MAS NMR spectroscopy of protein assemblies.A peptide study of the relationship between the collagen triple-helix and amyloid Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core Expanding the repertoire of amyloid polymorphs by co-polymerization of related protein precursors Molecular structures of amyloid and prion fibrils: consensus versus controversy The amyloid state of proteins in human diseases.Self-assembly of amphipathic β-sheet peptides: insights and applications.Amyloid-based nanosensors and nanodevices.Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy.Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements.Disaggregation of Amylin Aggregate by Novel Conformationally Restricted Aminobenzoic Acid containing α/β and α/γ Hybrid Peptidomimetics.Light and heat control over secondary structure and amyloid-like fiber formation in an overcrowded-alkene-modified Trp zipper.β-hairpin-mediated nucleation of polyglutamine amyloid formation.Domain swapping and amyloid fibril conformation.Structural characterization of the caveolin scaffolding domain in association with cholesterol-rich membranes.Exploring the sequence-structure relationship for amyloid peptides.Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides.Hierarchical organization from self-assembling disulfide macrocycles.Structural characterization of supramolecular assemblies by ¹³C spin dilution and 3D solid-state NMR.The molecular structure of Alzheimer β-amyloid fibrils formed in the presence of phospholipid vesicles.Energetics Underlying Twist Polymorphisms in Amyloid Fibrils.Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.On the use of ultracentrifugal devices for sedimented solute NMR.An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils.Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR.Inhibitory effect of hydrophobic fullerenes on the β-sheet-rich oligomers of a hydrophilic GNNQQNY peptide revealed by atomistic simulations

P2860

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P2860

Structural complexity of a composite amyloid fibril.

http://www.wikidata.org/entity/Q35302543

description

2011 nî lūn-bûn

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2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Structural complexity of a composite amyloid fibril.

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Structural complexity of a composite amyloid fibril.

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type

label

Structural complexity of a composite amyloid fibril.

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Structural complexity of a composite amyloid fibril.

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prefLabel

Structural complexity of a composite amyloid fibril.

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Structural complexity of a composite amyloid fibril.

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P1433

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P1433

Journal of the American Chemical Society

P1476

Structural complexity of a composite amyloid fibril.

@en

P2093

Józef R Lewandowski

http://www.w3.org/2001/XMLSchema#string

Mike Rigney

http://www.w3.org/2001/XMLSchema#string

Patrick C A van der Wel

http://www.w3.org/2001/XMLSchema#string

Robert G Griffin

http://www.w3.org/2001/XMLSchema#string

P2860

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

De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy.

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

Atomic structures of amyloid cross-beta spines reveal varied steric zippers

Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy

High-Resolution Solid-State NMR Structure of a 17.6 kDa Protein

SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields

Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA

An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid

Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils

P304

14686-14698

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scholarly article

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10.1021/JA203736Z

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P407

P433

37

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P478

133

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P50

Nikolaus Grigorieff

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2011-08-23T00:00:00Z

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51499990

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21766841

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P932

3190136

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