Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. - Wikidata - awgldk - TriplyDB

Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing.

Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing.

http://www.wikidata.org/entity/Q30175871

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Fluorescent Proteins as Biomarkers and Biosensors: Throwing Color Lights on Molecular and Cellular Processes Molecular chaperone properties of serum amyloid P component Structure of the cross-beta spine of amyloid-like fibrils Pauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy Deciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily.High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy High-resolution Electron Microscopy of Helical Specimens: A Fresh Look at Tobacco Mosaic Virus Atomic structure and hierarchical assembly of a cross- amyloid fibril Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro Ultrastructural organization of amyloid fibrils by atomic force microscopy.Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance.Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils Solid-state NMR as a probe of amyloid structure Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril NMR assignments of PI3-SH3 domain aided by protonless NMR spectroscopy.Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR.High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .Low molecular weight oligomers of amyloid peptides display beta-barrel conformations: a replica exchange molecular dynamics study in explicit solvent.NMR characterizations of an amyloidogenic conformational ensemble of the PI3K SH3 domain.Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.Peptide dimer structure in an Aβ(1-42) fibril visualized with cryo-EM.Structural polymorphism of Alzheimer Abeta and other amyloid fibrils Contact order and ab initio protein structure prediction Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure.Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Interprotofilament interactions between Alzheimer's Abeta1-42 peptides in amyloid fibrils revealed by cryoEM Problems in fitting high resolution structures into electron microscopic reconstructions.Biophysical studies of the development of amyloid fibrils from a peptide fragment of cold shock protein B.Monitoring disappearance of monomers and generation of resistance to proteolysis during the formation of the activation domain of human procarboxypeptidase A2 (ADA2h) amyloid fibrils by matrix-assisted laser-desorption ionization-time-of-flight-MS.Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspB Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p.Prediction of amyloidogenic and disordered regions in protein chains AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides.

P2860

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P2860

Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing.

http://www.wikidata.org/entity/Q30175871

description

1999 nî lūn-bûn

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1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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1999 թվականի փետրվարին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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Cryo-electron microscopy struc ...... odel of the molecular packing.

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Cryo-electron microscopy struc ...... odel of the molecular packing.

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Cryo-electron microscopy struc ...... odel of the molecular packing.

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The EMBO Journal

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C M Dobson

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P2860

Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif

Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase

Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer

NMR structure of the mouse prion protein domain PrP(121-231)

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

Raster3D Version 2.0. A program for photorealistic molecular graphics

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

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New domain motif: the structure of pectate lyase C, a secreted plant virulence factor

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4

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Elena V. Orlova

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232758746

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10022824

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cryogenic electron microscopy

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1171174

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