Structure of the cross-beta spine of amyloid-like fibrils - Wikidata - wikimedia - TriplyDB

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

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

http://www.wikidata.org/entity/Q24548308

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Degradation of the disease-associated prion protein by a serine protease from lichens β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptides A scientific revolution? The prion anomaly may challenge the central dogma of molecular biology The 3D profile method for identifying fibril-forming segments of proteins Collagen structure and stability Expression of Fap amyloids in Pseudomonas aeruginosa, P. fluorescens, and P. putida results in aggregation and increased biofilm formation Dry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wires Expression and purification of 15N- and 13C-isotope labeled 40-residue human Alzheimer's β-amyloid peptide for NMR-based structural analysis Dynamic nuclear polarization at high magnetic fields Amyloids: friend or foe?Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure High-Field Dynamic Nuclear Polarization for Solid and Solution Biological NMR Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure Breaking up (amyloid) is hard to do.Amyloid-beta Alzheimer targets - protein processing, lipid rafts, and amyloid-beta pores New Potential Pharmacological Functions of Chinese Herbal Medicines via Regulation of Autophagy The centriolar protein CPAP G-box: an amyloid fibril in a single domain Peptide-Induced Amyloid-Like Conformational Transitions in Proteins Mechanisms of amyloid formation revealed by solution NMR Fibrillogenesis of huntingtin and other glutamine containing proteins Yeast prions and human prion-like proteins: sequence features and prediction methods Amyloid cannot resist identification Oligomerization of Peptides LVEALYL and RGFFYT and Their Binding Affinity to Insulin Imaging cervical cytology with scanning near-field optical microscopy (SNOM) coupled with an IR-FEL.An introduction to biomolecular graphics.A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils Mapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerization Hydrophobic Surface Burial Is the Major Stability Determinant of a Flat, Single-layer β-Sheet Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains A β-Hairpin Comprising the Nuclear Localization Sequence Sustains the Self-associated States of Nucleosome Assembly Protein 1 Protein crystallography with a micrometre-sized synchrotron-radiation beam Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core High-Resolution Structure of a Self-Assembly-Competent Form of a Hydrophobic Peptide Captured in a Soluble β-Sheet Scaffold The structure of a fibril-forming sequence, NNQQNY, in the context of a globular fold Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin)Aromatic Cross-Strand Ladders Control the Structure and Stability of β-Rich Peptide Self-Assembly Mimics Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils Molecular Mechanism of Thioflavin-T Binding to the Surface of β-Rich Peptide Self-Assemblies Structural Alterations within Native Amyloidogenic Immunoglobulin Light Chains Structural and Functional Studies of Truncated Hemolysin A from Proteus mirabilis

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

http://www.wikidata.org/entity/Q24548308

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2005 nî lūn-bûn

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2005 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2005 թվականի հունիսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

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

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

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

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

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

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

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

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

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

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

@en

P2093

Christian Riekel

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

Melinda Balbirnie

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

Rebecca Nelson

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

Robert Grothe

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

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

Improved methods for building protein models in electron density maps and the location of errors in these models

PROCHECK: a program to check the stereochemical quality of protein structures

Shape complementarity at protein/protein interfaces

Refinement of macromolecular structures by the maximum-likelihood method

The CCP4 suite: programs for protein crystallography

Review: history of the amyloid fibril

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

[URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae

A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

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773-8

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scholarly article

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124664

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10.1038/NATURE03680

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7043

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435

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David Eisenberg

Michael R Sawaya

Anders Østergaard Madsen

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2005-06-09T00:00:00Z

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7797112

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1052170050

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15944695

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1479801

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