Molecular basis for insulin fibril assembly - Test2 - elhamkhani - TriplyDB

Molecular basis for insulin fibril assembly

Molecular basis for insulin fibril assembly

http://www.wikidata.org/entity/Q24657505

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Amino acid sequence determinants in self-assembly of insulin chiral amyloid superstructures: role of C-terminus of B-chain in association of fibrils Peptides that form β-sheets on hydrophobic surfaces accelerate surface-induced insulin amyloidal aggregation Oligomerization of Peptides LVEALYL and RGFFYT and Their Binding Affinity to Insulin Mapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerization X-ray Crystallographic Structure of an Artificial β-Sheet Dimer Crystallographic Studies of Prion Protein (PrP) Segments Suggest How Structural Changes Encoded by Polymorphism at Residue 129 Modulate Susceptibility to Human Prion Disease Molecular basis for amyloid- polymorphism Crystal Structure of a Human Prion Protein Fragment Reveals a Motif for Oligomer Formation Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS The Inhibitory Effect of Natural Products on Protein Fibrillation May Be Caused by Degradation Products--A Study Using Aloin and Insulin Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy.Stepwise organization of the β-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils.Intrinsic fibrillation of fast-acting insulin analogs.Observation of spatial propagation of amyloid assembly from single nuclei The effect of red pigment on the amyloidization of yeast proteins.Evaluating nuclei concentration in amyloid fibrillation reactions using back-calculation approach.Insulin glycation by methylglyoxal results in native-like aggregation and inhibition of fibril formation The mechanism of enhanced insulin amyloid fibril formation by NaCl is better explained by a conformational change model Disulfide bridges remain intact while native insulin converts into amyloid fibrils Fibril-forming motifs are essential and sufficient for the fibrillization of human Tau.Polarized Raman Spectroscopy of Aligned Insulin Fibrils Inhibition study on insulin fibrillation and cytotoxicity by paclitaxel.Amyloid fibrillation of insulin under water-limited conditions Macrocyclic β-sheet peptides that inhibit the aggregation of a tau-protein-derived hexapeptide.Isolating toxic insulin amyloid reactive species that lack β-sheets and have wide pH stability Highly amyloidogenic two-chain peptide fragments are released upon partial digestion of insulin with pepsin.De novo design and experimental characterization of ultrashort self-associating peptides Accelerated insulin aggregation under alternating current electric fields: Relevance to amyloid kinetics Normal and reversed supramolecular chirality of insulin fibrils probed by vibrational circular dichroism at the protofilament level of fibril structure Structure and composition of insulin fibril surfaces probed by TERS.Fibril formation from the amyloid-β peptide is governed by a dynamic equilibrium involving association and dissociation of the monomer.Thioredoxin-80 is a product of alpha-secretase cleavage that inhibits amyloid-beta aggregation and is decreased in Alzheimer's disease brain.The supramolecular chemistry of β-sheets.Comparative analysis of anti-polyglutamine Fab crystals grown on Earth and in microgravity.Surface characterization of insulin protofilaments and fibril polymorphs using tip-enhanced Raman spectroscopy (TERS).Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity.Modular design in natural and biomimetic soft materials.The amyloid state of proteins in human diseases.Chirality and chiroptical properties of amyloid fibrils.A Vibrational Circular Dichroism Microsampling Accessory: Mapping Enhanced Vibrational Circular Dichroism in Amyloid Fibril Films.

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P2860

Molecular basis for insulin fibril assembly

http://www.wikidata.org/entity/Q24657505

description

2009 nî lūn-bûn

@nan

2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2009 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Molecular basis for insulin fibril assembly

@ast

Molecular basis for insulin fibril assembly

@en

Molecular basis for insulin fibril assembly

@nl

type

label

Molecular basis for insulin fibril assembly

@ast

Molecular basis for insulin fibril assembly

@en

Molecular basis for insulin fibril assembly

@nl

prefLabel

Molecular basis for insulin fibril assembly

@ast

Molecular basis for insulin fibril assembly

@en

Molecular basis for insulin fibril assembly

@nl

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PNAS.0910080106

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Molecular basis for insulin fibril assembly

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P2093

Joseph S Wall

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

Magdalena I Ivanova

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

Michael R Sawaya

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

Stuart A Sievers

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P2860

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

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils

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

A model of insulin fibrils derived from the x-ray crystal structure of a monomeric insulin (despentapeptide insulin)

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

Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure.

Sequence determinants of amyloid fibril formation

Studies of the structure of insulin fibrils by Fourier transform infrared (FTIR) spectroscopy and electron microscopy.

The protofilament structure of insulin amyloid fibrils.

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18990-5

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scholarly article

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10.1073/PNAS.0910080106

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45

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106

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David Eisenberg

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2009-11-10T00:00:00Z

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38043697

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19864624

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2776439

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