Molecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation. - Wikidata - awgldk - TriplyDB

Molecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation.

Molecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation.

http://www.wikidata.org/entity/Q34984401

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Dry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wires The centriolar protein CPAP G-box: an amyloid fibril in a single domain High-Resolution Structure of a Self-Assembly-Competent Form of a Hydrophobic Peptide Captured in a Soluble β-Sheet Scaffold Minimalist design of water-soluble cross-beta architecture.A multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35 Atomic structures of peptide self-assembly mimics Nanomaterials design and tests for neural tissue engineering.Free cholesterol induces higher β-sheet content in Aβ peptide oligomers by aromatic interaction with Phe19.Modeling the Alzheimer Abeta17-42 fibril architecture: tight intermolecular sheet-sheet association and intramolecular hydrated cavities Polyglutamine variation in a flowering time protein correlates with island age in a Hawaiian plant radiation Formation and growth of oligomers: a Monte Carlo study of an amyloid tau fragment Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine Atomic-scale simulations confirm that soluble beta-sheet-rich peptide self-assemblies provide amyloid mimics presenting similar conformational properties.Insight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation.Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR Role of intermolecular forces in defining material properties of protein nanofibrils.Conformational stability of fibrillar amyloid-beta oligomers via protofilament pair formation - a systematic computational study Role of hydration force in the self-assembly of collagens and amyloid steric zipper filaments Interplay of sequence, topology and termini charge in determining the stability of the aggregates of GNNQQNY mutants: a molecular dynamics study.Structural complexity of a composite amyloid fibril.Spontaneous formation of twisted Aβ(16-22) fibrils in large-scale molecular-dynamics simulations.Molecular dynamics simulations on the oligomer-formation process of the GNNQQNY peptide from yeast prion protein Sup35.All-atom computer simulations of amyloid fibrils disaggregation.Computational simulations of the early steps of protein aggregation.Aggregation of amyloids in a cellular context: modelling and experiment.The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy.Unique example of amyloid aggregates stabilized by main chain H-bond instead of the steric zipper: molecular dynamics study of the amyloidogenic segment of amylin wild-type and mutants.GNNQQNY--investigation of early steps during amyloid formation.Investigating the mechanism of peptide aggregation: insights from mixed monte carlo-molecular dynamics simulations.Insights into stability and toxicity of amyloid-like oligomers by replica exchange molecular dynamics analyses.Effect of dehydration on the aggregation kinetics of two amyloid peptides.Insights into structure, stability, and toxicity of monomeric and aggregated polyglutamine models from molecular dynamics simulations.Thermodynamic description of polymorphism in Q- and N-rich peptide aggregates revealed by atomistic simulation.Characterizing the assembly of the Sup35 yeast prion fragment, GNNQQNY: structural changes accompany a fiber-to-crystal switch.Molecular modeling to investigate the binding of Congo red toward GNNQQNY protofibril and in silico virtual screening for the identification of new aggregation inhibitors.Simulation studies on the stabilities of aggregates formed by fibril-forming segments of alpha-Synuclein.Thermodynamic analysis of structural transitions during GNNQQNY aggregation.Energetics Underlying Twist Polymorphisms in Amyloid Fibrils.Characterizing Structural Stability of Amyloid Motif Fibrils Mediated by Water Molecules.Structural and Material Properties of Amyloid Aβ40/42 Fibrils.

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P2860

Molecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation.

http://www.wikidata.org/entity/Q34984401

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2006 nî lūn-bûn

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Molecular dynamics analyses of ...... heet twisting and aggregation.

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Molecular dynamics analyses of ...... heet twisting and aggregation.

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Molecular dynamics analyses of ...... heet twisting and aggregation.

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Molecular dynamics analyses of ...... heet twisting and aggregation.

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Luciana Esposito

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Luigi Vitagliano

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P2860

The 3D profile method for identifying fibril-forming segments of proteins

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

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

VMD: visual molecular dynamics

GROMACS: fast, flexible, and free

Protein misfolding, evolution and disease

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

Protein aggregation and neurodegenerative disease

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

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

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