What determines the structure and stability of KFFE monomers, dimers, and protofibrils?
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Effects of surface interactions on peptide aggregate morphology.Effect of beta-sheet propensity on peptide aggregation.Modeling the self-assembly of the cellulosome enzyme complex.Nanomaterials design and tests for neural tissue engineering.Atomic-scale simulations confirm that soluble beta-sheet-rich peptide self-assemblies provide amyloid mimics presenting similar conformational properties.Globular state in the oligomers formed by Abeta peptides.Nonsteroidal anti-inflammatory drug naproxen destabilizes Aβ amyloid fibrils: a molecular dynamics investigation.Binding of nonsteroidal anti-inflammatory drugs to Abeta fibrilNaproxen interferes with the assembly of Aβ oligomers implicated in Alzheimer's disease.Does amino acid sequence determine the properties of Aβ dimer?Role of water in protein aggregation and amyloid polymorphism.Protein fibrillation and nanoparticle interactions: opportunities and challenges.Structural and Spectroscopic Properties of Assemblies of Self-Replicating Peptide Macrocycles.Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides.Molecular interactions of Alzheimer's biomarker FDDNP with Aβ peptide.An Italian cohort study identifies four new pathologic mutations in the ARSA gene.Two-dimensional replica exchange approach for peptide-peptide interactions.Diversity of kinetic pathways in amyloid fibril formation.Thermodynamics of peptide dimer formation.Balancing hydrophobicity and sequence pattern to influence self-assembly of amphipathic peptides.Molecular simulations of self-assembling bio-inspired supramolecular systems and their connection to experiments.Relationship between population of the fibril-prone conformation in the monomeric state and oligomer formation times of peptides: insights from all-atom simulations.Triphenylalanine peptides self-assemble into nanospheres and nanorods that are different from the nanovesicles and nanotubes formed by diphenylalanine peptides.Sodium chloride interaction with solvated and crystalline cellulose: sodium ion affects the cellotetraose molecule and the cellulose fibril in aqueous solutionThe interaction with gold suppresses fiber-like conformations of the amyloid β (16–22) peptideFactors Governing Fibrillogenesis of Polypeptide Chains Revealed by Lattice Models
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P2860
What determines the structure and stability of KFFE monomers, dimers, and protofibrils?
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article científic
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article scientifique
@fr
articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on February 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
What determines the structure and stability of KFFE monomers, dimers, and protofibrils?
@en
What determines the structure and stability of KFFE monomers, dimers, and protofibrils?
@nl
type
label
What determines the structure and stability of KFFE monomers, dimers, and protofibrils?
@en
What determines the structure and stability of KFFE monomers, dimers, and protofibrils?
@nl
prefLabel
What determines the structure and stability of KFFE monomers, dimers, and protofibrils?
@en
What determines the structure and stability of KFFE monomers, dimers, and protofibrils?
@nl
P2860
P1433
P1476
What determines the structure and stability of KFFE monomers, dimers, and protofibrils?
@en
P2093
Giovanni Bellesia
Joan-Emma Shea
P2860
P304
P356
10.1016/J.BPJ.2008.10.040
P407
P577
2009-02-01T00:00:00Z