Lipid composition influences the release of Alzheimer's amyloid β-peptide from membranes.
about
Cholesterol balance in prion diseases and Alzheimer's diseaseAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Genome-wide analysis of Saccharomyces cerevisiae identifies cellular processes affecting intracellular aggregation of Alzheimer's amyloid-β42: importance of lipid homeostasis.Binding, conformational transition and dimerization of amyloid-β peptide on GM1-containing ternary membrane: insights from molecular dynamics simulation.Role of membrane biophysics in Alzheimer's-related cell pathways.Lipid rafts and Alzheimer's disease: protein-lipid interactions and perturbation of signaling.Molecular interactions of Alzheimer amyloid-β oligomers with neutral and negatively charged lipid bilayers.Embedding Aβ42 in heterogeneous membranes depends on cholesterol asymmetriesAlterations in cerebrospinal fluid glycerophospholipids and phospholipase A2 activity in Alzheimer's disease.The role of molecular simulations in the development of inhibitors of amyloid β-peptide aggregation for the treatment of Alzheimer's diseaseMolecular understanding of a potential functional link between antimicrobial and amyloid peptides.Alzheimer's Disease Risk Genes and Lipid Regulators.Effect of Different Phospholipids on α-Secretase Activity in the Non-Amyloidogenic Pathway of Alzheimer's Disease.Lipid insertion domain unfolding regulates protein orientational transition behavior in a lipid bilayer.Molecular Dynamics Simulations of Amyloid β-Peptide (1-42): Tetramer Formation and Membrane InteractionsCharacterization of 3D Voronoi tessellation nearest neighbor lipid shells provides atomistic lipid disruption profile of protein containing lipid membranes.Scaling and alpha-helix regulation of protein relaxation in a lipid bilayer.Stability of transmembrane amyloid β-peptide and membrane integrity tested by molecular modeling of site-specific Aβ42 mutations.The impact of cholesterol, DHA, and sphingolipids on Alzheimer's disease.Investigation of the interaction of amyloid β peptide (11-42) oligomers with a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) membrane using molecular dynamics simulation.Embedded in the Membrane: How Lipids Confer Activity and Specificity to Intramembrane Proteases.Energetics Underlying Twist Polymorphisms in Amyloid Fibrils.The Effects of Extracellular Serum Concentration on APP Processing in Npc1-Deficient APP-Overexpressing N2a Cells.The molecular behavior of a single β-amyloid inside a dipalmitoylphosphatidylcholine bilayer at three different temperatures: An atomistic simulation study: Aβ interaction with DPPC: Atomistic simulation.
P2860
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P2860
Lipid composition influences the release of Alzheimer's amyloid β-peptide from membranes.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh
2011年學術文章
@zh-hant
name
Lipid composition influences the release of Alzheimer's amyloid β-peptide from membranes.
@en
type
label
Lipid composition influences the release of Alzheimer's amyloid β-peptide from membranes.
@en
prefLabel
Lipid composition influences the release of Alzheimer's amyloid β-peptide from membranes.
@en
P2860
P356
P1433
P1476
Lipid composition influences the release of Alzheimer's amyloid β-peptide from membranes
@en
P2093
David R Bevan
Justin A Lemkul
P2860
P304
P356
10.1002/PRO.678
P577
2011-07-13T00:00:00Z