Alzheimer Aβ peptide interactions with lipid membranes: fibrils, oligomers and polymorphic amyloid channels.
about
Familial Alzheimer's disease Osaka mutant (ΔE22) β-barrels suggest an explanation for the different Aβ1-40/42 preferred conformational states observed by experiment.Membrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory.Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Conformational dynamics and aggregation behavior of piezoelectric diphenylalanine peptides in an external electric field.Soluble amyloid-β oligomers as synaptotoxins leading to cognitive impairment in Alzheimer's diseaseEffects of intramolecular distance between amyloidogenic domains on amyloid aggregation.Molecular interactions of Alzheimer amyloid-β oligomers with neutral and negatively charged lipid bilayers.Proteasome regulates turnover of toxic human amylin in pancreatic cells.Atomic force microscopy to study molecular mechanisms of amyloid fibril formation and toxicity in Alzheimer's disease.Molecular understanding of a potential functional link between antimicrobial and amyloid peptides.Changes in lipid membranes may trigger amyloid toxicity in Alzheimer's disease.Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry.HIV Tat protein and amyloid-β peptide form multifibrillar structures that cause neurotoxicity.Ring-like N-fold Models of Aβ42 fibrils.Unlocking the atomic-level details of amyloid fibril growth through advanced biomolecular simulations.Single-cell screening of cytosolic [Ca(2+)] reveals cell-selective action by the Alzheimer's Aβ peptide ion channel.The Molecular Physiopathogenesis of Islet Amyloidosis.Molecular dynamics simulation studies of the structural response of an isolated Aβ1-42 monomer localized in the vicinity of the hydrophilic TiO 2 surface.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.
P2860
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P2860
Alzheimer Aβ peptide interactions with lipid membranes: fibrils, oligomers and polymorphic amyloid channels.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Alzheimer Aβ peptide interacti ...... polymorphic amyloid channels.
@en
Alzheimer Aβ peptide interacti ...... polymorphic amyloid channels.
@nl
type
label
Alzheimer Aβ peptide interacti ...... polymorphic amyloid channels.
@en
Alzheimer Aβ peptide interacti ...... polymorphic amyloid channels.
@nl
prefLabel
Alzheimer Aβ peptide interacti ...... polymorphic amyloid channels.
@en
Alzheimer Aβ peptide interacti ...... polymorphic amyloid channels.
@nl
P2860
P356
P1433
P1476
Alzheimer Aβ peptide interacti ...... d polymorphic amyloid channels
@en
P2093
Florentina Tofoleanu
P2860
P304
P356
10.4161/PRI.21022
P577
2012-08-09T00:00:00Z