Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.
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The Role of Amyloid-β Oligomers in Toxicity, Propagation, and ImmunotherapyInter-species cross-seeding: stability and assembly of rat-human amylin aggregatesFamilial Alzheimer's disease Osaka mutant (ΔE22) β-barrels suggest an explanation for the different Aβ1-40/42 preferred conformational states observed by experiment.Maximally asymmetric transbilayer distribution of anionic lipids alters the structure and interaction with lipids of an amyloidogenic protein dimer bound to the membrane surfaceThe conformational stability of nonfibrillar amyloid-β peptide oligomers critically depends on the C-terminal peptide length.Activity and architecture of pyroglutamate-modified amyloid-β (AβpE3-42) poresDisordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranesAlzheimer's disease: which type of amyloid-preventing drug agents to employ?Role of the fast kinetics of pyroglutamate-modified amyloid-β oligomers in membrane binding and membrane permeability.Stability of Iowa mutant and wild type Aβ-peptide aggregatesBinding, conformational transition and dimerization of amyloid-β peptide on GM1-containing ternary membrane: insights from molecular dynamics simulation.Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation.Amyloid β oligomers in Alzheimer's disease pathogenesis, treatment, and diagnosis.Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulationsOn the lack of polymorphism in Aβ-peptide aggregates derived from patient brainsThe higher level of complexity of K-Ras4B activation at the membrane.Proteasome regulates turnover of toxic human amylin in pancreatic cells.In silico cross seeding of Aβ and amylin fibril-like oligomers.Mutations and seeding of amylin fibril-like oligomers.Atomic force microscopy to study molecular mechanisms of amyloid fibril formation and toxicity in Alzheimer's disease.The structure and function of cell membranes examined by atomic force microscopy and single-molecule force spectroscopy.Proteotoxicity and cardiac dysfunction.More Than a Pore: The Interplay of Pore-Forming Proteins and Lipid Membranes.β-Amyloid peptides display protective activity against the human Alzheimer's disease-associated herpes simplex virus-1.Dewetting transition assisted clearance of (NFGAILS) amyloid fibrils from cell membranes by graphene.Characteristics of C-terminal, β-amyloid peptide binding fragment of neuroprotective protease inhibitor, cystatin C.Molecular dynamics simulations of early steps in RNA-mediated conversion of prions.Small molecule NPT-440-1 inhibits ionic flux through Aβ1-42 pores: Implications for Alzheimer's disease therapeutics.The Molecular Physiopathogenesis of Islet Amyloidosis.APP/Aβ structural diversity and Alzheimer's disease pathogenesis.Unmodified and pyroglutamylated amyloid β peptides form hypertoxic hetero-oligomers of unique secondary structure.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.No effects without causes: the Iron Dysregulation and Dormant Microbes hypothesis for chronic, inflammatory diseases.The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade.Characterisation of the Structure and Oligomerisation of Islet Amyloid Polypeptides (IAPP): A Review of Molecular Dynamics Simulation Studies
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P2860
Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.
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2012 nî lūn-bûn
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2012 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.
@ast
Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.
@en
Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.
@nl
type
label
Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.
@ast
Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.
@en
Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.
@nl
prefLabel
Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.
@ast
Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.
@en
Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.
@nl
P2093
P2860
P50
P356
P1476
Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.
@en
P2093
Bruce L Kagan
Hyunbum Jang
Laura Connelly
Ratnesh Lal
P2860
P304
P356
10.1021/CT300916F
P577
2012-12-05T00:00:00Z