Formation of amyloid fibers triggered by phosphatidylserine-containing membranes.
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Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes MellitusBacteriocins as Potential Anticancer AgentsOrchestration of secretory protein folding by ER chaperonesFRET studies of lipid-protein aggregates related to amyloid-like fibersRole of Cholesterol and Phospholipids in Amylin Misfolding, Aggregation and Etiology of Islet AmyloidosisBiophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Antimicrobial peptides temporins B and L induce formation of tubular lipid protrusions from supported phospholipid bilayerspH-Dependent interaction of cytochrome c with mitochondrial mimetic membranes: the role of an array of positively charged amino acids.Amyloidogenesis abolished by proline substitutions but enhanced by lipid binding.Lipid classes and fatty acid patterns are altered in the brain of γ-synuclein null mutant mice.Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers.The role of the lipid bilayer in tau aggregationNon-esterified fatty acids generate distinct low-molecular weight amyloid-β (Aβ42) oligomers along pathway different from fibril formationAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Phospholipids enhance nucleation but not elongation of apolipoprotein C-II amyloid fibrilsMolecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseasesNBD-labeled phospholipid accelerates apolipoprotein C-II amyloid fibril formation but is not incorporated into mature fibrils.Amyloid fibrillation of insulin under water-limited conditionsRubber elongation factor (REF), a major allergen component in Hevea brasiliensis latex has amyloid propertiesQuantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopyAntimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional link.Can misfolded proteins be beneficial? The HAMLET case.Amyloidogenic and non-amyloidogenic transthyretin variants interact differently with human cardiomyocytes: insights into early events of non-fibrillar tissue damage.Membrane lipid co-aggregation with α-synuclein fibrils.Characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase early amyloid-like oligomers and their implication in α-synuclein aggregation.How type II diabetes-related islet amyloid polypeptide damages lipid bilayers.Atomic Force Microscopy Characterization of Protein Fibrils Formed by the Amyloidogenic Region of the Bacterial Protein MinE on Mica and a Supported Lipid Bilayer.Binding of lysozyme to phospholipid bilayers: evidence for protein aggregation upon membrane associationMembrane-mediated amyloid formation of PrP 106-126: A kinetic study.Identification of an aggregation-prone structure of tau.Membrane damage by human islet amyloid polypeptide through fibril growth at the membraneGeneric cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity.Membranes: a meeting point for lipids, proteins and therapiesRecent insights in islet amyloid polypeptide-induced membrane disruption and its role in beta-cell death in type 2 diabetes mellitusAmyloid formation by the pro-inflammatory S100A8/A9 proteins in the ageing prostate.Liberation of GPI-anchored prion from phospholipids accelerates amyloidogenic conversion.Synthetic lipid vesicles recruit native-like aggregates and affect the aggregation process of the prion Ure2p: insights on vesicle permeabilization and charge selectivity.K3 fragment of amyloidogenic beta(2)-microglobulin forms ion channels: implication for dialysis related amyloidosis.Physiological responses to protein aggregates: fibrinolysis, coagulation and inflammation (new roles for old factors).Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity.
P2860
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P2860
Formation of amyloid fibers triggered by phosphatidylserine-containing membranes.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Formation of amyloid fibers triggered by phosphatidylserine-containing membranes.
@en
Formation of amyloid fibers triggered by phosphatidylserine-containing membranes.
@nl
type
label
Formation of amyloid fibers triggered by phosphatidylserine-containing membranes.
@en
Formation of amyloid fibers triggered by phosphatidylserine-containing membranes.
@nl
prefLabel
Formation of amyloid fibers triggered by phosphatidylserine-containing membranes.
@en
Formation of amyloid fibers triggered by phosphatidylserine-containing membranes.
@nl
P2093
P356
P1433
P1476
Formation of amyloid fibers triggered by phosphatidylserine-containing membranes.
@en
P2093
Esa K J Tuominen
Hongxia Zhao
Paavo K J Kinnunen
P304
10302-10307
P356
10.1021/BI049002C
P407
P577
2004-08-01T00:00:00Z