Hen lysozyme amyloid fibrils induce aggregation of erythrocytes and lipid vesicles. (Q51750540)

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24 January 2020

title

Hen lysozyme amyloid fibrils induce aggregation of erythrocytes and lipid vesicles (English)

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24 January 2020

1

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24 January 2020

author name string

Ramakrishnan Nagaraj

series ordinal

2

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24 January 2020

publication date

26 March 2009

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Molecular and Cellular Biochemistry

24 January 2020

published in

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volume

328

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24 January 2020

issue

1-2

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24 January 2020

page(s)

209-215

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https://scigraph.springernature.com/pub.10.1007/s11010-009-0091-8

24 January 2020

exact match

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cites work

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Evidence that Perutz's double-beta-stranded subunit structure for beta-amyloids also applies to their channel-forming structures in membranes

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Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology

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Binding of lysozyme to phospholipid bilayers: evidence for protein aggregation upon membrane association

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Amyloid-beta peptide assembly: a critical step in fibrillogenesis and membrane disruption

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Small-volume extrusion apparatus for preparation of large, unilamellar vesicles

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Lysozyme interactions with phospholipid vesicles: relationships with fusion and release of aqueous content

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Cytotoxicity of albebetin oligomers depends on cross-beta-sheet formation.

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Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid

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Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants.

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Association of lysozyme to phospholipid surfaces and vesicle fusion

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Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain

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A lipid-specific toxin reveals heterogeneity of sphingomyelin-containing membranes

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Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture

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Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease.

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A highly amyloidogenic region of hen lysozyme

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Structural transitions of lysozyme in urea solution

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Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

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Guanidine hydrochloride can induce amyloid fibril formation from hen egg-white lysozyme

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Modulation of lysozyme charge influences interaction with phospholipid vesicles.

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Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers

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Thermally induced fibrillar aggregation of hen egg white lysozyme

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Lysozyme induced fusion of negatively charged phospholipid vesicles

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Only amyloidogenic intermediates of transthyretin induce apoptosis

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Formation of amyloid fibrils from fully reduced hen egg white lysozyme

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Formation of amyloid fibers triggered by phosphatidylserine-containing membranes

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Association of lysozyme with phospholipid vesicles is accompanied by membrane surface dehydration

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Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1.

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Islet amyloid polypeptide inserts into phospholipid monolayers as monomer

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Lysozyme Amyloid Oligomers and Fibrils Induce Cellular Death via Different Apoptotic/Necrotic Pathways

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Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases

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The role of protein charge in protein-lipid interactions. pH-dependent changes of the electrophoretic mobility of liposomes through adsorption of water-soluble, globular proteins

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Human lysozyme gene mutations cause hereditary systemic amyloidosis

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Interaction of human stefin B in the prefibrillar oligomeric form with membranes. Correlation with cellular toxicity

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12 December 2020

10.1007/S11010-009-0091-8

Identifiers

DOI

1 reference

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24 January 2020

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