Fibrillogenesis and cytotoxic activity of the amyloid-forming apomyoglobin mutant W7FW14F.
about
Mapping out the multistage fibrillation of glucagonMisfolding and amyloid aggregation of apomyoglobinβ-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Differential effects of glycation on protein aggregation and amyloid formation.Heparin induces harmless fibril formation in amyloidogenic W7FW14F apomyoglobin and amyloid aggregation in wild-type protein in vitro.Unraveling amyloid toxicity pathway in NIH3T3 cells by a combined proteomic and 1 H-NMR metabonomic approach.Fluctuation methods to study protein aggregation in live cells: concanavalin A oligomers formationMonitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the aggregating species.Glycation accelerates fibrillization of the amyloidogenic W7FW14F apomyoglobinThe curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization.Generic cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity.Protein folding and aggregation into amyloid: the interference by natural phenolic compoundsBiochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity.Inhibition of aggregate formation as therapeutic target in protein misfolding diseases: effect of tetracycline and trehalose.Platelet-activating factor mediates the cytotoxicity induced by W7FW14F apomyoglobin amyloid aggregates in neuroblastoma cells.Heme binding inhibits the fibrillization of amyloidogenic apomyoglobin and determines lack of aggregate cytotoxicity.The C-terminal repeating units of CsgB direct bacterial functional amyloid nucleation.Glycation of Wild-Type Apomyoglobin Induces Formation of Highly Cytotoxic Oligomeric Species.Protein folding and misfolding on surfaces.Time-resolved small-angle x-ray scattering study of the early stage of amyloid formation of an apomyoglobin mutant.Formation of lamellar micelle-like oligomers and membrane disruption revealed by the study of short peptide hIAPP18-27.sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability.Cytotoxicity of albebetin oligomers depends on cross-beta-sheet formation.
P2860
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P2860
Fibrillogenesis and cytotoxic activity of the amyloid-forming apomyoglobin mutant W7FW14F.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Fibrillogenesis and cytotoxic ...... g apomyoglobin mutant W7FW14F.
@en
Fibrillogenesis and cytotoxic ...... g apomyoglobin mutant W7FW14F.
@nl
type
label
Fibrillogenesis and cytotoxic ...... g apomyoglobin mutant W7FW14F.
@en
Fibrillogenesis and cytotoxic ...... g apomyoglobin mutant W7FW14F.
@nl
prefLabel
Fibrillogenesis and cytotoxic ...... g apomyoglobin mutant W7FW14F.
@en
Fibrillogenesis and cytotoxic ...... g apomyoglobin mutant W7FW14F.
@nl
P2093
P2860
P356
P1476
Fibrillogenesis and cytotoxic ...... g apomyoglobin mutant W7FW14F.
@en
P2093
Antonio Mezzogiorno
Clara Iannuzzi
Clorinda Malmo
Gaetano Irace
Ivana Sirangelo
Maria Rosaria Bianco
P2860
P304
13183-13189
P356
10.1074/JBC.M308207200
P407
P50
P577
2003-12-30T00:00:00Z