about
Misfolding and amyloid aggregation of apomyoglobinEffects of surface interactions on peptide aggregate morphology.Evaluating the fitness cost of protein expression in Saccharomyces cerevisiae.Maximally asymmetric transbilayer distribution of anionic lipids alters the structure and interaction with lipids of an amyloidogenic protein dimer bound to the membrane surfaceTGF-β induces TIAF1 self-aggregation via type II receptor-independent signaling that leads to generation of amyloid β plaques in Alzheimer's disease.Isothermal microcalorimetry to investigate non specific interactions in biophysical chemistry.Heparin induces harmless fibril formation in amyloidogenic W7FW14F apomyoglobin and amyloid aggregation in wild-type protein in vitro.A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffectedOxidative stress in mammalian cells impinges on the cysteines redox state of human XRCC3 protein and on its cellular localization.Structure, stability, and aggregation of β-2 microglobulin mutants: insights from a Fourier transform infrared study in solution and in the crystalline stateHow Do the Size, Charge and Shape of Nanoparticles Affect Amyloid β Aggregation on Brain Lipid Bilayer?Mild exposure of RIN-5F β-cells to human islet amyloid polypeptide aggregates upregulates antioxidant enzymes via NADPH oxidase-RAGE: an hormetic stimulus.Mechanism of suppression of protein aggregation by α-crystallin.Polyphenolic compounds for treating neurodegenerative disorders involving protein misfolding.Inhibition of aggregate formation as therapeutic target in protein misfolding diseases: effect of tetracycline and trehalose.Protein/Peptide Aggregation and Amyloidosis on Biointerfaces.Fitness costs of minimal sequence alterations causing protein instability and toxicity.Combined effects of solvation and aggregation propensity on the final supramolecular structures adopted by hydrophobic, glycine-rich, elastin-like polypeptides.Interactions of lysozyme with phospholipid vesicles: effects of vesicle biophysical features on protein misfolding and aggregation
P2860
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P2860
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh-hant
name
Protein folding and misfolding on surfaces.
@en
Protein folding and misfolding on surfaces.
@nl
type
label
Protein folding and misfolding on surfaces.
@en
Protein folding and misfolding on surfaces.
@nl
prefLabel
Protein folding and misfolding on surfaces.
@en
Protein folding and misfolding on surfaces.
@nl
P2860
P356
P1476
Protein folding and misfolding on surfaces
@en
P2093
Massimo Stefani
P2860
P304
P356
10.3390/IJMS9122515
P407
P577
2008-12-09T00:00:00Z