Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: the role of dangerous unchaperoned molecules.
about
Cytotoxic ribonucleases: molecular weapons and their targetsPhage display and peptide mapping of an immunoglobulin light chain fibril-related conformational epitopeEvaluating the fitness cost of protein expression in Saccharomyces cerevisiae.Amyloid ion channels: a common structural link for protein-misfolding diseaseOligomeric forms of insulin amyloid aggregation disrupt outgrowth and complexity of neuron-like PC12 cells.Calcitonin forms oligomeric pore-like structures in lipid membranes.Class II G protein-coupled receptors and their ligands in neuronal function and protectionSoluble amyloid oligomers increase bilayer conductance by altering dielectric structure.Amyloid beta ion channel: 3D structure and relevance to amyloid channel paradigm.Generic cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity.Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution.Synthetic lipid vesicles recruit native-like aggregates and affect the aggregation process of the prion Ure2p: insights on vesicle permeabilization and charge selectivity.Inhibition of aggregate formation as therapeutic target in protein misfolding diseases: effect of tetracycline and trehalose.Amyloidogenesis of type III-dependent harpins from plant pathogenic bacteria.The yeast prion Ure2p native-like assemblies are toxic to mammalian cells regardless of their aggregation state.Natively folded HypF-N and its early amyloid aggregates interact with phospholipid monolayers and destabilize supported phospholipid bilayers.Protein folding and misfolding on surfaces.An efficient combinatorial synthesis of allocolchicine analogues via a triple cascade reaction and their evaluation as inhibitors of insulin aggregation.Drift Barriers to Quality Control When Genes Are Expressed at Different Levels.Channels formed with a mutant prion protein PrP(82-146) homologous to a 7-kDa fragment in diseased brain of GSS patients.
P2860
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P2860
Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: the role of dangerous unchaperoned molecules.
description
2002 nî lūn-bûn
@nan
2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Ion channel formation and memb ...... gerous unchaperoned molecules.
@ast
Ion channel formation and memb ...... gerous unchaperoned molecules.
@en
Ion channel formation and memb ...... gerous unchaperoned molecules.
@nl
type
label
Ion channel formation and memb ...... gerous unchaperoned molecules.
@ast
Ion channel formation and memb ...... gerous unchaperoned molecules.
@en
Ion channel formation and memb ...... gerous unchaperoned molecules.
@nl
prefLabel
Ion channel formation and memb ...... gerous unchaperoned molecules.
@ast
Ion channel formation and memb ...... gerous unchaperoned molecules.
@en
Ion channel formation and memb ...... gerous unchaperoned molecules.
@nl
P2860
P1476
Ion channel formation and memb ...... gerous unchaperoned molecules.
@en
P2093
Christine L Henry
Joseph I Kourie
P2860
P304
P356
10.1046/J.1440-1681.2002.03737.X
P577
2002-09-01T00:00:00Z