Hsp20, a novel alpha-crystallin, prevents Abeta fibril formation and toxicity.
about
The role of small heat shock proteins in parasitesIdentification of the key structural motifs involved in HspB8/HspB6-Bag3 interactionHeat shock proteins: cellular and molecular mechanisms in the central nervous system.Molecular mechanisms for Alzheimer's disease: implications for neuroimaging and therapeutics.Genome-wide transcriptional analysis of temperature shift in L. interrogans serovar lai strain 56601.Amyloid beta-protein assembly as a therapeutic target of Alzheimer's disease.Inhibition of Abeta42 aggregation using peptides selected from combinatorial libraries.Multifunctional antioxidants for the treatment of age-related diseasesThe interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation.Reversal of amyloid-induced heart disease in desmin-related cardiomyopathy.αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide.Carnosine's effect on amyloid fibril formation and induced cytotoxicity of lysozyme.Attenuation of beta-amyloid-induced toxicity by sialic-acid-conjugated dendrimers: role of sialic acid attachment.Prospects for recombinant vaccines against Babesia bovis and related parasites.Interactive sequences in the molecular chaperone, human alphaB crystallin modulate the fibrillation of amyloidogenic proteins.Designing heart performance by gene transfer.Molecular chaperones as regulators of cell death.The cardioprotective role of small heat-shock protein 20.The potential inhibitory effect of β-casein on the aggregation and deposition of Aβ1-42 fibrils in Alzheimer's disease: insight from in-vitro and in-silico studies.Structure-activity relationships in peptide modulators of β-amyloid protein aggregation: variation in α,α-disubstitution results in altered aggregate size and morphologyFormation of highly toxic soluble amyloid beta oligomers by the molecular chaperone prefoldin.Real-time probing of β-amyloid self-assembly and inhibition using fluorescence self-quenching between neighbouring dyes.Suppression of in vivo beta-amyloid peptide toxicity by overexpression of the HSP-16.2 small chaperone protein.Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1-42) aggregation in vitro.
P2860
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P2860
Hsp20, a novel alpha-crystallin, prevents Abeta fibril formation and toxicity.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Hsp20, a novel alpha-crystallin, prevents Abeta fibril formation and toxicity.
@ast
Hsp20, a novel alpha-crystallin, prevents Abeta fibril formation and toxicity.
@en
type
label
Hsp20, a novel alpha-crystallin, prevents Abeta fibril formation and toxicity.
@ast
Hsp20, a novel alpha-crystallin, prevents Abeta fibril formation and toxicity.
@en
prefLabel
Hsp20, a novel alpha-crystallin, prevents Abeta fibril formation and toxicity.
@ast
Hsp20, a novel alpha-crystallin, prevents Abeta fibril formation and toxicity.
@en
P2093
P2860
P356
P1433
P1476
Hsp20, a novel alpha-crystallin, prevents Abeta fibril formation and toxicity
@en
P2093
Allison Rice-Ficht
Kenneth Carson
Theresa Good
P2860
P304
P356
10.1110/PS.041020705
P50
P577
2005-03-01T00:00:00Z