BRICHOS domains efficiently delay fibrillation of amyloid β-peptide.
about
Assessing the causes and consequences of co-polymerization in amyloid formationInteraction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formationSpecific chaperones and regulatory domains in control of amyloid formation.The chaperone domain BRICHOS prevents CNS toxicity of amyloid-β peptide in Drosophila melanogasterLessons from a Rare Familial Dementia: Amyloid and Beyond.A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomersLung fibrosis-associated surfactant protein A1 and C variants induce latent transforming growth factor β1 secretion in lung epithelial cells.Biophysical studies of the amyloid β-peptide: interactions with metal ions and small molecules.On the lag phase in amyloid fibril formation.Charge dependent retardation of amyloid β aggregation by hydrophilic proteins.Current and future treatment of amyloid diseases.Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation.BRI2 ectodomain affects Aβ42 fibrillation and tau truncation in human neuroblastoma cells.Transthyretin and BRICHOS: The Paradox of Amyloidogenic Proteins with Anti-Amyloidogenic Activity for Aβ in the Central Nervous System.Effect of curcumin analogs onα-synuclein aggregation and cytotoxicity.Folding and Intramembraneous BRICHOS Binding of the Prosurfactant Protein C Transmembrane SegmentEffects of polyamino acids and polyelectrolytes on amyloid β fibril formation.Nucleobindin 1 binds to multiple types of pre-fibrillar amyloid and inhibits fibrillization.Non-chaperone proteins can inhibit aggregation and cytotoxicity of Alzheimer amyloid β peptide.Short Aβ peptides attenuate Aβ42 toxicity in vivo.Cellular prion protein targets amyloid-β fibril ends via its C-terminal domain to prevent elongation.Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state.Elevated Surfactant Protein Levels and Increased Flow of Cerebrospinal Fluid in Cranial Magnetic Resonance Imaging.On-chip label-free protein analysis with downstream electrodes for direct removal of electrolysis products.Human lysozyme inhibits the in vitro aggregation of Aβ peptides, which in vivo are associated with Alzheimer's disease.BRICHOS domain of Bri2 inhibits islet amyloid polypeptide (IAPP) fibril formation and toxicity in human beta cells.BRICHOS - an anti-amyloid chaperone: evaluation of blood-brain barrier permeability of Bri2 BRICHOS.Identification and characterization of the BRI2 interactome in the brain.
P2860
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P2860
BRICHOS domains efficiently delay fibrillation of amyloid β-peptide.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
BRICHOS domains efficiently delay fibrillation of amyloid β-peptide.
@en
type
label
BRICHOS domains efficiently delay fibrillation of amyloid β-peptide.
@en
prefLabel
BRICHOS domains efficiently delay fibrillation of amyloid β-peptide.
@en
P2093
P2860
P50
P356
P1476
BRICHOS domains efficiently delay fibrillation of amyloid β-peptide
@en
P2093
Birgitta Frohm
Glareh Askarieh
Hanna Willander
P2860
P304
31608-31617
P356
10.1074/JBC.M112.393157
P407
P577
2012-07-16T00:00:00Z