Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones
about
Amyloid-β Receptors: The Good, the Bad, and the Prion ProteinPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Protein homeostasis at the plasma membraneStructural evolution and membrane interactions of Alzheimer's amyloid-beta peptide oligomers: new knowledge from single-molecule fluorescence studiesInteraction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formationSingle molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Intracellular clusterin interacts with brain isoforms of the bridging integrator 1 and with the microtubule-associated protein Tau in Alzheimer's diseaseMechanisms of action of therapeutic amyloidogenic hexapeptides in amelioration of inflammatory brain disease.Ultrasensitive Measurement of Ca2+ Influx into Lipid Vesicles Induced by Protein Aggregates.Crucial role of nonspecific interactions in amyloid nucleation.Proteomics of old world camelid (Camelus dromedarius): Better understanding the interplay between homeostasis and desert environment.Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulationsCrystallins and neuroinflammation: The glial side of the story.Single-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids.Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.Chaperones as Suppressors of Protein Misfolded Oligomer ToxicitySelf-assembly of protein aggregates in ageing disorders: the lens and cataract model.In vivo modification of Abeta plaque toxicity as a novel neuroprotective lithium-mediated therapy for Alzheimer's disease pathology.Inhibiting the Ca2+ Influx Induced by Human CSF.The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.Plasma and platelet clusterin ratio is altered in Alzheimer's disease patients with distinct neuropsychiatric symptoms: findings from a pilot study.Alzheimer's Disease, Oligomers, and Inflammation.Ultrasensitive Measurement of Ca2+ Influx into Lipid Vesicles Induced by Protein AggregatesSOLVING SINGLE BIOMOLECULES BY ADVANCED FRET-BASED SINGLE-MOLECULE FLUORESCENCE TECHNIQUES
P2860
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P2860
Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones
description
2012 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2012
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scientific journal article
@en
wetenschappelijk artikel (gepubliceerd op 2012/11/20)
@nl
wissenschaftlicher Artikel
@de
наукова стаття, опублікована в листопаді 2012
@uk
مقالة علمية (نشرت في 20-11-2012)
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name
Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones
@ast
Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones
@en
type
label
Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones
@ast
Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones
@en
prefLabel
Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones
@ast
Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones
@en
P2093
P2860
P50
P921
P356
P1433
P1476
Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones
@en
P2093
Mark R. Wilson
Priyanka Narayan
Sarah Meehan
P2860
P304
P356
10.1021/BI301277K
P407
P577
2012-11-20T00:00:00Z