Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
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Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.The Mitochondrial-Derived Peptides, HumaninS14G and Small Humanin-like Peptide 2, Exhibit Chaperone-like ActivityMethods of probing the interactions between small molecules and disordered proteins.The Amyloid Phenomenon and Its Links with Human Disease.Transthyretin and BRICHOS: The Paradox of Amyloidogenic Proteins with Anti-Amyloidogenic Activity for Aβ in the Central Nervous System.Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method.Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates.Monomer-dependent secondary nucleation in amyloid formation.Nucleobindin 1 binds to multiple types of pre-fibrillar amyloid and inhibits fibrillization.The Aggregation Paths and Products of Aβ42 Dimers Are Distinct from Those of the Aβ42 Monomer.Cellular prion protein targets amyloid-β fibril ends via its C-terminal domain to prevent elongation.Reduced Lipid Bilayer Thickness Regulates the Aggregation and Cytotoxicity of Amyloid-β.Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state.Biophysical Aspects of Alzheimer's Disease: Implications for Pharmaceutical Sciences : Theme: Drug Discovery, Development and Delivery in Alzheimer's Disease Guest Editor: Davide Brambilla.Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein.Stereochemistry and amyloid inhibition: Asymmetric triplex metallohelices enantioselectively bind to Aβ peptide.Mathematical Modeling of Protein Misfolding Mechanisms in Neurological Diseases: A Historical Overview.How Do Gyrating Beads Accelerate Amyloid Fibrillization?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.Alzheimer's Disease, Oligomers, and Inflammation.A Rationally Designed Hsp70 Variant Rescues the Aggregation-Associated Toxicity of Human IAPP in Cultured Pancreatic Islet β-Cells.Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface.The neuronal S100B protein is a calcium-tuned suppressor of amyloid-β aggregation.Targeting Amyloid Aggregation: An Overview of Strategies and MechanismsScaling and dimensionality in the chemical kinetics of protein filament formationMapping interactions with the chaperone network reveals factors that protect against tau aggregation
P2860
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P2860
Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
Kinetic analysis reveals the d ...... nes suppress amyloid formation
@en
Kinetic analysis reveals the d ...... es suppress amyloid formation.
@nl
type
label
Kinetic analysis reveals the d ...... nes suppress amyloid formation
@en
Kinetic analysis reveals the d ...... es suppress amyloid formation.
@nl
prefLabel
Kinetic analysis reveals the d ...... nes suppress amyloid formation
@en
Kinetic analysis reveals the d ...... es suppress amyloid formation.
@nl
P2093
P2860
P50
P356
P1476
Kinetic analysis reveals the d ...... nes suppress amyloid formation
@en
P2093
Cecilia Emanuelsson
Cecilia Månsson
Jenny Presto
Paolo Arosio
Thomas C T Michaels
Tuomas P J Knowles
P2860
P2888
P356
10.1038/NCOMMS10948
P407
P577
2016-03-24T00:00:00Z