Z-Phe-Ala-diazomethylketone (PADK) disrupts and remodels early oligomer states of the Alzheimer disease Aβ42 protein.
about
Brain pyroglutamate amyloid-β is produced by cathepsin B and is reduced by the cysteine protease inhibitor E64d, representing a potential Alzheimer's disease therapeuticAmyloid β-Protein Assembly: The Effect of Molecular Tweezers CLR01 and CLR03Novel insights into protein misfolding diseases revealed by ion mobility-mass spectrometry.Rational design of a structural framework with potential use to develop chemical reagents that target and modulate multiple facets of Alzheimer's disease.Ion mobility spectrometry: A personal view of its development at UCSBSDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer´s disease: appealing for ESI-IM-MSAmyloid β-Protein Assembly: Differential Effects of the Protective A2T Mutation and Recessive A2V Familial Alzheimer's Disease Mutation.Loss of Cathepsin B and L Leads to Lysosomal Dysfunction, NPC-Like Cholesterol Sequestration and Accumulation of the Key Alzheimer's ProteinsOpposing Effects of Cucurbit[7]uril and 1,2,3,4,6-Penta-O-galloyl-β-d-glucopyranose on Amyloid β25-35 Assembly.Mechanism of C-Terminal Fragments of Amyloid β-Protein as Aβ Inhibitors: Do C-Terminal Interactions Play a Key Role in Their Inhibitory Activity?Pulsed hydrogen-deuterium exchange mass spectrometry probes conformational changes in amyloid beta (Aβ) peptide aggregation.Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.Methods of probing the interactions between small molecules and disordered proteins.Role of Species-Specific Primary Structure Differences in Aβ42 Assembly and NeurotoxicityIdentification of small-molecule binding pockets in the soluble monomeric form of the Aβ42 peptide.Conformational dynamics of α-synuclein: insights from mass spectrometry.Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.Capping of aβ42 oligomers by small molecule inhibitors.1,2,3,4,6-penta-O-galloyl-β-D-glucopyranose Binds to the N-terminal Metal Binding Region to Inhibit Amyloid β-protein Oligomer and Fibril Formation.Ion Mobility-Mass Spectrometry Reveals a Dipeptide That Acts as a Molecular Chaperone for Amyloid β.
P2860
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P2860
Z-Phe-Ala-diazomethylketone (PADK) disrupts and remodels early oligomer states of the Alzheimer disease Aβ42 protein.
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
Z-Phe-Ala-diazomethylketone (P ...... lzheimer disease Aβ42 protein.
@ast
Z-Phe-Ala-diazomethylketone (P ...... lzheimer disease Aβ42 protein.
@en
type
label
Z-Phe-Ala-diazomethylketone (P ...... lzheimer disease Aβ42 protein.
@ast
Z-Phe-Ala-diazomethylketone (P ...... lzheimer disease Aβ42 protein.
@en
prefLabel
Z-Phe-Ala-diazomethylketone (P ...... lzheimer disease Aβ42 protein.
@ast
Z-Phe-Ala-diazomethylketone (P ...... lzheimer disease Aβ42 protein.
@en
P2093
P2860
P50
P356
P1476
Z-Phe-Ala-diazomethylketone (P ...... Alzheimer disease Aβ42 protein
@en
P2093
Ben A Bahr
Kishore Viswanathan
Meagan L Wisniewski
Michael T Bowers
P2860
P304
P356
10.1074/JBC.C111.328575
P407
P577
2012-01-17T00:00:00Z