C-terminal peptides coassemble into Abeta42 oligomers and protect neurons against Abeta42-induced neurotoxicity.
about
Atomic-level characterization of the ensemble of the Aβ(1-42) monomer in water using unbiased molecular dynamics simulations and spectral algorithmsModulating self-assembly of amyloidogenic proteins as a therapeutic approach for neurodegenerative diseases: strategies and mechanismsAmyloid β-Protein Assembly: The Effect of Molecular Tweezers CLR01 and CLR03Lysine-Specific Molecular Tweezers Are Broad-Spectrum Inhibitors of Assembly and Toxicity of Amyloid ProteinsPeptide dimer structure in an Aβ(1-42) fibril visualized with cryo-EM.Flexibility and binding affinity in protein-ligand, protein-protein and multi-component protein interactions: limitations of current computational approaches.Mechanisms of enzymatic degradation of amyloid Beta microfibrils generating nanofilaments and nanospheres related to cytotoxicity.Amyloid-beta associated with chitosan nano-carrier has favorable immunogenicity and permeates the BBB.Modulation of Amyloid β-Protein (Aβ) Assembly by Homologous C-Terminal Fragments as a Strategy for Inhibiting Aβ Toxicity.Mary S. Easton Center of Alzheimer's Disease Research at UCLA: advancing the therapeutic imperative.Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of alpha-synuclein and beta-amyloid and protect against amyloid-induced toxicityDespite its role in assembly, methionine 35 is not necessary for amyloid beta-protein toxicityMechanistic investigation of the inhibition of Abeta42 assembly and neurotoxicity by Abeta42 C-terminal fragmentsA novel "molecular tweezer" inhibitor of α-synuclein neurotoxicity in vitro and in vivo.Peptides for therapy and diagnosis of Alzheimer's disease.Modeling amyloid-beta as homogeneous dodecamers and in complex with cellular prion protein.Minimal model of self-assembly: emergence of diversity and complexity.Structural basis for Aβ1–42 toxicity inhibition by Aβ C-terminal fragments: discrete molecular dynamics study.Neurotrophins enhance CaMKII activity and rescue amyloid-β-induced deficits in hippocampal synaptic plasticity.Strong inhibition of beta-amyloid peptide aggregation realized by two-steps evolved peptides.Intrinsic determinants of Aβ(12-24) pH-dependent self-assembly revealed by combined computational and experimental studies.Induction of methionine-sulfoxide reductases protects neurons from amyloid β-protein insults in vitro and in vivo.Structure-based design of conformation- and sequence-specific antibodies against amyloid β.Aβ(39-42) modulates Aβ oligomerization but not fibril formationComparison of three amyloid assembly inhibitors: the sugar scyllo-inositol, the polyphenol epigallocatechin gallate, and the molecular tweezer CLR01Alzheimer's amyloid-β A2T variant and its N-terminal peptides inhibit amyloid-β fibrillization and rescue the induced cytotoxicity.Mechanism of C-Terminal Fragments of Amyloid β-Protein as Aβ Inhibitors: Do C-Terminal Interactions Play a Key Role in Their Inhibitory Activity?Discrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid β-protein.The structure of Abeta42 C-terminal fragments probed by a combined experimental and theoretical study.Amino acid position-specific contributions to amyloid beta-protein oligomerization.Small molecule inhibitors of amyloid β peptide aggregation as a potential therapeutic strategy for Alzheimer's disease.Nanotechnology-based drug delivery systems for targeting, imaging and diagnosis of neurodegenerative diseases.Perspectives on Inhibiting β-Amyloid Aggregation through Structure-Based Drug Design.Energetic contributions of residues to the formation of early amyloid-β oligomers.Biophysical characterization of Abeta42 C-terminal fragments: inhibitors of Abeta42 neurotoxicity.Inhibiting the nucleation of amyloid structure in a huntingtin fragment by targeting α-helix-rich oligomeric intermediates.HP-β-cyclodextrin as an inhibitor of amyloid-β aggregation and toxicity.C-terminal tetrapeptides inhibit Aβ42-induced neurotoxicity primarily through specific interaction at the N-terminus of Aβ42.Role of Species-Specific Primary Structure Differences in Aβ42 Assembly and NeurotoxicityRapid α-oligomer formation mediated by the Aβ C terminus initiates an amyloid assembly pathway.
P2860
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P2860
C-terminal peptides coassemble into Abeta42 oligomers and protect neurons against Abeta42-induced neurotoxicity.
description
2008 nî lūn-bûn
@nan
2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
C-terminal peptides coassemble ...... Abeta42-induced neurotoxicity.
@ast
C-terminal peptides coassemble ...... Abeta42-induced neurotoxicity.
@en
type
label
C-terminal peptides coassemble ...... Abeta42-induced neurotoxicity.
@ast
C-terminal peptides coassemble ...... Abeta42-induced neurotoxicity.
@en
prefLabel
C-terminal peptides coassemble ...... Abeta42-induced neurotoxicity.
@ast
C-terminal peptides coassemble ...... Abeta42-induced neurotoxicity.
@en
P2093
P2860
P356
P1476
C-terminal peptides coassemble ...... Abeta42-induced neurotoxicity.
@en
P2093
Aleksey Lomakin
Bernhard H Monien
Brigita Urbanc
Cui-Wei Xie
Erica A Fradinger
George B Benedek
Huiyuan Li
Margaret M Condron
P2860
P304
14175-14180
P356
10.1073/PNAS.0807163105
P407
P577
2008-09-08T00:00:00Z