Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders
about
Functional amyloid formation within mammalian tissue.Predicting the conformations of peptides and proteins in early evolution. A review article submitted to Biology DirectTowards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson's, Huntington's, Alzheimer's, prions, bactericides, chemical toxicology and others as examplesDequalinium-induced protofibril formation of alpha-synucleinalphaB-crystallin competes with Alzheimer's disease beta-amyloid peptide for peptide-peptide interactions and induces oxidation of Abeta-Met35Molecular determinants of α-synuclein mutants' oligomerization and membrane interactionsCharacterizing affinity epitopes between prion protein and β-amyloid using an epitope mapping immunoassayDirect visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson's disease brainProgressive accumulation of amyloid-beta oligomers in Alzheimer's disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteinsHDAC6 and microtubules are required for autophagic degradation of aggregated huntingtinDissecting the pathological effects of human Abeta40 and Abeta42 in Drosophila: a potential model for Alzheimer's diseaseImmunization with amyloid-beta attenuates inclusion body myositis-like myopathology and motor impairment in a transgenic mouse modelStructural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrilsSoluble oligomers of the amyloid beta-protein impair synaptic plasticity and behaviorCharacterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagyMechanism of prion propagation: amyloid growth occurs by monomer additionDysregulation of Na+/K+ ATPase by amyloid in APP+PS1 transgenic miceCharacterization of the aggregates formed during recombinant protein expression in bacteriaGut Feelings About α-Synuclein in Gastrointestinal Biopsies: Biomarker in the Making?Insights into Mechanisms of Chronic NeurodegenerationTargeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer's disease immunotherapeuticsElectrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomicsAlzheimer's therapeutics: translation of preclinical science to clinical drug developmentDye-binding assays for evaluation of the effects of small molecule inhibitors on amyloid (aβ) self-assemblyExploring the accessible conformations of N-terminal acetylated α-synucleinPathogenesis of synaptic degeneration in Alzheimer's disease and Lewy body diseaseNLRP3 inflammasome: activation and regulation in age-related macular degenerationEffect of the inhaled anesthetics isoflurane, sevoflurane and desflurane on the neuropathogenesis of Alzheimer's disease (review)Mechanisms of protein-folding diseases at a glanceUbiquitous amyloidsTau mutant A152T, a risk factor for FTD/PSP, induces neuronal dysfunction and reduced lifespan independently of aggregation in a C. elegans Tauopathy modelNeuronal death induced by misfolded prion protein is due to NAD+ depletion and can be relieved in vitro and in vivo by NAD+ replenishment.The physical relationship between infectivity and prion protein aggregates is strain-dependentSynthetic prions with novel strain-specified propertiesNovel polyglutamine model uncouples proteotoxicity from agingA helical structural nucleus is the primary elongating unit of insulin amyloid fibrilsPK-sensitive PrP is infectious and shares basic structural features with PK-resistant PrPCharacteristics of Amyloid-Related Oligomers Revealed by Crystal Structures of Macrocyclic β-Sheet MimicsAtomic View of a Toxic Amyloid Small Oligomer
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P2860
Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders
description
2003 թուականին հրատարակուած գիտական յօդուած
@hyw
2003 թվականին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2003
@ast
im Jahr 2003 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: 2003)
@en
wetenschappelijk artikel (gepubliceerd in 2003)
@nl
наукова стаття, опублікована у 2003
@uk
مقالة علمية (نشرت عام 2003)
@ar
name
Protofibrils, pores, fibrils, ...... s from the innocent bystanders
@ast
Protofibrils, pores, fibrils, ...... s from the innocent bystanders
@en
type
label
Protofibrils, pores, fibrils, ...... s from the innocent bystanders
@ast
Protofibrils, pores, fibrils, ...... s from the innocent bystanders
@en
prefLabel
Protofibrils, pores, fibrils, ...... s from the innocent bystanders
@ast
Protofibrils, pores, fibrils, ...... s from the innocent bystanders
@en
P3181
P1476
Protofibrils, pores, fibrils, ...... s from the innocent bystanders
@en
P2093
Lansbury PT
P304
P3181
P356
10.1146/ANNUREV.NEURO.26.010302.081142
P407
P577
2003-01-01T00:00:00Z