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The emerging importance of group II PAKsAutoproteolytic fragments are intermediates in the oligomerization/aggregation of the Parkinson's disease protein alpha-synuclein as revealed by ion mobility mass spectrometryProtein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseasesParallel manifestations of neuropathologies in the enteric and central nervous systemsPlasma exosomal α-synuclein is likely CNS-derived and increased in Parkinson's disease.The parkin-like human homolog of Drosophila ariadne-1 (HHARI) can induce aggresome formation in mammalian cells and is immunologically detectable in Lewy bodiesThe ubiquitin proteasome system in glia and its role in neurodegenerative diseasesProtein-metal interactions of calmodulin and alpha-synuclein monitored by selective noncovalent adduct protein probing mass spectrometry.Differential effects of glycation on protein aggregation and amyloid formation.Glycation in Demetalated Superoxide Dismutase 1 Prevents Amyloid Aggregation and Produces Cytotoxic Ages Adducts.Mitochondrial quality, dynamics and functional capacity in Parkinson's disease cybrid cell lines selected for Lewy body expression.Identification of glutathione S-transferase pi as a protein involved in Parkinson disease progression.Ribosylation rapidly induces alpha-synuclein to form highly cytotoxic molten globules of advanced glycation end products.The chaperone-like activity of α-synuclein attenuates aggregation of its alternatively spliced isoform, 112-synuclein in vitro: plausible cross-talk between isoforms in protein aggregation.The gut-brain axis: is intestinal inflammation a silent driver of Parkinson's disease pathogenesis?The clustering and spatial arrangement of beta-sheet sequence, but not order, govern alpha-synuclein fibrillogenesisSynphilin-1 enhances α-synuclein aggregation in yeast and contributes to cellular stress and cell death in a Sir2-dependent mannerExtensive enteric nervous system abnormalities in mice transgenic for artificial chromosomes containing Parkinson disease-associated alpha-synuclein gene mutations precede central nervous system changes.Progressive neurodegeneration or endogenous compensation in an animal model of Parkinson's disease produced by decreasing doses of alpha-synuclein.Increased intestinal permeability correlates with sigmoid mucosa alpha-synuclein staining and endotoxin exposure markers in early Parkinson's disease.Expression of human A53T alpha-synuclein in the rat substantia nigra using a novel AAV1/2 vector produces a rapidly evolving pathology with protein aggregation, dystrophic neurite architecture and nigrostriatal degeneration with potential to model tQuantitative analysis of α-synuclein solubility in living cells using split GFP complementationSequestration of cellular interacting partners by protein aggregates: implication in a loss-of-function pathology.p62/SQSTM1-dependent autophagy of Lewy body-like α-synuclein inclusionsA53T human α-synuclein overexpression in transgenic mice induces pervasive mitochondria macroautophagy defects preceding dopamine neuron degenerationCell type specific sequestration of choline acetyltransferase and tyrosine hydroxylase within Lewy bodies.Modeling human neurological disorders with induced pluripotent stem cells.Glycation accelerates fibrillization of the amyloidogenic W7FW14F apomyoglobinCNS expression of glucocerebrosidase corrects alpha-synuclein pathology and memory in a mouse model of Gaucher-related synucleinopathySystematic comparison of the effects of alpha-synuclein mutations on its oligomerization and aggregation.Progressive parkinsonism in mice with respiratory-chain-deficient dopamine neuronsMolecular chaperones in Parkinson's disease--present and futureColonic bacterial composition in Parkinson's disease.NMR Metabolomics Analysis of Parkinson's DiseaseAxon degeneration in Parkinson's diseaseGlucocerebrosidase is present in α-synuclein inclusions in Lewy body disorders.Radiating amyloid fibril formation on the surface of lipid membranes through unit-assembly of oligomeric species of α-synuclein.Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson's disease patients.Protein quality control: the who's who, the where's and therapeutic escapes.Premotor biomarkers for Parkinson's disease - a promising direction of research.
P2860
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P2860
description
2006 nî lūn-bûn
@nan
2006 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Lewy bodies.
@ast
Lewy bodies.
@en
Lewy bodies.
@nl
type
label
Lewy bodies.
@ast
Lewy bodies.
@en
Lewy bodies.
@nl
prefLabel
Lewy bodies.
@ast
Lewy bodies.
@en
Lewy bodies.
@nl
P2860
P356
P1476
Lewy bodies.
@en
P2093
Clifford W Shults
P2860
P304
P356
10.1073/PNAS.0509567103
P407
P577
2006-01-31T00:00:00Z