Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy - Wikidata - awgldk - TriplyDB

Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

http://www.wikidata.org/entity/Q24683089

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Genetic perspective on the role of the autophagy-lysosome pathway in Parkinson disease Chaperone-mediated autophagy: molecular mechanisms and physiological relevance The role of oxidative stress in Parkinson's disease Interplay of LRRK2 with chaperone-mediated autophagy Reduced glucocerebrosidase is associated with increased α-synuclein in sporadic Parkinson's disease Glycation-altered proteolysis as a pathobiologic mechanism that links dietary glycemic index, aging, and age-related disease (in nondiabetics)Chaperone-mediated autophagy: a unique way to enter the lysosome world Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing Neuroinflammation in Multiple System Atrophy: Response to and Cause of α-Synuclein Aggregation Unfolded Protein Response and Macroautophagy in Alzheimer's, Parkinson's and Prion Diseases Redox control of protein degradation Relevance of chronic stress and the two faces of microglia in Parkinson's disease Mitochondrial biology and Parkinson's disease Genetically engineered mouse models of Parkinson's disease Autophagy and disease: always two sides to a problem Chaperone-mediated autophagy: roles in neurodegeneration Oxidative stress induces autophagy in response to multiple noxious stimuli in retinal ganglion cells Protein degradation pathways in Parkinson's disease: curse or blessing Edaravone guards dopamine neurons in a rotenone model for Parkinson's disease Seeking a mechanism for the toxicity of oligomeric α-synuclein Parkinson's disease as a result of aging Autophagy in neurodegenerative diseases: from mechanism to therapeutic approach VPS35 in Dopamine Neurons Is Required for Endosome-to-Golgi Retrieval of Lamp2a, a Receptor of Chaperone-Mediated Autophagy That Is Critical for α-Synuclein Degradation and Prevention of Pathogenesis of Parkinson's Disease ATP13A2 and Alpha-synuclein: a Metal Taste in Autophagy ATP13A2 regulates mitochondrial bioenergetics through macroautophagy PARK9-associated ATP13A2 localizes to intracellular acidic vesicles and regulates cation homeostasis and neuronal integrity Gene-environment interactions: key to unraveling the mystery of Parkinson's disease Interactions of iron, dopamine and neuromelanin pathways in brain aging and Parkinson's disease Autophagy gone awry in neurodegenerative diseases Heat shock proteins: cellular and molecular mechanisms in the central nervous system.Mitochondrial metabolism in Parkinson's disease impairs quality control autophagy by hampering microtubule-dependent traffic.Stereotaxical infusion of rotenone: a reliable rodent model for Parkinson's disease.Cathepsin D is the main lysosomal enzyme involved in the degradation of alpha-synuclein and generation of its carboxy-terminally truncated species.Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy Dopamine-induced conformational changes in alpha-synuclein Alpha-synuclein overexpression increases dopamine toxicity in BE2-M17 cells Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases MHC-I expression renders catecholaminergic neurons susceptible to T-cell-mediated degeneration Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathies

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P2860

Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

http://www.wikidata.org/entity/Q24683089

description

2008 nî lūn-bûn

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2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի փետրվարին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

@ast

Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

@en

Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

@nl

type

label

Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

@ast

Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

@en

Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

@nl

prefLabel

Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

@ast

Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

@en

Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

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Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

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Du-Chu Wu

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Eugene V Mosharov

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Harry Ischiropoulos

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Joseph Mazzulli

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Peter T Lansbury

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Roberto Hodara

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Ross Fredenburg

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Zsolt Talloczy

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P2860

A receptor for the selective uptake and degradation of proteins by lysosomes

Activation of chaperone-mediated autophagy during oxidative stress

Mechanisms of chaperone-mediated autophagy

Degradative organelles containing mislocalized alpha-and beta-synuclein proliferate in presenilin-1 null neurons

Unique properties of lamp2a compared to other lamp2 isoforms

A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins

Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system

Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy

Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders

Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct.

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777-88

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2329676

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10.1172/JCI32806

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P433

2

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118

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Ana María Cuervo

Susmita Kaushik

Marta Martinez-Vicente

Antonia Follenzi

William T Dauer

Serge Przedborski

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2008-02-01T00:00:00Z

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5676543

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18172548

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molecular chaperones

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2157565

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