Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo. - Wikidata - wikimedia - TriplyDB

Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo.

Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo.

http://www.wikidata.org/entity/Q37102231

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Reduced glucocerebrosidase is associated with increased α-synuclein in sporadic Parkinson's disease Glucocerebrosidase is shaking up the synucleinopathies Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling Role of the Retromer Complex in Neurodegenerative Diseases The Potential Role of the Proteases Cathepsin D and Cathepsin L in the Progression and Metastasis of Epithelial Ovarian Cancer Genetically engineered mouse models of Parkinson's disease Genetics in Parkinson disease: Mendelian versus non-Mendelian inheritance Parkinson Disease-linked Vps35 R524W Mutation Impairs the Endosomal Association of Retromer and Induces α-Synuclein Aggregation NADPH oxidase promotes Parkinsonian phenotypes by impairing autophagic flux in an mTORC1-independent fashion in a cellular model of Parkinson's disease Excess α-synuclein worsens disease in mice lacking ubiquitin carboxy-terminal hydrolase L1 Comprehensive functional characterization of murine infantile Batten disease including Parkinson-like behavior and dopaminergic markers.Astrocytic expression of Parkinson's disease-related A53T alpha-synuclein causes neurodegeneration in mice.Genetic regulation of alpha-synuclein mRNA expression in various human brain tissues.Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy Long-Term Assessment of AAV-Mediated Zinc Finger Nuclease Expression in the Mouse Brain.Lysosomal function in macromolecular homeostasis and bioenergetics in Parkinson's disease.Low-dose bafilomycin attenuates neuronal cell death associated with autophagy-lysosome pathway dysfunction.The pallidopyramidal syndromes: nosology, aetiology and pathogenesis.Lack of interleukin-1 type 1 receptor enhances the accumulation of mutant huntingtin in the striatum and exacerbates the neurological phenotypes of Huntington's disease mice.α-Synuclein Transgenic Drosophila As a Model of Parkinson's Disease and Related Synucleinopathies.Mitochondrial dysfunction in Parkinson's disease: pathogenesis and neuroprotection.Cyclin-G-associated kinase modifies α-synuclein expression levels and toxicity in Parkinson's disease: results from the GenePD Study.Accumulation of α-synuclein in dementia with Lewy bodies is associated with decline in the α-synuclein-degrading enzymes kallikrein-6 and calpain-1.A neurodegeneration-specific gene-expression signature of acutely isolated microglia from an amyotrophic lateral sclerosis mouse model Drosophila models of Parkinson's disease: discovering relevant pathways and novel therapeutic strategies.Genetic variations of GAK in two Chinese Parkinson's disease populations: a case-control study.Proteolytic characteristics of cathepsin D related to the recognition and cleavage of its target proteins.Systems biology of the autophagy-lysosomal pathway.Solid microparticles based on chitosan or methyl-β-cyclodextrin: a first formulative approach to increase the nose-to-brain transport of deferoxamine mesylate Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies.α-Synuclein-independent histopathological and motor deficits in mice lacking the endolysosomal Parkinsonism protein Atp13a2.New roles of glycosaminoglycans in α-synuclein aggregation in a cellular model of Parkinson disease.Autophagy in dementias.The Interplay between Alpha-Synuclein Clearance and Spreading Cysteine cathepsins are essential in lysosomal degradation of α-synuclein.Sustained Systemic Glucocerebrosidase Inhibition Induces Brain α-Synuclein Aggregation, Microglia and Complement C1q Activation in Mice.Mutation of the parkinsonism gene ATP13A2 causes neuronal ceroid-lipofuscinosis Parkinson's disease-linked LRRK2 is expressed in circulating and tissue immune cells and upregulated following recognition of microbial structures α-Synuclein in human cerebrospinal fluid is principally derived from neurons of the central nervous system.Mannose 6-Phosphate Receptor Is Reduced in -Synuclein Overexpressing Models of Parkinsons Disease.

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Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo.

http://www.wikidata.org/entity/Q37102231

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article científic

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scientific article published on 09 February 2009

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Cathepsin D expression level a ...... egation, and toxicity in vivo.

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Cathepsin D expression level a ...... egation, and toxicity in vivo.

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Cathepsin D expression level a ...... egation, and toxicity in vivo.

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Cathepsin D expression level a ...... egation, and toxicity in vivo.

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Cathepsin D expression level a ...... egation, and toxicity in vivo.

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Cathepsin D expression level a ...... egation, and toxicity in vivo.

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Molecular Brain

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Cathepsin D expression level a ...... regation, and toxicity in vivo

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Anders Paetau

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Erika Swinton

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Heather Boston

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Jaana Tyynelä

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John Woulfe

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Juliana Ng

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Liisa Myllykangas

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Maria Lindfors

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Mel B Feany

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Paul Saftig

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Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

Dopamine covalently modifies and functionally inactivates parkin

Mutation in the alpha-synuclein gene identified in families with Parkinson's disease

alpha-Synuclein locus triplication causes Parkinson's disease

Alpha-synuclein in Lewy bodies

Cathepsin D--many functions of one aspartic protease

Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells

Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein

Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease

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10.1186/1756-6606-2-5

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