Pharmacological promotion of inclusion formation: a therapeutic approach for Huntington's and Parkinson's diseases. - Wikidata - awgldk - TriplyDB

Pharmacological promotion of inclusion formation: a therapeutic approach for Huntington's and Parkinson's diseases.

Pharmacological promotion of inclusion formation: a therapeutic approach for Huntington's and Parkinson's diseases.

http://www.wikidata.org/entity/Q34573066

about

Identifying druggable disease-modifying gene products Longitudinal measures of proteostasis in live neurons: features that determine fate in models of neurodegenerative disease Developing treatment for spinal and bulbar muscular atrophy Protein degradation pathways in Parkinson's disease: curse or blessing Mutant huntingtin gene-dose impacts on aggregate deposition, DARPP32 expression and neuroinflammation in HdhQ150 mice Modulating self-assembly of amyloidogenic proteins as a therapeutic approach for neurodegenerative diseases: strategies and mechanisms Aggresome formation and neurodegenerative diseases: therapeutic implications Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease Genetic interaction between expanded murine Hdh alleles and p53 reveal deleterious effects of p53 on Huntington's disease pathogenesis Chronic treatment with novel small molecule Hsp90 inhibitors rescues striatal dopamine levels but not α-synuclein-induced neuronal cell loss Temporal separation of aggregation and ubiquitination during early inclusion formation in transgenic mice carrying the Huntington's disease mutation Dynamic imaging by fluorescence correlation spectroscopy identifies diverse populations of polyglutamine oligomers formed in vivo.Mutant PFN1 causes ALS phenotypes and progressive motor neuron degeneration in mice by a gain of toxicity.Peptide ligand screening of alpha-synuclein aggregation modulators by in silico panning High throughput screening for neurodegeneration and complex disease phenotypes.Conformational targeting of fibrillar polyglutamine proteins in live cells escalates aggregation and cytotoxicity.Aging is not associated with proteasome impairment in UPS reporter mice.The first N-terminal amino acids of alpha-synuclein are essential for alpha-helical structure formation in vitro and membrane binding in yeast.Modeling Huntington disease in yeast: perspectives and future directions.Synphilin-1 enhances α-synuclein aggregation in yeast and contributes to cellular stress and cell death in a Sir2-dependent manner Therapeutic Strategies in Huntington's Disease Designed α-sheet peptides inhibit amyloid formation by targeting toxic oligomers.Heparin induces harmless fibril formation in amyloidogenic W7FW14F apomyoglobin and amyloid aggregation in wild-type protein in vitro.The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solution Cystamine and intrabody co-treatment confers additional benefits in a fly model of Huntington's disease.Cellular strategies of protein quality control.Are long-range structural correlations behind the aggregration phenomena of polyglutamine diseases?Protein tau: prime cause of synaptic and neuronal degeneration in Alzheimer's disease.The role of alpha-synuclein oligomerization and aggregation in cellular and animal models of Parkinson's disease.Disentangling the relationship between lewy bodies and nigral neuronal loss in Parkinson's disease.Heat-shock protein 70 modulates toxic extracellular α-synuclein oligomers and rescues trans-synaptic toxicity.Is synaptic loss a unique hallmark of Alzheimer's disease?High-Throughput Multiplexed Quantitation of Protein Aggregation and Cytotoxicity in a Huntington's Disease Model.Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation.Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases.Mutual exacerbation of peroxisome proliferator-activated receptor γ coactivator 1α deregulation and α-synuclein oligomerization Amyloid deposits: protection against toxic protein species?RNAi screening in Drosophila cells identifies new modifiers of mutant huntingtin aggregation.Progressive aggregation of alpha-synuclein and selective degeneration of lewy inclusion-bearing neurons in a mouse model of parkinsonism.Neurodegenerative processes in Huntington's disease.

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Pharmacological promotion of inclusion formation: a therapeutic approach for Huntington's and Parkinson's diseases.

http://www.wikidata.org/entity/Q34573066

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2006 nî lūn-bûn

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Proceedings of the National Academy of Sciences of the United States of America

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Aleksey G Kazantsev

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Anne B Young

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David E Housman

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Michele M Maxwell

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Pamela J McLean

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Stephen Altmann

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Tiago Fleming Outeiro

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P2860

The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction

Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.

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

alpha-Synuclein locus triplication causes Parkinson's disease

Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Impairment of the ubiquitin-proteasome system by protein aggregation

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Folding of newly translated proteins in vivo: the role of molecular chaperones

Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae

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Parkinson's disease

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