Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70.
about
Drosophila NMNAT maintains neural integrity independent of its NAD synthesis activityIdentification of human proteins that modify misfolding and proteotoxicity of pathogenic ataxin-1Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulationCharacterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independentlyAtaxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALSASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeatsAn arginine/lysine-rich motif is crucial for VCP/p97-mediated modulation of ataxin-3 fibrillogenesis.Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptorsThe diverse members of the mammalian HSP70 machine show distinct chaperone-like activitiesLive-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis.Dissecting the pathological effects of human Abeta40 and Abeta42 in Drosophila: a potential model for Alzheimer's diseaseThe Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: neuropathologic and genetic evidence for a role in Huntington's disease pathogenesisImproved activities of CREB binding protein, heterogeneous nuclear ribonucleoproteins and proteasome following downregulation of noncoding hsromega transcripts help suppress poly(Q) pathogenesis in fly modelsThe neuroprotective properties of calorie restriction, the ketogenic diet, and ketone bodiesModel systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicityThe wonderous chaperones: A highlight on therapeutics of cancer and potentially malignant disordersTargeting heat shock proteins to modulate α-synuclein toxicityHeat shock transcription factor 1 as a therapeutic target in neurodegenerative diseasesGenome-wide screen for modifiers of ataxin-3 neurodegeneration in DrosophilaCrystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domainDrosophila as an In Vivo Model for Human Neurodegenerative DiseaseAmyloid-associated activity contributes to the severity and toxicity of a prion phenotypeProtein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiPRiluzole increases the amount of latent HSF1 for an amplified heat shock response and cytoprotectionIn vivo generation of neurotoxic prion protein: role for hsp70 in accumulation of misfolded isoformsOverexpression of human and fly frataxins in Drosophila provokes deleterious effects at biochemical, physiological and developmental levelsHSF1 protects neurons through a novel trimerization- and HSP-independent mechanismInteractions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assemblyHeat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar speciesComparative genomics of the eukaryotesProteotoxic stress and inducible chaperone networks in neurodegenerative disease and agingThe threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegansAn expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta -fibrils.Therapeutic prospects for spinocerebellar ataxia type 2 and 3.Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease.Neuronal circuitry regulates the response of Caenorhabditis elegans to misfolded proteinsHeat shock protein 70 prevents both tau aggregation and the inhibitory effects of preexisting tau aggregates on fast axonal transport.Exogenous delivery of chaperonin subunit fragment ApiCCT1 modulates mutant Huntingtin cellular phenotypesPGC-1α rescues Huntington's disease proteotoxicity by preventing oxidative stress and promoting TFEB function.A survey of human disease gene counterparts in the Drosophila genome
P2860
Q21090222-F3B01B18-846A-43D5-B7FB-47D7CDC1A1B1Q21144909-CB223EFA-0824-4E99-87AF-4B279CA3989FQ24290515-817607CF-0540-44B3-B4FE-269C41955F16Q24292471-FC67DDDF-05EF-4A92-AA18-4572C0E66599Q24297462-D659ED8B-45FE-48AA-8D18-E7D89CF982EAQ24298956-78D9F6CB-637A-4F55-8CE3-DF6495471D94Q24307381-1F3EBF57-8E61-44B4-B750-0C32A63D7A49Q24316293-60F04DE1-3506-4CA5-B8AB-727648E6DC33Q24336905-0CD9BA76-D633-484A-AC33-3BBEAD91575DQ24534867-893304AB-AA19-4EC6-9E4C-7374B8C1141FQ24564815-D4C292F3-569F-406A-9271-88F41C43EECAQ24616907-D3B96CA7-95A2-4C36-8339-01FB034102B5Q24626685-61552613-BD78-47EE-A4CF-B71CD53A832EQ24646616-B8E0195C-C353-4C71-97A0-8CD6E5C8AE0FQ26739032-5A16120D-8C47-4E09-AFAE-8BD6BFD7CF02Q26775973-80539014-9CD7-4B07-B612-C21606C9250DQ26827066-25A1B862-5AEB-48F0-99ED-AAFD5FC23283Q27026884-F5F93CD0-FCA0-4FFC-AE27-F1B9C31689E7Q27314808-8E7A4279-9869-440E-AF02-85705BCF7F48Q27641905-076385FF-B2C8-419B-8C09-355DD686A96BQ28088777-D35BC9FE-E03C-4890-A288-BBA629DB8DFBQ28243882-4248ADFB-B6B4-48B5-B522-71F4614971A4Q28268556-202F37CA-9857-4459-98EE-6D6034ACC0AEQ28473241-88A1FA65-D39B-4BA5-81CD-2123EEEF101BQ28475550-79E62624-7AEA-4FC0-864A-9AA21E821559Q28479044-33B0D6EA-8AC2-4DBD-8144-1FB636DDA3EFQ28582569-841ADC89-FE96-4D0C-891D-98A332F73714Q28910341-E6A94D0C-6151-47D2-A561-1055BDC5B2DAQ28910363-417F9C6B-B152-4947-89AC-61B9200D1E17Q29547504-5BF8FEC6-F6B0-4F17-8FE9-BE418D4DC4BEQ29614783-053F3ADC-A99B-4F46-BDDC-463F38BACFEDQ29619760-3A6A11E9-7D56-4965-BD40-E416E76F9D64Q30328684-0D4EF7C5-77D3-4A13-BDD6-E52BAB7BC1C8Q30410969-C63AB4AA-F02B-4685-A0C6-7643D0616305Q30474580-B9CA860E-557E-4CCB-BEF9-A2E0835EEA52Q30503728-5E45678D-A2DC-4BFB-BD9B-63BC87DC8276Q30519474-99C6CFD5-787F-456B-8B33-2F338A337BC6Q30536567-CFDF649D-7792-4024-AB4A-80CAEF1BB093Q30583566-DA3FB67B-22D7-4C00-9292-422FB7592DC5Q30887434-679C4863-60E6-4BAE-95C7-9D066F8C895F
P2860
Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
Suppression of polyglutamine-m ...... the molecular chaperone HSP70.
@en
Suppression of polyglutamine-m ...... the molecular chaperone HSP70.
@nl
type
label
Suppression of polyglutamine-m ...... the molecular chaperone HSP70.
@en
Suppression of polyglutamine-m ...... the molecular chaperone HSP70.
@nl
prefLabel
Suppression of polyglutamine-m ...... the molecular chaperone HSP70.
@en
Suppression of polyglutamine-m ...... the molecular chaperone HSP70.
@nl
P2093
P356
P1433
P1476
Suppression of polyglutamine-m ...... the molecular chaperone HSP70
@en
P2093
G L Gray-Board
H L Paulson
J M Warrick
N M Bonini
P2888
P304
P356
10.1038/70532
P407
P50
P577
1999-12-01T00:00:00Z