Hsp70 and Hsp40 chaperones do not modulate retinal phenotype in SCA7 mice.
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Mouse models of polyglutamine diseases in therapeutic approaches: review and data table. Part II.cAMP-response element-binding protein and heat-shock protein 70 additively suppress polyglutamine-mediated toxicity in DrosophilaHeat shock protein 70 (hsp70) as an emerging drug target.Preventing polyglutamine-induced activation of c-Jun delays neuronal dysfunction in a mouse model of SCA7 retinopathy.Suppression of protein aggregation by chaperone modification of high molecular weight complexesMolecular chaperones as regulators of cell death.Chaperones in Polyglutamine Aggregation: Beyond the Q-Stretch.Opportunities and challenges for molecular chaperone modulation to treat protein-conformational brain diseasesModulation of Molecular Chaperones in Huntington's Disease and Other Polyglutamine Disorders.Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models.
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Hsp70 and Hsp40 chaperones do not modulate retinal phenotype in SCA7 mice.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年學術文章
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2004年學術文章
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2004年學術文章
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name
Hsp70 and Hsp40 chaperones do not modulate retinal phenotype in SCA7 mice.
@en
type
label
Hsp70 and Hsp40 chaperones do not modulate retinal phenotype in SCA7 mice.
@en
prefLabel
Hsp70 and Hsp40 chaperones do not modulate retinal phenotype in SCA7 mice.
@en
P2860
P50
P356
P1476
Hsp70 and Hsp40 chaperones do not modulate retinal phenotype in SCA7 mice
@en
P2093
Jacques Bonnet
P2860
P304
55969-55977
P356
10.1074/JBC.M409062200
P407
P577
2004-10-19T00:00:00Z