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CHIP overexpression reduces mutant androgen receptor protein and ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model
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Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species
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In vivo evidence of CHIP up-regulation attenuating tau aggregation
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The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates α-synuclein degradation decisions between proteasomal and lysosomal pathways
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Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes
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CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
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CHIP promotes proteasomal degradation of familial ALS-linked mutant SOD1 by ubiquitinating Hsp/Hsc70
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