2014
DOI: 10.1021/cn500075u
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The Potential of Indole and a Synthetic Derivative for PolyQ Aggregation Reduction by Enhancement of the Chaperone and Autophagy Systems

Abstract: In polyglutamine (polyQ)-mediated disorders, the expansion of translated CAG repeats in the disease genes result in long polyQ tracts in their respective proteins, leading to intracellular accumulation of aggregated polyQ proteins, production of reactive oxygen species, and cell death. The molecular chaperones act in preventing protein misfolding and aggregation, thus inhibiting a wide range of harmful downstream events. In the circumstance of accumulation of aggregated polyQ proteins, the autophagic pathway i… Show more

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Cited by 17 publications
(16 citation statements)
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“…Therapeutic approaches vary, 4 but they typically fail to sufficiently alleviate symptoms. [5][6][7][8][9] Most degenerative ataxias feature Purkinje cell loss, 10,11 resulting in modified inputs to the deep cerebellar nuclei; thus, neuromodulation targeting these deep cerebellar nuclei may succeed in numerous DCAs.…”
mentioning
confidence: 99%
“…Therapeutic approaches vary, 4 but they typically fail to sufficiently alleviate symptoms. [5][6][7][8][9] Most degenerative ataxias feature Purkinje cell loss, 10,11 resulting in modified inputs to the deep cerebellar nuclei; thus, neuromodulation targeting these deep cerebellar nuclei may succeed in numerous DCAs.…”
mentioning
confidence: 99%
“…The collection from the UrFU was employed to search for the activators of Hsp70 synthesis; the chemicals were selected based on the similarity of their domain to the indole-like pharmacophore found earlier that increased the Hsp70 level [35]. We used the reporter assay comprised of rat C6 glioma cells expressing the luciferase gene under the control of the HSE promotor.…”
Section: Identification Of Hsp70 Inducersmentioning
confidence: 99%
“…Hsp40 overexpression decreased mutant ataxin-3 aggregation while increasing its levels in cells, prompting the hypothesis that Hsp40 may bind mutant ataxin-3 and delay its degradation [33]. Hsp70 overexpression decreased mutant protein aggregation in SCA3, SCA7 and DRPLA cellular models [128,204,205]. In a SCA3 Drosophila model, overexpression of Hsp40 or Hsp70 reduced mutant ataxin-3 induced toxicity.…”
Section: Genetic Modulation Of Molecular Chaperones In Scas and Drplamentioning
confidence: 99%
“…Treatment with GGA decreased mutant protein aggregation in SCA3 and SCA17 cells [205,210], but had no effect on mutant ataxin-3 toxicity in SCA3 Drosophila [141]. Indole and its derivate NC001-8 were recently tested in SCA models.…”
Section: Pharmacological Modulation Of Molecular Chaperones In Scas Amentioning
confidence: 99%
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