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- W2013504083 abstract "Despite a century of intensive investigation the effective treatment of protein aggregation diseases remains elusive. Ordinarily, molecular chaperones ensure that proteins maintain their functional conformation. The appearance of misfolded proteins that aggregate implies the collapse of the cellular chaperone quality control network. That said, the cellular chaperone network is extensive and functional information regarding the detailed action of specific chaperones is not yet available. J proteins (DnaJ/Hsp40) are a family of chaperone cofactors that harness Hsc70 (heat shock cognate protein of 70kDa) for diverse conformational cellular tasks and, as such, represent novel clinically relevant targets for diseases resulting from the disruption of proteostasis. Here we review incisive reports identifying mutations in individual J protein chaperones and the proteostasis collapse that ensues." @default.
- W2013504083 created "2016-06-24" @default.
- W2013504083 creator A5064484932 @default.
- W2013504083 creator A5071287301 @default.
- W2013504083 date "2014-07-08" @default.
- W2013504083 modified "2023-09-24" @default.
- W2013504083 title "J protein mutations and resulting proteostasis collapse" @default.
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- W2013504083 doi "https://doi.org/10.3389/fncel.2014.00191" @default.
- W2013504083 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4086201" @default.
- W2013504083 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25071450" @default.
- W2013504083 hasPublicationYear "2014" @default.
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