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Altered palmitoylation and neuropathological deficits in mice lacking HIP14.
Huntingtin interacting protein 14 (HIP14, ZDHHC17) is a huntingtin (HTT) interacting protein with palmitoyl transferase activity. In order to interrogate the function of Hip14, we generated mice withExpand
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Wild-type HTT modulates the enzymatic activity of the neuronal palmitoyl transferase HIP14.
Huntington disease (HD) is caused by polyglutamine expansion in the huntingtin (HTT) protein. Huntingtin-interacting protein 14 (HIP14), one of 23 DHHC domain-containing palmitoyl acyl transferasesExpand
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Human Sco1 and Sco2 Function as Copper-binding Proteins*
The function of human Sco1 and Sco2 is shown to be dependent on copper ion binding. Expression of soluble domains of human Sco1 and Sco2 either in bacteria or the yeast cytoplasm resulted in theExpand
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Putting proteins in their place: Palmitoylation in Huntington disease and other neuropsychiatric diseases
Post-translational modification of proteins by the lipid palmitate is critical for protein localization and function. Palmitoylation is regulated by the opposing enzymes palmitoyl acyltransferasesExpand
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Hip14l-deficient mice develop neuropathological and behavioural features of Huntington disease.
Palmitoylation, the dynamic post-translational addition of the lipid, palmitate, to proteins by Asp-His-His-Cys-containing palmitoyl acyltransferase (PAT) enzymes, modulates protein function andExpand
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Memory and synaptic deficits in Hip14/DHHC17 knockout mice
Significance Palmitoylation can influence the subcellular localization of various synaptic proteins; this process is therefore increasingly recognized as an important regulator of basal synapticExpand
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Low Levels of Human HIP14 Are Sufficient to Rescue Neuropathological, Behavioural, and Enzymatic Defects Due to Loss of Murine HIP14 in Hip14−/− Mice
Huntingtin Interacting Protein 14 (HIP14) is a palmitoyl acyl transferase (PAT) that was first identified due to altered interaction with mutant huntingtin, the protein responsible for HuntingtonExpand
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A life without pain? Hedonists take note
  • F. B. Young
  • Medicine, Biology
  • Clinical genetics
  • 7 December 2007
An SCN9A channelopathy causes congenital inability to experience pain
Cox et al. (2006)
Nature 444: 894–898
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When adaptive processes go awry: gain‐of‐function in SCN9A
  • F. B. Young
  • Medicine, Biology
  • Clinical genetics
  • 7 December 2007
SCN9A mutations in paroxysmal extreme pain disorder: allelic variants underlie distinct channel defects and phenotypes
Fertleman et al. (2006)
Neuron 52: 767–774
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