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FBP1 acts as a protein phosphatase to dephosphorylate histone H3

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NIAID Data Ecosystem2026-03-14 收录
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https://www.ncbi.nlm.nih.gov/sra/SRP385758
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We report nuclear FBP1 interacts with PPARa and binds to the promoter regions of PPARa-mediated b-oxidation genes. S170-phosphorylated FBP1 with an altered catalytic domain structure functions as a protein phosphatase that dephosphorylates histone H3 at T11 and suppresses PPARa-mediated gene expression. Chromatin immunoprecipitation DNA-sequencing (ChIP-seq) for FBP1 and PPARa with glucose deprivation in L02 cells. Overall design: Examine of FBP1 and PPARa regulated genes under glucose deprivation in L02 cells.
创建时间:
2022-10-05
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