| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8298036 | Biochemical and Biophysical Research Communications | 2011 | 5 Pages |
Abstract
⺠We performed comprehensive PTM analysis for HNF4α protein. ⺠We identified 8 PTMs in HNF4α protein including newly identified PTMs. ⺠Among them, we found acetylation at lysine 458 was one of the prime PTMs for HNF4α function. ⺠Acetylation at lysine 458 was inhibitory for HNF4α transcription function. ⺠This modification fluctuated in response to extracellular condition.
Keywords
PTMqPCRCIDFDRapoCIIIETDHNF4αApolipoprotein CIIISDS–PAGECollision-induced dissociationAcetylationpost-translational modificationsodium dodecyl sulfate–polyacrylamide gel electrophoresisElectron transfer dissociationdirect repeatquantitative reverse transcription-PCRhepatocyte nuclear factor 4αfalse discovery rate
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Authors
Atsushi Yokoyama, Shogo Katsura, Ryo Ito, Waka Hashiba, Hiroki Sekine, Ryoji Fujiki, Shigeaki Kato,