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. 2020 Jan 9;2020:6198628. doi: 10.1155/2020/6198628

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Copyright © 2020 Laurits J. Holm et al.

This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Structure and function of PPARs. (a) The peroxisome proliferator-activated receptor (PPAR) isoforms have a large degree of structural overlap, consisting of an N-terminal ligand-independent transactivation domain (NTD). The DNA-binding domain (DBD) contains two zinc finger (Zn) domains, which bind to peroxisome proliferator response element (PPRE) sequences. The DBD is connected through a hinge domain to the C terminal ligand-binding domain (LBD). (b) Illustration of the biological role of PPARs. PPARs heterodimerize with members of the retinoid X receptor (RXR) family. The isoforms are involved in a variety of pathways; shown are pathways with relation to type 1 diabetes. c-jun: transcription factor c-Jun; GLUT2: glucose transporter 2; MafA: MAF bZIP transcription factor A; NFκB: nuclear Factor-kB; Nkx6.1: NK6 homeobox 1; Pdx-1: pancreatic and duodenal homeobox 1; Tfh: follicular helper T cells; Th1: T helper 1 cells; Th17: T helper 17 cells; Th2: T helper 2 cells; TNFα: tumor necrosis factor alpha; Treg: regulatory T cells.