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. 2019 Jun 20;51(6):68. doi: 10.1038/s12276-019-0235-1

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — In oxygenated conditions, HIF is hydroxylated on proline residues by prolyl-4-hydroxylases (PHDs) and polyubiquitinated by the von Hippel–Lindau protein (pVHL). This leads to degradation of HIF by the 26S proteasome system. In hypoxic conditions, HIF is stabilized and translocated into the nucleus, where it binds to its dimerization partner HIF1B and enhances the transcription of HIF target genes