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SM-20, EGL-9, and the EGLN family of hypoxia-inducible factor prolyl hydroxylases
Journal article   Open access   Peer reviewed

SM-20, EGL-9, and the EGLN family of hypoxia-inducible factor prolyl hydroxylases

Robert S Freeman, Daphne M Hasbani, Elizabeth A Lipscomb, Jennifer A Straub and Liang Xie
Molecules and cells, v 16(1), pp 1-12
31 Aug 2003
PMID: 14503838
url
https://doi.org/10.1016/S1016-8478(23)13758-7View
Published, Version of Record (VoR) Open

Abstract

Key to the transduction of signals from the environment to the cell nucleus are enzymes that post-translationally modify proteins. Modifications such as protein phosphorylation have long been known to regulate protein interactions, stability, and localization, as well as enzyme activity. Recent investigations into how cells respond to varying oxygen levels have identified a new mechanism for regulating signal transduction involving the post-translational hydroxylation of proline. The enzymes that catalyze this reaction comprise a novel family of prolyl hydroxylases, which include a growth-factor-responsive and cell-death-related protein (SM-20) in mammals, and a protein (EGL-9) in C. elegans important for normal egg laying.

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Web of Science research areas
Biochemistry & Molecular Biology
Cell Biology
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