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January 1, 2021Journal of Lipid ResearchOpen Access

ANGPTL4 sensitizes lipoprotein lipase to PCSK3 cleavage by catalyzing its unfolding

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Design

In vitro hydrogen-deuterium exchange experimental study

Authors

AWAnne-Marie Lund WintherUniversity of CopenhagenAKAnni KumariUniversity of CopenhagenSYStephen G. YoungGeneral Cardiology

Discussion

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Implication

Extends molecular model of LPL regulation by ANGPTL4; leaves open therapeutic targeting in dyslipidemia.

Key Points

Key points are not available for this paper at this time.

Cite This Study

Winther et al. (2021) studied this question.

synapsesocial.com/papers/6a82c2987a209f4aae23bb3chttps://doi.org/10.1016/j.jlr.2021.100071
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1ANGPTL4 inactivates lipoprotein lipase by catalyzing the irreversible unfolding of LPL's hydrolase domain2020 · 21 citations
  2. 2The intrinsic instability of the hydrolase domain of lipoprotein lipase facilitates its inactivation by ANGPTL4-catalyzed unfolding2021 · 48 citations
  3. 3Proteolytic Processing of Angiopoietin-like Protein 4 by Proprotein Convertases Modulates Its Inhibitory Effects on Lipoprotein Lipase Activity2011 · 158 citations
  4. 4Angiopoietin-like 4 promotes the intracellular cleavage of lipoprotein lipase by PCSK3/furin in adipocytes2018 · 72 citations
  5. 5The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding2016 · 121 citations