ANGPTL4 inactivates lipoprotein lipase by catalyzing the irreversible unfolding of LPL's hydrolase domain

J Lipid Res. 2020 Sep;61(9):1253. doi: 10.1194/jlr.ILR120000780. Epub 2020 Apr 23.

Authors

Kristian Kølby Kristensen^{1

2}, Katrine Zinck Leth-Espensen^{1

2}, Stephen G Young^{3

4}, Michael Ploug^{1

2}

Affiliations

¹ Finsen Laboratory, Rigshospitalet, DK-2200 Copenhagen N, Denmark.
² Biotech Research and Innovation Centre (BRIC), University of Copenhagen, DK-2200 Copenhagen N, Denmark.
³ Department of Medicine, University of California, Los Angeles, CA 90095, USA.
⁴ Department of Human Genetics, University of California, Los Angeles, CA 90095, USA.

No abstract available

Publication types

Editorial

MeSH terms

Angiopoietin-Like Protein 4 / metabolism*
Biocatalysis*
Enzyme Activation
Hydrolases / metabolism*
Lipoprotein Lipase / chemistry*
Lipoprotein Lipase / metabolism*
Protein Domains

Substances

Angiopoietin-Like Protein 4
Hydrolases
Lipoprotein Lipase

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