Cargando…
ANGPTL4 sensitizes lipoprotein lipase to PCSK3 cleavage by catalyzing its unfolding
Autores principales: | Lund Winther, Anne-Marie, Kumari, Anni, Young, Stephen G., Ploug, Michael |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8175412/ https://www.ncbi.nlm.nih.gov/pubmed/33771536 http://dx.doi.org/10.1016/j.jlr.2021.100071 |
Ejemplares similares
-
Low Density Lipoprotein Binds to Proprotein Convertase Subtilisin/Kexin Type-9 (PCSK9) in Human Plasma and Inhibits PCSK9-mediated Low Density Lipoprotein Receptor Degradation
por: Kosenko, Tanja, et al.
Publicado: (2013) -
The Importance of Lipoprotein Lipase Regulation in Atherosclerosis
por: Kumari, Anni, et al.
Publicado: (2021) -
A transient amphipathic helix in the prodomain of PCSK9 facilitates binding to low-density lipoprotein particles
por: Sarkar, Samantha K., et al.
Publicado: (2020) -
Inverse effects of APOC2 and ANGPTL4 on the conformational dynamics of lid-anchoring structures in lipoprotein lipase
por: Kumari, Anni, et al.
Publicado: (2023) -
The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding
por: Mysling, Simon, et al.
Publicado: (2016)