| Title : The intrinsic instability of the hydrolase domain of lipoprotein lipase facilitates its inactivation by ANGPTL4-catalyzed unfolding - Leth-Espensen_2021_Proc.Natl.Acad.Sci.U.S.A_118_e2026650118 |
| Author(s) : Leth-Espensen KZ , Kristensen KK , Kumari A , Winther AL , Young SG , Jorgensen TJD , Ploug M |
| Ref : Proc Natl Acad Sci U S A , 118 : , 2021 |
| Abstract : Leth-Espensen_2021_Proc.Natl.Acad.Sci.U.S.A_118_e2026650118 |
| ESTHER : Leth-Espensen_2021_Proc.Natl.Acad.Sci.U.S.A_118_e2026650118 |
| PubMedSearch : Leth-Espensen_2021_Proc.Natl.Acad.Sci.U.S.A_118_e2026650118 |
| PubMedID: 33723082 |
| Gene_locus related to this paper: human-LPL |
| Gene_locus related to this paper: human-LPL |
Leth-Espensen KZ, Kristensen KK, Kumari A, Winther AL, Young SG, Jorgensen TJD, Ploug M (2021)
The intrinsic instability of the hydrolase domain of lipoprotein lipase facilitates its inactivation by ANGPTL4-catalyzed unfolding
Proc Natl Acad Sci U S A
118 :
Leth-Espensen KZ, Kristensen KK, Kumari A, Winther AL, Young SG, Jorgensen TJD, Ploug M (2021)
Proc Natl Acad Sci U S A
118 :