Research
Print page Print page
Switch language
The Capital Region of Denmark - a part of Copenhagen University Hospital
Published

ANGPTL4 sensitizes lipoprotein lipase to PCSK3 cleavage by catalyzing its unfolding

Research output: Contribution to journalJournal articleResearchpeer-review

  1. Expression and one-step purification of active lipoprotein lipase contemplated by biophysical considerations

    Research output: Contribution to journalJournal articleResearchpeer-review

  2. Chylomicronemia from GPIHBP1 autoantibodies

    Research output: Contribution to journalReviewResearchpeer-review

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

    Research output: Contribution to journalComment/debateResearchpeer-review

  4. The structural basis for monoclonal antibody 5D2 binding to the tryptophan-rich loop of lipoprotein lipase

    Research output: Contribution to journalJournal articleResearchpeer-review

  5. On the mechanism of angiopoietin-like protein 8 for control of lipoprotein lipase activity

    Research output: Contribution to journalJournal articleResearchpeer-review

  1. Expression and one-step purification of active lipoprotein lipase contemplated by biophysical considerations

    Research output: Contribution to journalJournal articleResearchpeer-review

  2. The Urokinase Receptor (uPAR) as a "Trojan Horse" in Targeted Cancer Therapy: Challenges and Opportunities

    Research output: Contribution to journalReviewResearchpeer-review

  3. The Importance of Lipoprotein Lipase Regulation in Atherosclerosis

    Research output: Contribution to journalReviewResearchpeer-review

  4. The intrinsic instability of the hydrolase domain of lipoprotein lipase facilitates its inactivation by ANGPTL4-catalyzed unfolding

    Research output: Contribution to journalJournal articleResearchpeer-review

View graph of relations
Original languageEnglish
JournalJournal of Lipid Research
Volume62
Pages (from-to)100071
ISSN0022-2275
DOIs
Publication statusPublished - 23 Mar 2021

ID: 64649579