ArticleProceedings of the National Academy of Sciences of the United States of America2019
Structure of lipoprotein lipase in complex with GPIHBP1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
36 citing papers in PubMed, 64 citations in OpenAlex.
- Reduced activity of two LPL C-terminal variants, p.Glu396Val and novel p.Trp417Cys: a clinical, biochemical and structural study.Frontiers in physiology · 2026Article
- Lipoprotein lipase requires a flexible lid and stable C-terminal, both maintained by ApoC-II peptide binding.bioRxiv : the preprint server for biology · 2025Article
- Article
- Review
- A negatively charged cluster in the disordered acidic domain of GPIHBP1 provides selectivity in the interaction with lipoprotein lipase.Scientific reports · 2024Article
- In Silico Description of the Direct Inhibition Mechanism of Endothelial Lipase by ANGPTL3.International journal of molecular sciences · 2024Article
- Review
- Polysorbates degrading enzymes in biotherapeutics - a current status and future perspectives.Frontiers in bioengineering and biotechnology · 2024Review
- Nonlinear relationship between serum 25-hydroxyvitamin D and lipid profile in Chinese adults.Frontiers in nutrition · 2024Article
- Macromolecular Interactions of Lipoprotein Lipase (LPL).Sub-cellular biochemistry · 2024Review
- Structure of dimeric lipoprotein lipase reveals a pore adjacent to the active site.Nature communications · 2023Article
- Combined action of albumin and heparin regulates lipoprotein lipase oligomerization, stability, and ligand interactions.PloS one · 2023Article
- A protein of capillary endothelial cells, GPIHBP1, is crucial for plasma triglyceride metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Identification of a Gain-of-FunctionCirculation · 2022Article
- Crystal Structures of the Plant Phospholipase A1 Proteins Reveal a Unique Dimerization Domain.Molecules (Basel, Switzerland) · 2022Article
- A homozygous variant in theFrontiers in genetics · 2022Article
- Heparin binding triggers human VLDL remodeling by circulating lipoprotein lipase: Relevance to VLDL functionality in health and disease.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2022Article
- Adiponectin, May Be a Potential Protective Factor for Obesity-Related Osteoarthritis.Diabetes, metabolic syndrome and obesity : targets and therapy · 2022Review
- Identification and Characterization of Two Novel Compounds: Heterozygous Variants ofFrontiers in endocrinology · 2022Article
- The Importance of Lipoprotein Lipase Regulation in Atherosclerosis.Biomedicines · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
23 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipoprotein lipase (LPL) plays a central role in triglyceride (TG) metabolism. By catalyzing the hydrolysis of TGs present in TG-rich lipoproteins (TRLs), LPL facilitates TG utilization and regulates circulating TG and TRL concentrations. Until very recently, structural information for LPL was limited to homology models, presumably due to the propensity of LPL to unfold and aggregate. By coexpressing LPL with a soluble variant of its accessory protein glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1 (GPIHBP1) and with its chaperone protein lipase maturation factor 1 (LMF1), we obtained a stable and homogenous LPL/GPIHBP1 complex that was suitable for structure determination. We report here X-ray crystal structures of human LPL in complex with human GPIHBP1 at 2.5-3.0 Å resolution, including a structure with a novel inhibitor bound to LPL. Binding of the inhibitor resulted in ordering of the LPL lid and lipid-binding regions and thus enabled determination of the first crystal structure of LPL that includes these important regions of the protein. It was assumed for many years that LPL was only active as a homodimer. The structures and additional biochemical data reported here are consistent with a new report that LPL, in complex with GPIHBP1, can be active as a monomeric 1:1 complex. The crystal structures illuminate the structural basis for LPL-mediated TRL lipolysis as well as LPL stabilization and transport by GPIHBP1.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.