The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Comparison of angiopoietin-like protein 3 and 4 reveals structural and mechanistic similarities
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“As with ANGPTL4, ANGPTL3 oligomerizes, appearing to form trimers or hexamers, and oligomerization is mediated by the N-terminal domain (72, 100).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [100]
Experimental — accuracy not yet measuredIn the citing paper
“This mechanism has not yet been universally accepted and studies from the laboratory of Saskia Neher have suggested that ANGPTL4 acts as a reversible, uncompetitive inhibitor of LPL (53, 100).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [100]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Genetic and Pharmacologic Inactivation of ANGPTL3 and Cardiovascular Disease
Dewey, F. E., Gusarova, V., Dunbar, R. L., O’Dushlaine, C., Schurmann, C., Gottesman, O., McCarthy, S., Van Hout, C. V., Bruse, S., Dansky, H. M., et al. (2017) · New England Journal of Medicine · doi:10.1056/nejmoa1612790 · Cited by 885
Inactivating Variants in ANGPTL4 and Risk of Coronary Artery Disease
Dewey, F. E., Gusarova, V., O’Dushlaine, C., Gottesman, O., Trejos, J., Hunt, C., Van Hout, C. V., Habegger, L., Buckler, D., Lai, K.-M. V., et al. (2016) · New England Journal of Medicine · doi:10.1056/nejmoa1510926 · Cited by 497
Coding Variation in ANGPTL4, LPL, and SVEP1 and the Risk of Coronary Disease
Myocardial Infarction Genetics and CARDIoGRAM Exome Consortia Investigators (2016) · New England Journal of Medicine · doi:10.1056/nejmoa1507652 · Cited by 493
ANGPTL3 deficiency and protection against coronary artery disease
Stitziel, N. O., Khera, A. V., Wang, X., Bierhals, A. J., Vourakis, A. C., Sperry, A. E., Natarajan, P., Klarin, D., Emdin, C. A., Zekavat, S. M., et al. (2017) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2017.02.030 · Cited by 467
Identification of a mammalian angiopoietin-related protein expressed specifically in liver
Conklin, D., Gilbertson, D., Taft, D. W., Maurer, M. F., Whitmore, T. E., Smith, D. L., Walker, K. M., Chen, L. H., Wattler, S., Nehls, M., et al. (1999) · Genomics · doi:10.1006/geno.1999.6041 · Cited by 169
Flagged first, then by citations
Research works printed but not linked: 55
- Dijk, 2016, Regulation of lipid metabolism by angiopoietin-like proteins, Curr. Opin. Lipidol., 27, 249, 10.1097/MOL.0000000000000290 · DOI
- Fried, 1983, Prolonged effects of fasting-refeeding on rat adipose tissue lipoprotein lipase activity: Influence of caloric restriction during refeeding, J. Nutr., 113, 1861, 10.1093/jn/113.9.1861 · DOI
- Quig, 1983, The influence of starvation and refeeding on the lipoprotein lipase activity of skeletal muscle and adipose tissue of lean and obese Zucker rats, J. Nutr., 113, 1150, 10.1093/jn/113.6.1150 · DOI
- Zhang, 2016, The ANGPTL3-4-8 model, a molecular mechanism for triglyceride trafficking, Open Biol., 6, 150272, 10.1098/rsob.150272 · DOI
- Kersten, 2000, Characterization of the fasting-induced adipose factor FIAF, a novel peroxisome proliferator-activated receptor target gene, J. Biol. Chem., 275, 28488, 10.1074/jbc.M004029200 · DOI · Paper page
- Zhang, 2012, Lipasin, a novel nutritionally-regulated liver-enriched factor that regulates serum triglyceride levels, Biochem. Biophys. Res. Commun., 424, 786, 10.1016/j.bbrc.2012.07.038 · DOI · Paper page
- Chi, 2017, ANGPTL8 promotes the ability of ANGPTL3 to bind and inhibit lipoprotein lipase, Mol. Metab., 6, 1137, 10.1016/j.molmet.2017.06.014 · DOI · Paper page
- Haller, 2017, ANGPTL8 requires ANGPTL3 to inhibit lipoprotein lipase and plasma triglyceride clearance, J. Lipid Res., 58, 1166, 10.1194/jlr.M075689 · DOI · Paper page
- Kovrov, 2019, On the mechanism of angiopoietin-like protein 8 for control of lipoprotein lipase activity, J. Lipid Res., 60, 783, 10.1194/jlr.M088807 · DOI · Paper page
- Chen, 2020, Angiopoietin-like protein 8 differentially regulates ANGPTL3 and ANGPTL4 during postprandial partitioning of fatty acids, J. Lipid Res., 61, 1203, 10.1194/jlr.RA120000781 · DOI · Paper page
- Willer, 2008, Newly identified loci that influence lipid concentrations and risk of coronary artery disease, Nat. Genet., 40, 161, 10.1038/ng.76 · DOI · Paper page
- Peloso, 2014, Association of low-frequency and rare coding-sequence variants with blood lipids and coronary heart disease in 56,000 whites and blacks, Am. J. Hum. Genet., 94, 223, 10.1016/j.ajhg.2014.01.009 · DOI
- Leiherer, 2020, High betatrophin in coronary patients protects from cardiovascular events, Atherosclerosis, 293, 62, 10.1016/j.atherosclerosis.2019.11.011 · DOI
- Essalmani, 2013, Furin is the primary in vivo convertase of angiopoietin-like 3 and endothelial lipase in hepatocytes, J. Biol. Chem., 288, 26410, 10.1074/jbc.M113.501304 · DOI · Paper page
- Yin, 2009, Genetic variation in ANGPTL4 provides insights into protein processing and function, J. Biol. Chem., 284, 13213, 10.1074/jbc.M900553200 · DOI · Paper page
- Lei, 2011, Proteolytic processing of angiopoietin-like protein 4 by proprotein convertases modulates its inhibitory effects on lipoprotein lipase activity, J. Biol. Chem., 286, 15747, 10.1074/jbc.M110.217638 · DOI · Paper page
- Ono, 2003, Protein region important for regulation of lipid metabolism in angiopoietin-like 3 (ANGPTL3): ANGPTL3 is cleaved and activated in vivo, J. Biol. Chem., 278, 41804, 10.1074/jbc.M302861200 · DOI · Paper page
- Lee, 2009, Identification of a new functional domain in angiopoietin-like 3 (ANGPTL3) and angiopoietin-like 4 (ANGPTL4) involved in binding and inhibition of lipoprotein lipase (LPL), J. Biol. Chem., 284, 13735, 10.1074/jbc.M807899200 · DOI · Paper page
- Shan, 2009, The angiopoietin-like proteins ANGPTL3 and ANGPTL4 inhibit lipoprotein lipase activity through distinct mechanisms, J. Biol. Chem., 284, 1419, 10.1074/jbc.M808477200 · DOI · Paper page
- Sonnenburg, 2009, GPIHBP1 stabilizes lipoprotein lipase and prevents its inhibition by angiopoietin-like 3 and angiopoietin-like 4, J. Lipid Res., 50, 2421, 10.1194/jlr.M900145-JLR200 · DOI · Paper page
- Reimund, 2017, Lipoprotein lipase activity and interactions studied in human plasma by isothermal titration calorimetry, J. Lipid Res., 58, 279, 10.1194/jlr.D071787 · DOI · Paper page
- Nimonkar, 2020, A lipoprotein lipase-GPI-anchored high-density lipoprotein-binding protein 1 fusion lowers triglycerides in mice: Implications for managing familial chylomicronemia syndrome, J. Biol. Chem., 295, 2900, 10.1074/jbc.RA119.011079 · DOI
- Mysling, 2016, The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding, Elife, 5
- Lafferty, 2013, Angiopoietin-like protein 4 inhibition of lipoprotein lipase: Evidence for reversible complex formation, J. Biol. Chem., 288, 28524, 10.1074/jbc.M113.497602 · DOI · Paper page
- Kristensen, 2020, Unfolding of monomeric lipoprotein lipase by ANGPTL4: Insight into the regulation of plasma triglyceride metabolism, Proc. Natl. Acad. Sci. U. S. A., 117, 4337, 10.1073/pnas.1920202117 · DOI · Paper page
- Biterova, 2018, Structures of Angptl3 and Angptl4, modulators of triglyceride levels and coronary artery disease, Sci. Rep., 8, 6752, 10.1038/s41598-018-25237-7 · DOI · Paper page
- Ge, 2005, Differential regulation and properties of angiopoietin-like proteins 3 and 4, J. Lipid Res., 46, 1484, 10.1194/jlr.M500005-JLR200 · DOI · Paper page
- Yau, 2009, A highly conserved motif within the NH2-terminal coiled-coil domain of angiopoietin-like protein 4 confers its inhibitory effects on lipoprotein lipase by disrupting the enzyme dimerization, J. Biol. Chem., 284, 11942, 10.1074/jbc.M809802200 · DOI · Paper page
- Yoshino, 1987, A graphical method for determining inhibition parameters for partial and complete inhibitors, Biochem. J., 248, 815, 10.1042/bj2480815 · DOI
- Shimamura, 2007, Angiopoietin-like protein3 regulates plasma HDL cholesterol through suppression of endothelial lipase, Arterioscler. Thromb. Vasc. Biol., 27, 366, 10.1161/01.ATV.0000252827.51626.89 · DOI · Paper page
- Cazes, 2006, Extracellular matrix-bound angiopoietin-like 4 inhibits endothelial cell adhesion, migration, and sprouting and alters actin cytoskeleton, Circ. Res., 99, 1207, 10.1161/01.RES.0000250758.63358.91 · DOI
- Gutgsell, 2019, Mapping the sites of the lipoprotein lipase (LPL)-angiopoietin-like protein 4 (ANGPTL4) interaction provides mechanistic insight into LPL inhibition, J. Biol. Chem., 294, 2678, 10.1074/jbc.RA118.005932 · DOI
- Bengtsson-Olivecrona, 1991, Phospholipase activity of milk lipoprotein lipase, Methods Enzymol., 197, 345, 10.1016/0076-6879(91)97160-Z · DOI
- Wu, 2018, Coexpression of novel furin-resistant LPL variants with lipase maturation factor 1 enhances LPL secretion and activity, J. Lipid Res., 59, 2456, 10.1194/jlr.D086793 · DOI · Paper page
- Classen, 2013, Implementation and performance of SIBYLS: A dual endstation small-angle X-ray scattering and macromolecular crystallography beamline at the advanced light source, J. Appl. Crystallogr., 46, 1, 10.1107/S0021889812048698 · DOI
- Dyer, 2014, High-throughput SAXS for the characterization of biomolecules in solution: A practical approach, Methods Mol. Biol., 1091, 245, 10.1007/978-1-62703-691-7_18 · DOI
- Hura, 2013, Comprehensive macromolecular conformations mapped by quantitative SAXS analyses, Nat. Methods, 10, 453, 10.1038/nmeth.2453 · DOI
- Putnam, 2007, X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution, Q. Rev. Biophys., 40, 191, 10.1017/S0033583507004635 · DOI · Paper page
- Forster, 2010, Scatter: Software for the analysis of nano- and mesoscale small-angle scattering, J. Appl. Crystallogr., 43, 639, 10.1107/S0021889810008289 · DOI
- Dominguez-Martin, 2020, Structural analysis of a new carotenoid-binding protein: The C-terminal domain homolog of the OCP, Sci. Rep., 10, 15564, 10.1038/s41598-020-72383-y · DOI
- Knott, 2019, Structural basis for AcrVA4 inhibition of specific CRISPR-Cas12a, Elife, 8, 10.7554/eLife.49110 · DOI
- Fischetti, 2004, The BioCAT undulator beamline 18ID: A facility for biological non-crystalline diffraction and X-ray absorption spectroscopy at the advanced photon source, J. Synchrotron Radiat., 11, 399, 10.1107/S0909049504016760 · DOI
- Hopkins, 2017, BioXTAS RAW: Improvements to a free open-source program for small-angle X-ray scattering data reduction and analysis, J. Appl. Crystallogr., 50, 1545, 10.1107/S1600576717011438 · DOI
- Franke, 2017, ATSAS 2.8: A comprehensive data analysis suite for small-angle scattering from macromolecular solutions, J. Appl. Crystallogr., 50, 1212, 10.1107/S1600576717007786 · DOI
- Konarev, 2003, PRIMUS: A windows PC-based system for small-angle scattering data analysis, J. Appl. Crystallogr., 36, 1277, 10.1107/S0021889803012779 · DOI
- Petoukhov, 2007, ATSAS 2.1 - towards automated and web-supported small-angle scattering data analysis, J. Appl. Crystallogr., 40, S223, 10.1107/S0021889807002853 · DOI
- Svergun, 1992, Determination of the regularization parameter in indirect-transform methods using perceptual criteria, J. Appl. Crystallogr., 25, 495, 10.1107/S0021889892001663 · DOI
- Franke, 2009, DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering, J. Appl. Crystallogr., 42, 342, 10.1107/S0021889809000338 · DOI · Paper page
- Volkov, 2003, Uniqueness of ab initio shape determination in small-angle scattering, J. Appl. Crystallogr., 36, 860, 10.1107/S0021889803000268 · DOI
- Svergun, 1999, Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing, Biophys. J., 76, 2879, 10.1016/S0006-3495(99)77443-6 · DOI
- Franke, 2015, Correlation Map, a goodness-of-fit test for one-dimensional X-ray scattering spectra, Nat. Methods, 12, 419, 10.1038/nmeth.3358 · DOI
- Gunn, 2020, The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage, Proc. Natl. Acad. Sci. U. S. A., 117, 10254, 10.1073/pnas.1916555117 · DOI
- Xu, 2017, Synthetic oligosaccharides can replace animal-sourced low-molecular weight heparins, Sci. Transl. Med., 9, 10.1126/scitranslmed.aan5954 · DOI
- Miller, 2018, 3-O sulfation of heparin leads to hepatotropism and longer circulatory half-life, Thromb. Res., 167, 80, 10.1016/j.thromres.2018.05.018 · DOI
- Kikhney, 2020, SASBDB: Towards an automatically curated and validated repository for biological scattering data, Protein Sci., 29, 66, 10.1002/pro.3731 · DOI
Cited by
Sorted by citations
Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8
Sylvers-Davie, K. L., & Davies, B. S. J. (2021) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00195.2021 · Cited by 154
Metadata
- Authors
- Gunn, K. H., Gutgsell, A. R., Xu, Y., Johnson, C. V., Liu, J., & Neher, S. B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2021-01
- Volume
- 296
- Pages
- 100312
- ISSN
- 0021-9258
- PMC
- PMC7949051
- Cited by
- 12
- References
- 5
- Language
- en
- Funders
- American Heart Association (19PRE34370070, 20POST35210031)
- Office of Science
- National Institutes of Health (R01-HL094463)
- Argonne National Laboratory (DE-AC02-06CH11357)
- U.S. Department of Energy
- University of North Carolina
- National Cancer Institute
- Office of Extramural Research, National Institutes of Health (1R42GM128484, 9 P41 GM103622, P30 GM124169, P30CA016086, R01-HL12565, R01-HL144970)
- National Institute of General Medical Sciences (S10OD018483)
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review