The DOI matches its Crossref record; 54 of the 56 references it cites were found in a registry or an index.
PCSK9 deficiency results in a specific shedding of excess LDLR in female mice only: Role of hepatic cholesterol
Open accessAbstract
PCSK9 promotes the lysosomal degradation of cell surface LDL receptor (LDLR). We analyzed how excess LDLR generated by PCSK9 deficiency is differently handled in male and female mice to possibly unveil the mechanism leading to the lower efficacy of PCSK9 mAb on LDL-cholesterol levels in women. Analysis of intact or ovariectomized PCSK9 knockout (KO) mice supplemented with placebo or 17β-estradiol (E2) demonstrated that female, but not male mice massively shed the soluble ectodomain of the LDLR in the plasma. Liver-specific PCSK9 KO or alirocumab-treated WT mice exhibit the same pattern. This shedding is distinct from the basal one and is inhibited by ZLDI-8, a metalloprotease inhibitor pointing at ADAM10/ADAM17. In PCSK9 KO female mice, ZLDI-8 raises by 80 % the LDLR liver content in a few hours. This specific shedding is likely cholesterol-dependent: it is prevented in PCSK9 KO male mice that exhibit low intra-hepatic cholesterol levels without activating SREBP-2, and enhanced by mevalonate or high cholesterol feeding, or by E2 known to stimulate cholesterol synthesis via the estrogen receptor-α. Liver transcriptomics demonstrates that critically low liver cholesterol in ovariectomized female or knockout male mice also hampers the cholesterol-dependent G2/M transition of the cell cycle. Finally, higher levels of shed LDLR were measured in the plasma of women treated with PCSK9 mAb. PCSK9 knockout female mice hormonally sustain cholesterol synthesis and shed excess LDLR, seemingly like women. In contrast, male mice rely on high surface LDLR to replenish their stocks, despite 80 % lower circulating LDL.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The text we found for this paper looks like another document, so the self-check wasn’t run.
Citations
Cites
Mutations in PCSK9 cause autosomal dominant hypercholesterolemia
Abifadel, M., Varret, M., Rabès, J.-P., Allard, D., Ouguerram, K., Devillers, M., Cruaud, C., Benjannet, S., Wickham, L., Erlich, D., et al. (2003) · Nature Genetics · doi:10.1038/ng1161 · Cited by 2,985
Self-citationEfficacy and Safety of Alirocumab in Reducing Lipids and Cardiovascular Events
Robinson, J. G., Farnier, M., Krempf, M., Bergeron, J., Luc, G., Averna, M., Stroes, E. S., Langslet, G., Raal, F. J., El Shahawy, M., et al. (2015) · New England Journal of Medicine · doi:10.1056/nejmoa1501031 · Cited by 2,296
Cohen, J., Pertsemlidis, A., Kotowski, I. K., Graham, R., Garcia, C. K., & Hobbs, H. H. (2005) · Nature Genetics · doi:10.1038/ng1509 · Cited by 1,381
Seidah, N. G., Benjannet, S., Wickham, L., Marcinkiewicz, J., Jasmin, S. B., Stifani, S., Basak, A., Prat, A., & Chrétien, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0335507100 · Cited by 1,191
Self-citationFoxM1 is required for execution of the mitotic programme and chromosome stability
Laoukili, J., Kooistra, M. R. H., Brás, A., Kauw, J. J. W., Kerkhoven, R. M., Morrison, A. J., Clevers, H. C., & Medema, R. H. (2005) · Nature Cell Biology · doi:10.1038/ncb1217 · Cited by 808
The biology and therapeutic targeting of the proprotein convertases
Seidah, N. G., & Prat, A. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3699 · Cited by 759
Self-citationSecreted PCSK9 decreases the number of LDL receptors in hepatocytes and inlivers of parabiotic mice
Lagace, T. A., Curtis, D. E., Garuti, R., McNutt, M. C., Park, S. W., Prather, H. B., Anderson, N. N., Ho, Y. K., Hammer, R. E., & Horton, J. D. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29383 · Cited by 681
Decreased plasma cholesterol and hypersensitivity to statins in mice lacking Pcsk9
Rashid, S., Curtis, D. E., Garuti, R., Anderson, N. N., Bashmakov, Y., Ho, Y. K., Hammer, R. E., Moon, Y.-A., & Horton, J. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501652102 · Cited by 679
Maxwell, K. N., & Breslow, J. L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402133101 · Cited by 613
Retrospective on Cholesterol Homeostasis: The Central Role of Scap
Brown, M. S., Radhakrishnan, A., & Goldstein, J. L. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-011852 · Cited by 477
Maxwell, K. N., Fisher, E. A., & Breslow, J. L. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409736102 · Cited by 415
Zaid, A., Roubtsova, A., Essalmani, R., Marcinkiewicz, J., Chamberland, A., Hamelin, J., Tremblay, M., Jacques, H., Jin, W., Davignon, J., et al. (2008) · Hepatology · doi:10.1002/hep.22354 · Cited by 404
Self-citationChan, J. C. Y., Piper, D. E., Cao, Q., Liu, D., King, C., Wang, W., Tang, J., Liu, Q., Higbee, J., Xia, Z., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903849106 · Cited by 371
Intracellular maturation and localization of the tumour necrosis factor α convertase (TACE)
Schlöndorff, J. S., Becherer, J. D., & Blobel, C. (2000) · Biochemical Journal · doi:10.1042/bj3470131 · Cited by 357
The MuvB complex sequentially recruits B-Myb and FoxM1 to promote mitotic gene expressionPreprint
Sadasivam, S., Duan, S., & DeCaprio, J. A. (2012) · Genes & Development · doi:10.1101/gad.181933.111 · Cited by 323
NPC1 regulates ER contacts with endocytic organelles to mediate cholesterol egress
Höglinger, D., Burgoyne, T., Sanchez-Heras, E., Hartwig, P., Colaco, A., Newton, J., Futter, C. E., Spiegel, S., Platt, F. M., & Eden, E. R. (2019) · Nature Communications · doi:10.1038/s41467-019-12152-2 · Cited by 299
Sandhu, J., Li, S., Fairall, L., Pfisterer, S. G., Gurnett, J. E., Xiao, X., Weston, T. A., Vashi, D., Ferrari, A., Orozco, J. L., et al. (2018) · Cell · doi:10.1016/j.cell.2018.08.033 · Cited by 287
McNutt, M. C., Lagace, T. A., & Horton, J. D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700095200 · Cited by 251
The Multifaceted Biology of PCSK9
Seidah, N. G., & Prat, A. (2022) · Endocrine Reviews · doi:10.1210/endrev/bnab035 · Cited by 232
Self-citationGrant, G. D., Brooks, L., Zhang, X., Mahoney, J. M., Martyanov, V., Wood, T. A., Sherlock, G., Cheng, C., & Whitfield, M. L. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-05-0264 · Cited by 179
Kuhn, P.-H., Colombo, A. V., Schusser, B., Dreymueller, D., Wetzel, S., Schepers, U., Herber, J., Ludwig, A., Kremmer, E., Montag, D., et al. (2016) · eLife · doi:10.7554/elife.12748 · Cited by 163
Phosphatidylserine exposure is required for ADAM17 sheddase function
Sommer, A., Kordowski, F., Büch, J., Maretzky, T., Evers, A., Andrä, J., Düsterhöft, S., Michalek, M., Lorenzen, I., Somasundaram, P., et al. (2016) · Nature Communications · doi:10.1038/ncomms11523 · Cited by 163
Infante, R. E., & Radhakrishnan, A. (2017) · eLife · doi:10.7554/elife.25466 · Cited by 163
The shedding activity of ADAM17 is sequestered in lipid rafts
Tellier, E., Canault, M., Rebsomen, L., Bonardo, B., Juhan-Vague, I., Nalbone, G., & Peiretti, F. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.08.027 · Cited by 150
Roles of G protein-coupled estrogen receptor GPER in metabolic regulation
Sharma, G., Mauvais‐Jarvis, F., & Prossnitz, E. R. (2017) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2017.02.012 · Cited by 132
Trinh, M. N., Brown, M. S., Goldstein, J. L., Han, J., Vale, G., McDonald, J. G., Seemann, J., Mendell, J. T., & Lu, F. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2010682117 · Cited by 129
Sever, P. S., Gouni‐Berthold, I., KEECH, A. C., Giugliano, R. P., Pedersen, T. R., Im, K., Wang, H., Knüsel, B., Sabatine, M. S., & O’Donoghue, M. L. (2020) · European Journal of Preventive Cardiology · doi:10.1177/2047487320902750 · Cited by 106
Zhang, Y., Li, D., Jiang, Q., Cao, S., Sun, H., Chai, Y., Li, X., Ren, T., Yang, R., Feng, F., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0804-6 · Cited by 103
A proteomic approach for the identification of cell-surface proteins shed by metalloproteases
Guo, L., Eisenman, J. R., Mahimkar, R. M., Peschon, J. J., Paxton, R. J., Black, R. A., & Johnson, R. S. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m100020-mcp200 · Cited by 82
ADAM10 sheddase activation is controlled by cell membrane asymmetry
Bleibaum, F., Sommer, A., Veit, M., Rabe, B., Andrä, J., Kunzelmann, K., Nehls, C., Correa, W., Gutsmann, T., Grötzinger, J., et al. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz008 · Cited by 79
Cholesterol starvation decreases P34 cdc2 kinase activity and arrests the cell cycle at G2
Martínez‐Botas, J., Suárez, Y., Ferruelo, A. J., Gómez‐Coronado, D., & Lasunció, M. A. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.11.1359 · Cited by 72
Lu, H., Zu, Y., Jiang, X., Sun, X., Liu, T., Li, R., Wu, Q., Zhang, Y., & Zhao, Q.-C. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104406 · Cited by 69
Sorrentino, V., Nelson, J. K., Maspero, E., Marques, A. R. A., Scheer, L., Polo, S., & Zelcer, N. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m037713 · Cited by 68
Wang, H. H., Afdhal, N. H., & Wang, D. Q. ‐. (2005) · Journal of Lipid Research · doi:10.1194/jlr.m500454-jlr200 · Cited by 67
Aster Proteins Regulate the Accessible Cholesterol Pool in the Plasma Membrane
Ferrari, A., He, C., Kennelly, J. P., Sandhu, J., Xiao, X., Chi, X., Jiang, H., Young, S. G., & Tontonoz, P. (2020) · Molecular and Cellular Biology · doi:10.1128/mcb.00255-20 · Cited by 66
Recovery from a DNA‐damage‐induced G2 arrest requires Cdk‐dependent activation of FoxM1
Álvarez‐Fernández, M., Halim, V. A., Krenning, L., Aprelia, M., Mohammed, S., Heck, A. J. R., & Medema, R. H. (2010) · EMBO Reports · doi:10.1038/embor.2010.46 · Cited by 64
Alabi, A., Xia, X.-D., Gu, H.-M., Wang, F., Deng, S.-J., Yang, N., Adijiang, A., Douglas, D. N., Kneteman, N. M., Xue, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22167-3 · Cited by 63
Contribution of ADAM17 and related ADAMs in cardiovascular diseases
Kawai, T., Elliott, K. J., Scalia, R. G., & Eguchi, S. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03779-w · Cited by 62
Moreno‐Càceres, J., Caja, L., Mainez, J., Mayoral, R., Martín‐Sanz, P., Moreno-Vicente, R., del Pozo, M. Á., Dooley, S., Egea, G., & Fabregat, I. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.294 · Cited by 60
Roubtsova, A., Chamberland, A., Marcinkiewicz, J., Essalmani, R., Fazel, A., Bergeron, J. J., Seidah, N. G., & Prat, A. (2015) · Journal of Lipid Research · doi:10.1194/jlr.m061952 · Cited by 55
Self-citationLi, D., Zhao, C., Ding, H., Wu, Q., Ren, T., Wang, J., Chen, C., & Zhao, Q. (2018) · Cell Proliferation · doi:10.1111/cpr.12480 · Cited by 55
The plasma membrane: Penultimate regulator of ADAM sheddase function
Reiß, K., & Bhakdi, S. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.06.006 · Cited by 51
Differential effects of ergosterol and cholesterol on Cdk1 activation and SRE‐driven transcription
Suárez, Y., Fernández, C., Ledo, B., Ferruelo, A., Martín, M., Vega, M. A., Gómez‐Coronado, D., & Lasunción, M. A. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2002.02822.x · Cited by 45
GRAMD1-mediated accessible cholesterol sensing and transport
Naito, T., & Saheki, Y. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2021.158957 · Cited by 45
Peyot, M., Roubtsova, A., Lussier, R., Chamberland, A., Essalmani, R., Madiraju, S. R. M., Seidah, N. G., Prentki, M., & Prat, A. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2021.158968 · Cited by 39
Self-citationSusan-Resiga, D., Girard, E., Kiss, R. S., Essalmani, R., Hamelin, J., Asselin, M.-C., Awan, Z., Butkinaree, C., Fleury, A., Soldera, A., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.769430 · Cited by 35
Self-citationHepatic Cholesterol Homeostasis
Sniderman, A. D., Qi, Y., Ma, C.-I. J., Wang, R. H. L., Naples, M., Baker, C., Zhang, J., Adeli, K., & Kiss, R. S. (2013) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.113.301517 · Cited by 34
Cordero, A., Olmo, M. R. F., Quiroga, G. A. C., Romero‐Menor, C., Fácila, L., Seijas‐Amigo, J., Fornovi, A., Murillo, J. R., Rodríguez‐Mañero, M., Mora, M. C. B., et al. (2022) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000001205 · Cited by 33
Estradiol accelerates liver regeneration through estrogen receptor α
Tsugawa, Y., Natori, M., Handa, H., & Imai, T. (2019) · Clinical and Experimental Gastroenterology · doi:10.2147/ceg.s214196 · Cited by 31
Mayne, J., Ooi, T. C., Tepliakova, L., Seebun, D., Walker, K., Mohottalage, D., Ning, Z., Abujrad, H., Mbikay, M., Wassef, H., et al. (2018) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2018-00777 · Cited by 24
Alabi, R. O., Lora, J., Celen, A. B., Maretzky, T., & Blobel, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041846 · Cited by 21
Imai, T., Umeda, M., & Hiramoto, M. (2015) · Clinical and Experimental Gastroenterology · doi:10.2147/ceg.s80212 · Cited by 19
ASCH, B. V., & da Costa, L. F. T. (2021) · Genetica · doi:10.1007/s10709-021-00113-x · Cited by 9
ADAM17 mediates ectodomain shedding of the soluble VLDL receptor fragment in the retinal epithelium
Ma, X., Takahashi, Y., Wu, W., Liang, W., Chen, J., Chakraborty, D., Li, Y., Du, Y., Benyajati, S., & Ma, J.-X. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101185 · Cited by 9
Flagged first, then by citations
2 of the 56 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
PCSK9 in metabolism and diseases
Ajoolabady, A., Pratico, D., Mazidi, M., Davies, I. G., Lip, G. Y. H., Seidah, N., Libby, P., Kroemer, G., & Ren, J. (2025) · Metabolism · doi:10.1016/j.metabol.2024.156064 · Cited by 49
Self-citationLDL lowering effect of PCSK9 inhibition is reduced in women
Myasoedova, V. A., Rimbert, A., Camera, M., May, C. L., Capoulade, R., Cariou, B., & Poggio, P. (2023) · European Heart Journal - Cardiovascular Pharmacotherapy · doi:10.1093/ehjcvp/pvad009 · Cited by 28
Self-citationSachan, V., Dévéhat, M. L., Roubtsova, A., Essalmani, R., Laurendeau, J.-F., Garçon, D., Susan‐Resiga, D., Duval, S., Mikaeeli, S., Hamelin, J., et al. (2023) · Metabolism · doi:10.1016/j.metabol.2023.155736 · Cited by 24
Self-citationFruchart‐Gaillard, C., Ouadda, A. B. D., Ciccone, L., Girard, E., Mikaeeli, S., Evagelidis, A., Dévéhat, M. L., Susan‐Resiga, D., Lajeunesse, E. C., Nozach, H., et al. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101662 · Cited by 22
Self-citationEssalmani, R., Andréo, U., Evagelidis, A., Dévéhat, M. L., Ramos, O. H. P., Fruchart‐Gaillard, C., Susan‐Resiga, D., Cohen, É. A., & Seidah, N. G. (2023) · Viruses · doi:10.3390/v15020360 · Cited by 17
Self-citationGiglio, R. V., Muzurović, E. M., Patti, A. M., Toth, P. P., Agarwal, M. A., Almahmeed, W. A., Klisic, A. N., Ciaccio, M., & Rizzo, M. (2023) · Journal of Cardiovascular Pharmacology and Therapeutics · doi:10.1177/10742484231186855 · Cited by 11
PCSK9 deficiency promotes the development of peripheral neuropathy
Jaafar, A. K., Paulo-Ramos, A., Rastoldo, G., Veeren, B., Planesse, C., Bringart, M., Rondeau, P., Chemello, K., Meilhac, O., Lambert, G. C., et al. (2025) · JCI Insight · doi:10.1172/jci.insight.183786 · Cited by 11
Tissue-specific mechanism of estrogen in osteoporosis and vascular calcification
Wu, W., Qiao, A., & Du, T. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.177783 · Cited by 9
The Biology and Clinical Implications of PCSK7
Sachan, V., Susan‐Resiga, D., Lam, K., & Seidah, N. G. (2024) · Endocrine Reviews · doi:10.1210/endrev/bnae031 · Cited by 9
Self-citationSurface LDLR is a major receptor for lipoprotein(a) clearance in male mice lacking PCSK9
Roubtsova, A., Scipione, C. A., Garçon, D., Boffa, M. B., Seidah, N. G., Koschinsky, M. L., & Prat, A. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2023.159288 · Cited by 5
Self-citationPark, S. K., Hwang, J., Choi, H., & Lee, J. (2025) · Chinese Medicine · doi:10.1186/s13020-025-01178-y · Cited by 8
Unraveling Estrogen and PCSK9’s Roles in Lipid Metabolism Disorders among Ovariectomized Mice
Yang, J., Xu, M., Wang, Z., He, M., Zhang, G., Jin, L., Zhao, R., Pan, Y., Tong, J., & Nie, L. (2024) · Reproductive Sciences · doi:10.1007/s43032-024-01614-8 · Cited by 8
Nowacka, A., Śniegocki, M., & Ziółkowska, E. (2025) · Cells · doi:10.3390/cells14181479 · Cited by 5
Krauss, R. M., Fisher, L. M., King, S. M., & Gardner, C. D. (2024) · Journal of Lipid Research · doi:10.1016/j.jlr.2024.100503 · Cited by 5
Papanikolaou, A., Anastasiou, G., Barkas, F., Tellis, C. C., Zikopoulos, K., & Liberopoulos, E. N. (2024) · Journal of Cardiovascular Development and Disease · doi:10.3390/jcdd11010025 · Cited by 1
Zhao, J., Tong, X., Peng, J., Lyu, C., & Lu, S. (2024) · Reviews in Cardiovascular Medicine · doi:10.31083/j.rcm2503094 · Cited by 1
Maternal Hypercholesterolemia is a Significant Risk Factor for Atherogenesis – A Systematic Review
Poznyak, A. V., Khotina, V. A., Sukhorukov, V. N., Sadykhov, N. K., Postnov, A. Y., & Orekhov, A. A. N. (2024) · Journal of Angiotherapy · doi:10.25163/angiotherapy.819390
Sotin, T. (2024) · theses.fr (ABES) · doi:10.70675/31b0eb9azda79z4da2za798zb99c1e201121
Self-citationShehab, H. F., Rajan, R., Al‐Jarallah, M., Dashti, R., Al-Sarraf, A. J., Alsaber, A., Tse, G., AlObaid, L., & Lansberg, P. J. (2025) · Annals of Clinical Cardiology · doi:10.4103/accj.accj_28_24
PCSK9 Inhibition and Coronary Artery Disease in Mice
Xiong, T. (2023) · MacSphere (McMaster University) · doi:10.71548/14044
Système nerveux périphérique et neuropathie : le rôle de PCSK9
Paulo-Ramos, A. (2024) · theses.fr (ABES) · doi:10.70675/3e184b77zbe61z498fza406zcc1a7a8b5e9f
Lafortune, C., Haddad, Y., Marcinkiewicz, M. M., Chrétien, M., Turcotte, S., & Mbikay, M. (2026) · Lipids in Health and Disease · doi:10.1186/s12944-026-02981-8
Metadata
- Authors
- Roubtsova, A., Garçon, D., Lacoste, S., Chamberland, A., Marcinkiewicz, J., Métivier, R., Sotin, T., Paquette, M., Bernard, S., Cariou, B., Le May, C., Koschinsky, M. L., Seidah, N. G., & Prat, A.
- Affiliations
- Montreal Clinical Research Institute (CA)
- Centre National de la Recherche Scientifique (FR)
- Western University (CA)
- Université du Québec à Montréal (CA)
- Corresponding author
- Prat, Annik
- ORCID
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
- Publisher
- Elsevier BV
- Published
- 2022-12
- Volume
- 1867
- Issue
- 12
- Pages
- 159217
- ISSN
- 1388-1981 (ISSN-L)
- OpenAlex
- W4292261879
- Cited by
- 22
- References
- 56
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 9 · 2023: 6 · 2022: 1
- FWCI
- 3.69
- Type
- journal article
- Language
- en
- Open access
- green
- hal.science
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- HAL (submittedVersion, cc-by-nc)
- Funders
- Canadian Institutes of Health Research (145572, 148363, # 950-231335)
- Topics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
- Keywords
- sex differences, liver cholesterol, estradiol, ovariectomy, ADAM10, ADAM17, SREBP2, mevalonate, estrogen receptor alpha, cholesterol biosynthesis, G2/M transition, PCSK9 monoclonal antibodies, alirocumab, PCSK9 knockout mice, LDL cholesterol
- MeSH terms
- Proprotein Convertase 9, Animals, Cholesterol, Estradiol, Female, Liver, Mevalonic Acid, Receptors, Cell Surface, Receptors, Estrogen, Receptors, LDL, Mice, Knockout, Metalloproteases, Mice, Sterol Regulatory Element Binding Protein 1
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.
A second model labelled each claim on 2026-11-10 (model jev-1.13-20260917, definition revision gold-guideline-v0.2).
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
