Molecular Characterization of Loss-of-Function Mutations in PCSK9 and Identification of a Compound Heterozygote

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302

Sequence Variations in PCSK9, Low LDL, and Protection against Coronary Heart Disease

Cohen, J. C., Boerwinkle, E., Mosley, T. H., & Hobbs, H. H. (2006) · New England Journal of Medicine · doi:10.1056/nejmoa054013 · Cited by 3,181

Low LDL cholesterol in individuals of African descent resulting from frequent nonsense mutations in PCSK9

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

Nonsense-mediated mRNA decay: splicing, translation and mRNP dynamics

Maquat, L. E. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1310 · Cited by 1,214

Effect of mutations in the PCSK9 gene on the cell surface LDL receptors

Cameron, J., Holla, Ø. L., Ranheim, T., Kulseth, M. A., Berge, K. E., & Leren, T. P. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl077 · Cited by 258

Wild-type PCSK9 inhibits LDL clearance but does not affect apoB-containing lipoprotein production in mouse and cultured cells

Lalanne, F., Lambert, G., Amar, M. J. A., Chétiveaux, M., Zaïr, Y., Jarnoux, A.-L., Ouguerram, K., Friburg, J., Seidah, N. G., Brewer, H. B., et al. (2005) · Journal of Lipid Research · doi:10.1194/jlr.m400396-jlr200 · Cited by 104

Inclisiran for the Treatment of Heterozygous Familial Hypercholesterolemia

Raal, F. J., Kallend, D., Ray, K. K., Turner, T., Koenig, W., Wright, R. S., Wijngaard, P. L. J., Curcio, D., Jaros, M. J., Leiter, L. A., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa1913805 · Cited by 818

In vivo CRISPR base editing of PCSK9 durably lowers cholesterol in primates

Musunuru, K., Chadwick, A. C., Mizoguchi, T., Garcia, S. P., DeNizio, J. E., Reiss, C. W., Wang, K., Iyer, S., Dutta, C., Clendaniel, V., et al. (2021) · Nature · doi:10.1038/s41586-021-03534-y · Cited by 793

Binding of Proprotein Convertase Subtilisin/Kexin Type 9 to Epidermal Growth Factor-like Repeat A of Low Density Lipoprotein Receptor Decreases Receptor Recycling and Increases Degradation

Zhang, D.-W., Lagace, T. A., Garuti, R., Zhao, Z., McDonald, M., Horton, J. D., Cohen, J. C., & Hobbs, H. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702027200 · Cited by 788

A highly durable RNAi therapeutic inhibitor of PCSK9

Fitzgerald, K., White, S., Borodovsky, A., Bettencourt, B. R., Strahs, A., Clausen, V., Wijngaard, P., Horton, J. D., Taubel, J., Brooks, A., et al. (2017) · New England Journal of Medicine · doi:10.1056/nejmoa1609243 · Cited by 768

Secreted 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

Effect of a Monoclonal Antibody to PCSK9 on LDL Cholesterol

Stein, E. A., Mellis, S., Yancopoulos, G. D., Stahl, N., Logan, D., Smith, W. B., Lisbon, E., Gutierrez, M., Webb, C., Wu, R., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1105803 · Cited by 664

Molecular biology of PCSK9: its role in LDL metabolism

HORTON, J., COHEN, J., & HOBBS, H. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.12.008 · Cited by 621

Untitled work

Seidah (2014) · doi:10.1161/circresaha.114.301621 · Cited by 596

Permanent Alteration of PCSK9 With In Vivo CRISPR-Cas9 Genome Editing

Ding, Q., Strong, A., Patel, K. M., Ng, S.-L., Gosis, B. S., Regan, S. N., Cowan, C. A., Rader, D. J., & Musunuru, K. (2014) · Circulation Research · doi:10.1161/circresaha.115.304351 · Cited by 522

The Proprotein Convertase PCSK9 Induces the Degradation of Low Density Lipoprotein Receptor (LDLR) and Its Closest Family Members VLDLR and ApoER2

Poirier, S., Mayer, G., Benjannet, S., Bergeron, E., Marcinkiewicz, J., Nassoury, N., Mayer, H., Nimpf, J., Prat, A., & Seidah, N. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708098200 · Cited by 477

Genetic and metabolic determinants of plasma PCSK9 levels

Lakoski, S. G., Lagace, T. A., Cohen, J. C., Horton, J. D., & Hobbs, H. H. (2009) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2009-0141 · Cited by 475

Untitled work

Lambert (2012) · doi:10.1194/jlr.r026658 · Cited by 448

Cholesterol, the central lipid of mammalian cells

Maxfield, F. R., & van Meer, G. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.05.004 · Cited by 414

Structural and biophysical studies of PCSK9 and its mutants linked to familial hypercholesterolemia

Cunningham, D., Danley, D. E., Geoghegan, K. F., Griffor, M. C., Hawkins, J. L., Subashi, T. A., Varghese, A. H., Ammirati, M. J., Culp, J. S., Hoth, L. R., et al. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1235 · Cited by 409

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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

Molecular basis for LDL receptor recognition by PCSK9

Kwon, H. J., Lagace, T. A., McNutt, M. C., Horton, J. D., & Deisenhofer, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712064105 · Cited by 389

A proprotein convertase subtilisin/kexin type 9 neutralizing antibody reduces serum cholesterol in mice and nonhuman primates

Chan, 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

Progress in Understanding and Treating SCN2A-Mediated Disorders

Sanders, S. J., Campbell, A. J., Cottrell, J. R., Moller, R. S., Wagner, F. F., Auldridge, A. L., Bernier, R. A., Catterall, W. A., Chung, W. K., Empfield, J. R., et al. (2018) · Trends in Neurosciences · doi:10.1016/j.tins.2018.03.011 · Cited by 338

The activation and physiological functions of the proprotein convertases

Seidah, N. G., Mayer, G., Zaid, A., Rousselet, E., Nassoury, N., Poirier, S., Essalmani, R., & Prat, A. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.01.030 · Cited by 314

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Wadhera, R. K., Steen, D. L., Khan, I., Giugliano, R. P., & Foody, J. M. (2016) · Journal of Clinical Lipidology · doi:10.1016/j.jacl.2015.11.010 · Cited by 306

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Shapiro, M. D., Tavori, H., & Fazio, S. (2018) · Circulation Research · doi:10.1161/circresaha.118.311227 · Cited by 285

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Catalytic Activity Is Not Required for Secreted PCSK9 to Reduce Low Density Lipoprotein Receptors in HepG2 Cells

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The crystal structure of PCSK9: A regulator of plasma LDL-cholesterol

Piper, D. E., Jackson, S., Liu, Q., Romanow, W. G., Shetterly, S., Thibault, S. T., Shan, B., & Walker, N. P. C. (2007) · Structure · doi:10.1016/j.str.2007.04.004 · Cited by 251

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The Multifaceted Biology of PCSK9

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High-dose atorvastatin causes a rapid sustained increase in human serum PCSK9 and disrupts its correlation with LDL cholesterol

Welder, G., Zineh, I., Pacanowski, M. A., Troutt, J. S., Cao, G., & Konrad, R. J. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m008144 · Cited by 227

Mechanistic implications for LDL receptor degradation from the PCSK9/LDLR structure at neutral pH

Surdo, P. L., Bottomley, M. J., Calzetta, A., Settembre, E. C., Cirillo, A., Pandit, S., Ni, Y. G., Hubbard, B., Sitlani, A., & Carfí, A. (2011) · The EMBO Reports · doi:10.1038/embor.2011.205 · Cited by 226

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Shapiro, M. D., & Fazio, S. (2016) · Circulation Research · doi:10.1161/circresaha.115.306471 · Cited by 217

Gene Inactivation of Proprotein Convertase Subtilisin/Kexin Type 9 Reduces Atherosclerosis in Mice

Denis, M., Marcinkiewicz, J., Zaid, A., Gauthier, D., Poirier, S., Lazure, C., Seidah, N. G., & Prat, A. (2012) · Circulation · doi:10.1161/circulationaha.111.057406 · Cited by 212

Rare dyslipidaemias, from phenotype to genotype to management: a European Atherosclerosis Society task force consensus statement

Hegele, R. A., Borén, J., Ginsberg, H. N., Arca, M., Averna, M., Binder, C. J., Calabresi, L., Chapman, M. J., Cuchel, M., von Eckardstein, A., et al. (2020) · The Lancet Diabetes & Endocrinology · doi:10.1016/s2213-8587(19)30264-5 · Cited by 204

Safety of Very Low Low-Density Lipoprotein Cholesterol Levels With Alirocumab

Robinson, J. G., Rosenson, R. S., Farnier, M., Chaudhari, U., Sasiela, W. J., Merlet, L., Miller, K., & Kastelein, J. J. P. (2017) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2016.11.037 · Cited by 197

Secreted PCSK9 downregulates low density lipoprotein receptor through receptor-mediated endocytosis

Qian, Y.-W., Schmidt, R. J., Zhang, Y., Chu, S., Lin, A., Wang, H., Wang, X., Beyer, T. P., Bensch, W. R., Li, W., et al. (2007) · Journal of Lipid Research · doi:10.1194/jlr.m700071-jlr200 · Cited by 194

Targeting proprotein convertase subtilisin/kexin type 9 (PCSK9): From bench to bedside

Bao, X., Liang, Y., Chang, H., Cai, T., Feng, B., Gordon, K., Zhu, Y., Shi, H., He, Y., & Xie, L. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01690-3 · Cited by 187

Low density lipoprotein binds to proprotein convertase subtilisin/kexin type-9 (PCSK9) in human plasma and inhibits PCSK9-mediated low density lipoprotein receptor degradation

Kosenko, T., Golder, M., Leblond, G., Weng, W., & Lagace, T. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.421370 · Cited by 181

Low LDL cholesterol,PCSK9 and HMGCR genetic variation, and risk of Alzheimer’s disease and Parkinson’s disease: Mendelian randomisation study

Benn, M., Nordestgaard, B. G., Frikke-Schmidt, R., & Tybjærg-Hansen, A. (2017) · BMJ · doi:10.1136/bmj.j1648 · Cited by 178

A locked nucleic acid antisense oligonucleotide (LNA) silences PCSK9 and enhances LDLR expression in vitro and in vivo

Gupta, N., Fisker, N., Asselin, M.-C., Lindholm, M., Rosenbohm, C., Ørum, H., Elmén, J., Seidah, N. G., & Straarup, E. M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010682 · Cited by 174

Proprotein Convertase Subtilisin/Kexin Type 9 Inhibition: A New Therapeutic Mechanism for Reducing Cardiovascular Disease Risk

Bergeron, N., Phan, B. A. P., Ding, Y., Fong, A., & Krauss, R. M. (2015) · Circulation · doi:10.1161/circulationaha.115.016080 · Cited by 171

Targeting PCSK9 to tackle cardiovascular disease

Hummelgaard, S., Vilstrup, J. P., Gustafsen, C., Glerup, S., & Weyer, K. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108480 · Cited by 150

In vivo evidence that furin from hepatocytes inactivates PCSK9

Essalmani, R., Susan-Resiga, D., Chamberland, A., Abifadel, M., Creemers, J. W., Boileau, C., Seidah, N. G., & Prat, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.192104 · Cited by 144

Inhibiting PCSK9 — biology beyond LDL control

Stoekenbroek, R. M., Lambert, G., Cariou, B., & Hovingh, G. K. (2019) · Nature Reviews Endocrinology · doi:10.1038/s41574-018-0110-5 · Cited by 141

Regulation of PCSK9 by nutraceuticals

Momtazi, A. A., Banach, M., Pirro, M., Katsiki, N., & Sahebkar, A. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.03.023 · Cited by 131

Targeting PCSK9 for hypercholesterolemia

Norata, G. D., Tibolla, G., & Catapano, A. L. (2014) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011613-140025 · Cited by 127

Regulation of PCSK9 Expression and Function: Mechanisms and Therapeutic Implications

Xia, X.-D., Peng, Z.-S., Gu, H.-M., Wang, M., Wang, G.-Q., & Zhang, D.-W. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.764038 · Cited by 125

Inclisiran—New hope in the management of lipid disorders?

Dyrbuś, K., Gąsior, M., Penson, P., Ray, K. K., & Banach, M. (2020) · Journal of Clinical Lipidology · doi:10.1016/j.jacl.2019.11.001 · Cited by 120

Characterization of Three Kindreds With Familial Combined Hypolipidemia Caused by Loss-of-Function Mutations of ANGPTL3

Pisciotta, L., Favari, E., Magnolo, L., Simonelli, S., Adorni, M. P., Sallo, R., Fancello, T., Zavaroni, I., Ardigò, D., Bernini, F., et al. (2012) · Circulation: Cardiovascular Genetics · doi:10.1161/circgenetics.111.960674 · Cited by 120

Annexin A2 is a natural extrahepatic inhibitor of the PCSK9-induced LDL receptor degradation

Seidah, N. G., Poirier, S., Denis, M., Parker, R., Miao, B., Mapelli, C., Prat, A., Wassef, H., Davignon, J., Hajjar, K. A., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041865 · Cited by 117

The proprotein convertases in hypercholesterolemia and cardiovascular diseases: Emphasis on proprotein convertase subtilisin/kexin 9

Seidah, N. G., Abifadel, M., Prost, S., Boileau, C., & Prat, A. (2017) · Pharmacological Reviews · doi:10.1124/pr.116.012989 · Cited by 116

PCSK9 as a therapeutic target of dyslipidemia

Seidah, N. G. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220802600715 · Cited by 110

PCSK9 reduces the protein levels of the LDL receptor in mouse brain during development and after ischemic stroke

Rousselet, E., Marcinkiewicz, J., Kriz, J., Zhou, A., Hatten, M. E., Prat, A., & Seidah, N. G. (2011) · Journal of Lipid Research · doi:10.1194/jlr.m014118 · Cited by 107

PCSK9 (Proprotein convertase subtilisin/kexin type 9) inhibitors: past, present, and the future

Shimada, Y. J., & Cannon, C. P. (2015) · European Heart Journal · doi:10.1093/eurheartj/ehv174 · Cited by 98

Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) in the Brain and Relevance for Neuropsychiatric Disorders

O’Connell, E. M., & Lohoff, F. W. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00609 · Cited by 93

Reduction of low-density lipoprotein cholesterol by monoclonal antibody inhibition of PCSK9

Stein, E. A., & Raal, F. (2014) · Annual Review of Medicine · doi:10.1146/annurev-med-022613-090402 · Cited by 89

On the function and homeostasis of PCSK9: Reciprocal interaction with LDLR and additional lipid effects

Tavori, H., Rashid, S., & Fazio, S. (2015) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2014.12.017 · Cited by 86

PCSK9 inhibition in the management of familial hypercholesterolemia

Ogura, M. (2018) · Journal of Cardiology · doi:10.1016/j.jjcc.2017.07.002 · Cited by 84

Small molecules as inhibitors of PCSK9: Current status and future challenges

Xu, S., Luo, S., Zhu, Z., & Xu, J. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.11.011 · Cited by 85

Identification and characterization of two non-secreted PCSK9 mutants associated with familial hypercholesterolemia in cohorts from New Zealand and South Africa

Homer, V. M., Marais, A. D., Charlton, F., Laurie, A. D., Hurndell, N., Scott, R., Mangili, F., Sullivan, D. R., Barter, P. J., Rye, K.-A., et al. (2008) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2007.07.022 · Cited by 84

Plasma PCSK9 levels correlate with cholesterol in men but not in women.

Mayne, J., Raymond, A., Chaplin, A., Cousins, M., Kaefer, N., Gyamera-Acheampong, C., Seidah, N. G., Mbikay, M., Chrétien, M., & Ooi, T. C. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.07.029 · Cited by 81

Proprotein convertase subtilisin/kexin type 9 (PCSK9) gene is a risk factor of large-vessel atherosclerosis stroke

Abboud, S., Karhunen, P. J., Lütjohann, D., Goebeler, S., Luoto, T., Friedrichs, S., Lehtimaki, T., Pandolfo, M., & Laaksonen, R. (2007) · PLoS ONE · doi:10.1371/journal.pone.0001043 · Cited by 77

PCSK9: Regulation and Target for Drug Development for Dyslipidemia

Burke, A. C., Dron, J. S., Hegele, R. A., & Huff, M. W. (2017) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104944 · Cited by 74

Complexity of mechanisms among human proprotein convertase subtilisin-kexin type 9 variants

Dron, J. S., & Hegele, R. A. (2017) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000386 · Cited by 72

PCSK9: A Multi-Faceted Protein That Is Involved in Cardiovascular Biology

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PCSK9 Inhibition With Monoclonal Antibodies: Modern Management of Hypercholesterolemia

Ito, M. K., & Santos, R. D. (2017) · The Journal of Clinical Pharmacology · doi:10.1002/jcph.766 · Cited by 59

PCSK9 is present in human cerebrospinal fluid and is maintained at remarkably constant concentrations throughout the course of the day

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PCSK9 deficiency unmasks a sex- and tissue-specific subcellular distribution of the LDL and VLDL receptors in mice

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PCSK9 acts as a chaperone for the LDL receptor in the endoplasmic reticulum

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Genome‐wide expression analysis of cells expressing gain of function mutant D374Y‐PCSK9

Ranheim, T., Mattingsdal, M., Lindvall, J. M., Holla, Ø. L., Berge, K. E., Kulseth, M. A., & Leren, T. P. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21519 · Cited by 41

Threshold Effects of Circulating Angiopoietin-Like 3 Levels on Plasma Lipoproteins

Fazio, S., Minnier, J., Shapiro, M. D., Tsimikas, S., Tarugi, P., Averna, M. R., Arca, M., & Tavori, H. (2017) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2016-4043 · Cited by 40

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Disrupted recycling of the low density lipoprotein receptor by PCSK9 is not mediated by residues of the cytoplasmic domain

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Targeting PCSK9 With Antibodies and Gene Silencing to Reduce LDL Cholesterol

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Stepwise processing analyses of the single-turnover PCSK9 protease reveal its substrate sequence specificity and link clinical genotype to lipid phenotype

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PCSK9 deficiency alters brain lipid composition without affecting brain development and function

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