Associated Papers
First LDLRAP1 and Recurrent LDLR Mutations in Tunisian Families With Familial Hypercholesterolemia.
Ncir WB et al.
Journal of Cellular and Molecular Medicine, 2026
Targeting PCSK9 to tackle cardiovascular disease.
Hummelgaard S et al.
Pharmacology & Therapeutics, 2023
Protein structural insights into a rare PCSK9 gain-of-function variant (R496W) causing familial hypercholesterolemia in a Saudi family: whole exome sequencing and computational analysis.
Shaik NA et al.
Frontiers in Physiology, 2023
Pathogenic gain-of-function mutations in the prodomain and C-terminal domain of PCSK9 inhibit LDL binding.
Sarkar SK et al.
Frontiers in Physiology, 2022
Physiology and role of PCSK9 in vascular disease: Potential impact of localized PCSK9 in vascular wall.
Guo Y et al.
Journal of Cellular Physiology, 2021
A transient amphipathic helix in the prodomain of PCSK9 facilitates binding to low-density lipoprotein particles.
Sarkar SK et al.
The Journal of Biological Chemistry, 2020
Emerging role of proprotein convertase subtilisin/kexin type-9 (PCSK-9) in inflammation and diseases.
Brown M et al.
Toxicology and Applied Pharmacology, 2019
Stepwise processing analyses of the single-turnover PCSK9 protease reveal its substrate sequence specificity and link clinical genotype to lipid phenotype.
Chorba JS et al.
The Journal of Biological Chemistry, 2018
Complexity of mechanisms among human proprotein convertase subtilisin-kexin type 9 variants.
Dron JS et al.
Current Opinion in Lipidology, 2017
Characterisation of de novo mutations in the C-terminal domain of proprotein convertase subtilisin/kexin type 9.
Geschwindner S et al.
Protein Engineering, Design & Selection : Peds, 2015
Proprotein convertase subtilisin/kexin type 9 (PCSK9): lessons learned from patients with hypercholesterolemia.
Awan Z et al.
Clinical Chemistry, 2014
An antibody against the C-terminal domain of PCSK9 lowers LDL cholesterol levels in vivo.
Schiele F et al.
Journal of Molecular Biology, 2014
The M2 module of the Cys-His-rich domain (CHRD) of PCSK9 protein is needed for the extracellular low-density lipoprotein receptor (LDLR) degradation pathway.
Saavedra YG et al.
The Journal of Biological Chemistry, 2012
Effect of a splice site mutation in LDLR gene and two variations in PCSK9 gene in Tunisian families with familial hypercholesterolaemia.
Jelassi A et al.
Annals of Clinical Biochemistry, 2011
Mutations and polymorphisms in the proprotein convertase subtilisin kexin 9 (PCSK9) gene in cholesterol metabolism and disease.
Abifadel M et al.
Human Mutation, 2009
PCSK9 as a therapeutic target of dyslipidemia.
Seidah NG
Expert Opinion on Therapeutic Targets, 2009
Molecular population genetics of PCSK9: a signature of recent positive selection.
Ding K et al.
Pharmacogenetics and Genomics, 2008
Evidence for positive selection in the C-terminal domain of the cholesterol metabolism gene PCSK9 based on phylogenetic analysis in 14 primate species.
Ding K et al.
Plos One, 2007
[After the LDL receptor and apolipoprotein B, autosomal dominant hypercholesterolemia reveals its third protagonist: PCSK9].
Abifadel M et al.
Annales D'endocrinologie, 2007
A spectrum of PCSK9 alleles contributes to plasma levels of low-density lipoprotein cholesterol.
Kotowski IK et al.
American Journal of Human Genetics, 2006
Familial hypercholesterolemia mutations in the Middle Eastern and North African region: a need for a national registry.
Bamimore MA et al.
Journal of Clinical Lipidology, 0