Associated Papers
Targeting proprotein convertase subtilisin/kexin type 9 (PCSK9): from bench to bedside.
Bao X et al.
Signal Transduction and Targeted Therapy, 2024
PCSK9: A Multi-Faceted Protein That Is Involved in Cardiovascular Biology.
Sundararaman SS et al.
Biomedicines, 2021
PCSK9 Biology and Its Role in Atherothrombosis.
Barale C et al.
International Journal of Molecular Sciences, 2021
Construction of point mutation rabbits using CRISPR/Cas9.
Yan K et al.
Zhejiang Da Xue Xue Bao. Yi Xue Ban = Journal of Zhejiang University. Medical Sciences, 2021
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
The loss-of-function PCSK9Q152H variant increases ER chaperones GRP78 and GRP94 and protects against liver injury.
Lebeau PF et al.
The Journal of Clinical Investigation, 2021
The PCSK9 discovery, an inactive protease with varied functions in hypercholesterolemia, viral infections, and cancer.
Seidah NG
Journal of Lipid Research, 2021
A High-Throughput Luciferase Assay to Evaluate Proteolysis of the Single-Turnover Protease PCSK9.
Chorba JS et al.
Journal of Visualized Experiments : Jove, 2018
Loss-of-function PCSK9 mutants evade the unfolded protein response sensor GRP78 and fail to induce endoplasmic reticulum stress when retained.
Lebeau P et al.
The Journal of Biological Chemistry, 2018
PCSK9: From Basic Science Discoveries to Clinical Trials.
Shapiro MD et al.
Circulation Research, 2018
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
Studies of the autoinhibitory segment comprising residues 31-60 of the prodomain of PCSK9: Possible implications for the mechanism underlying gain-of-function mutations.
Wierød L et al.
Molecular Genetics and Metabolism Reports, 2016
Point mutations at the catalytic site of PCSK9 inhibit folding, autoprocessing, and interaction with the LDL receptor.
Garvie CW et al.
Protein Science : a Publication of the Protein Society, 2016
The proprotein convertase subtilisin/kexin type 9 (PCSK9) active site and cleavage sequence differentially regulate protein secretion from proteolysis.
Chorba JS et al.
The Journal of Biological Chemistry, 2014
PCSK9 acts as a chaperone for the LDL receptor in the endoplasmic reticulum.
Strøm TB et al.
The Biochemical Journal, 2014
Regulation of epithelial sodium channel trafficking by proprotein convertase subtilisin/kexin type 9 (PCSK9).
Sharotri V et al.
The Journal of Biological Chemistry, 2012
Proprotein convertase subtilisin kexin type 9 (PCSK9) secreted by cultured smooth muscle cells reduces macrophages LDLR levels.
Ferri N et al.
Atherosclerosis, 2012
Proprotein convertase subtilisin/kexin type 9: from the discovery to the development of new therapies for cardiovascular diseases.
Ferri N
Scientifica, 2012
Role of the C-terminal domain of PCSK9 in degradation of the LDL receptors.
Holla ØL et al.
Journal of Lipid Research, 2011
Removal of acidic residues of the prodomain of PCSK9 increases its activity towards the LDL receptor.
Holla ØL et al.
Biochemical and Biophysical Research Communications, 2011
PCSK9 dominant negative mutant results in increased LDL catabolic rate and familial hypobetalipoproteinemia.
Cariou B et al.
Arteriosclerosis, Thrombosis, and Vascular Biology, 2009
Cellular and secreted pro-protein convertase subtilisin/kexin type 9 catalytic activity in hepatocytes.
Kourimate S et al.
Atherosclerosis, 2009
Mutation S462P in the PCSK9 gene reduces secretion of mutant PCSK9 without affecting the autocatalytic cleavage.
Cameron J et al.
Atherosclerosis, 2009
Structural and biochemical characterization of the wild type PCSK9-EGF(AB) complex and natural familial hypercholesterolemia mutants.
Bottomley MJ et al.
The Journal of Biological Chemistry, 2009
Investigations on the evolutionary conservation of PCSK9 reveal a functionally important protrusion.
Cameron J et al.
The Febs Journal, 2008
Secreted proprotein convertase subtilisin/kexin type 9 reduces both hepatic and extrahepatic low-density lipoprotein receptors in vivo.
Schmidt RJ et al.
Biochemical and Biophysical Research Communications, 2008
Functional analysis of sites within PCSK9 responsible for hypercholesterolemia.
Pandit S et al.
Journal of Lipid Research, 2008
Plasma PCSK9 preferentially reduces liver LDL receptors in mice.
Grefhorst A et al.
Journal of Lipid Research, 2008
Characterization of novel mutations in the catalytic domain of the PCSK9 gene.
Cameron J et al.
Journal of Internal Medicine, 2008
Identification and characterization of two non-secreted PCSK9 mutants associated with familial hypercholesterolemia in cohorts from New Zealand and South Africa.
Homer VM et al.
Atherosclerosis, 2008
Secreted PCSK9 promotes LDL receptor degradation independently of proteolytic activity.
Li J et al.
The Biochemical Journal, 2007
Catalytic activity is not required for secreted PCSK9 to reduce low density lipoprotein receptors in HepG2 cells.
McNutt MC et al.
The Journal of Biological Chemistry, 2007
Effects of pH and low density lipoprotein (LDL) on PCSK9-dependent LDL receptor regulation.
Fisher TS et al.
The Journal of Biological Chemistry, 2007
Unravelling the functional significance of PCSK9.
Lambert G
Current Opinion in Lipidology, 2007
Effect of mutations in the PCSK9 gene on the cell surface LDL receptors.
Cameron J et al.
Human Molecular Genetics, 2006
PCSK9: a promising therapeutic target for dyslipidemias?
Lambert G et al.
Trends in Endocrinology and Metabolism: Tem, 2006
Low-density lipoprotein receptor activity in Epstein-Barr virus-transformed lymphocytes from heterozygotes for the D374Y mutation in the PCSK9 gene.
Holla ØL et al.
Scandinavian Journal of Clinical and Laboratory Investigation, 2006
Severe hypercholesterolemia in four British families with the D374Y mutation in the PCSK9 gene: long-term follow-up and treatment response.
Naoumova RP et al.
Arteriosclerosis, Thrombosis, and Vascular Biology, 2005
Evidence for effect of mutant PCSK9 on apolipoprotein B secretion as the cause of unusually severe dominant hypercholesterolaemia.
Sun XM et al.
Human Molecular Genetics, 2005
[PCSK9: a new gene involved in familial hypercholesteremia].
Lambert G et al.
Medecine Sciences : M/s, 2004
Post-transcriptional regulation of low density lipoprotein receptor protein by proprotein convertase subtilisin/kexin type 9a in mouse liver.
Park SW et al.
The Journal of Biological Chemistry, 2004