Published in J Biol Chem on September 10, 2014
Molecular and cellular function of the proprotein convertase subtilisin/kexin type 9 (PCSK9). Basic Res Cardiol (2015) 0.85
Suppressor of Cytokine Signaling-3 (SOCS-3) Induces Proprotein Convertase Subtilisin Kexin Type 9 (PCSK9) Expression in Hepatic HepG2 Cell Line. J Biol Chem (2015) 0.78
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Point mutations at the catalytic site of PCSK9 inhibit folding, autoprocessing, and interaction with the LDL receptor. Protein Sci (2016) 0.75
Endoplasmic reticulum stress and Ca2+ depletion differentially modulate the sterol-regulatory protein PCSK9 to control lipid metabolism. J Biol Chem (2016) 0.75
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Sequence variations in PCSK9, low LDL, and protection against coronary heart disease. N Engl J Med (2006) 23.83
Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat Methods (2009) 22.47
Low LDL cholesterol in individuals of African descent resulting from frequent nonsense mutations in PCSK9. Nat Genet (2005) 12.12
Mutations in PCSK9 cause autosomal dominant hypercholesterolemia. Nat Genet (2003) 11.67
Effect of a monoclonal antibody to PCSK9 on LDL cholesterol. N Engl J Med (2012) 8.24
The secretory proprotein convertase neural apoptosis-regulated convertase 1 (NARC-1): liver regeneration and neuronal differentiation. Proc Natl Acad Sci U S A (2003) 5.26
Evolutionary optimization of fluorescent proteins for intracellular FRET. Nat Biotechnol (2005) 4.75
NARC-1/PCSK9 and its natural mutants: zymogen cleavage and effects on the low density lipoprotein (LDL) receptor and LDL cholesterol. J Biol Chem (2004) 4.37
Adenoviral-mediated expression of Pcsk9 in mice results in a low-density lipoprotein receptor knockout phenotype. Proc Natl Acad Sci U S A (2004) 4.27
A 52-week placebo-controlled trial of evolocumab in hyperlipidemia. N Engl J Med (2014) 4.14
Post-transcriptional regulation of low density lipoprotein receptor protein by proprotein convertase subtilisin/kexin type 9a in mouse liver. J Biol Chem (2004) 3.93
Secreted PCSK9 decreases the number of LDL receptors in hepatocytes and in livers of parabiotic mice. J Clin Invest (2006) 3.54
Molecular characterization of loss-of-function mutations in PCSK9 and identification of a compound heterozygote. Am J Hum Genet (2006) 3.38
An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol. BMC Biotechnol (2008) 3.27
The biology and therapeutic targeting of the proprotein convertases. Nat Rev Drug Discov (2012) 3.18
Overexpression of PCSK9 accelerates the degradation of the LDLR in a post-endoplasmic reticulum compartment. Proc Natl Acad Sci U S A (2005) 3.15
Structural and biophysical studies of PCSK9 and its mutants linked to familial hypercholesterolemia. Nat Struct Mol Biol (2007) 2.76
Molecular basis for LDL receptor recognition by PCSK9. Proc Natl Acad Sci U S A (2008) 2.42
The cellular trafficking of the secretory proprotein convertase PCSK9 and its dependence on the LDLR. Traffic (2007) 2.09
The crystal structure of PCSK9: a regulator of plasma LDL-cholesterol. Structure (2007) 1.99
Catalytic activity is not required for secreted PCSK9 to reduce low density lipoprotein receptors in HepG2 cells. J Biol Chem (2007) 1.97
Functional characterization of Narc 1, a novel proteinase related to proteinase K. Arch Biochem Biophys (2003) 1.88
The proprotein convertase PCSK9 induces the degradation of low density lipoprotein receptor (LDLR) and its closest family members VLDLR and ApoER2. J Biol Chem (2007) 1.84
PCSK9: a key modulator of cardiovascular health. Circ Res (2014) 1.71
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Antagonism of secreted PCSK9 increases low density lipoprotein receptor expression in HepG2 cells. J Biol Chem (2009) 1.65
Dissection of the endogenous cellular pathways of PCSK9-induced low density lipoprotein receptor degradation: evidence for an intracellular route. J Biol Chem (2009) 1.49
Structure-based drug design: the discovery of novel nonpeptide orally active inhibitors of human renin. Chem Biol (2000) 1.37
The hypercholesterolemia-risk gene SORT1 facilitates PCSK9 secretion. Cell Metab (2014) 1.32
The self-inhibited structure of full-length PCSK9 at 1.9 A reveals structural homology with resistin within the C-terminal domain. Proc Natl Acad Sci U S A (2007) 1.29
The multifaceted proprotein convertases: their unique, redundant, complementary, and opposite functions. J Biol Chem (2013) 1.27
SEC24A deficiency lowers plasma cholesterol through reduced PCSK9 secretion. Elife (2013) 1.18
Novel loss-of-function PCSK9 variant is associated with low plasma LDL cholesterol in a French-Canadian family and with impaired processing and secretion in cell culture. Clin Chem (2011) 1.14
Loss- and gain-of-function PCSK9 variants: cleavage specificity, dominant negative effects, and low density lipoprotein receptor (LDLR) degradation. J Biol Chem (2012) 1.00
Folding pathway mediated by an intramolecular chaperone. The inhibitory and chaperone functions of the subtilisin propeptide are not obligatorily linked. J Biol Chem (2000) 0.92
Genetic defects causing familial hypercholesterolaemia: identification of deletions and duplications in the LDL-receptor gene and summary of all mutations found in patients attending the Hammersmith Hospital Lipid Clinic. Atherosclerosis (2006) 0.91
Novel domain interaction regulates secretion of proprotein convertase subtilisin/kexin type 9 (PCSK9) protein. J Biol Chem (2011) 0.90
Mutation S462P in the PCSK9 gene reduces secretion of mutant PCSK9 without affecting the autocatalytic cleavage. Atherosclerosis (2008) 0.82
PCSK9 acts as a chaperone for the LDL receptor in the endoplasmic reticulum. Biochem J (2014) 0.81
Cellular and secreted pro-protein convertase subtilisin/kexin type 9 catalytic activity in hepatocytes. Atherosclerosis (2009) 0.81
PCSK9 prosegment chimera as novel inhibitors of LDLR degradation. PLoS One (2013) 0.77