Jamie Cameron
Publications 2023
Self-Assembled Surfactant-Polyoxovanadate Soft Materials as Tuneable Vanadium Oxide Cathode Precursors for Lithium-Ion Batteries
Angew Chem Int Ed Engl (in press)
DOI 10.1002/anie.202216066, PubMed 36637995
Publications 2022
Privacy and safety: Issues of dual compliance in high-secure and other forensic psychiatric hospitals
Int J Law Psychiatry, 82, 101780
DOI 10.1016/j.ijlp.2022.101780, PubMed 35279456
Publications 2021
Characteristics, treatment patterns, and residual cardiovascular risk of patients with a first acute myocardial infarction: A nationwide population-based cohort study in Norway
Fundam Clin Pharmacol, 36 (3), 563-571
DOI 10.1111/fcp.12744, PubMed 34904750
Publications 2017
Investigation of a Medieval Pilgrim Burial Excavated from the Leprosarium of St Mary Magdalen Winchester, UK
PLoS Negl Trop Dis, 11 (1), e0005186
DOI 10.1371/journal.pntd.0005186, PubMed 28125649
Publications 2016
Studies of the autoinhibitory segment comprising residues 31-60 of the prodomain of PCSK9: Possible implications for the mechanism underlying gain-of-function mutations
Mol Genet Metab Rep, 9, 86-93
DOI 10.1016/j.ymgmr.2016.11.003, PubMed 27896130
Publications 2014
New dentist spotlight: Dr. Jamie Cameron
J Okla Dent Assoc, 105 (1), 27
PubMed 24624747
Publications 2012
Serum levels of proprotein convertase subtilisin/kexin type 9 in subjects with familial hypercholesterolemia indicate that proprotein convertase subtilisin/kexin type 9 is cleared from plasma by low-density lipoprotein receptor-independent pathways
Transl Res, 160 (2), 125-30
DOI 10.1016/j.trsl.2012.01.010, PubMed 22683370
Mutations in the SORT1 gene are unlikely to cause autosomal dominant hypercholesterolemia
Atherosclerosis, 225 (2), 370-5
DOI 10.1016/j.atherosclerosis.2012.10.026, PubMed 23102784
Publications 2011
Role of the C-terminal domain of PCSK9 in degradation of the LDL receptors
J Lipid Res, 52 (10), 1787-94
DOI 10.1194/jlr.M018093, PubMed 21771976
Removal of acidic residues of the prodomain of PCSK9 increases its activity towards the LDL receptor
Biochem Biophys Res Commun, 406 (2), 234-8
DOI 10.1016/j.bbrc.2011.02.023, PubMed 21324305
The cytoplasmic domain is not involved in directing Class 5 mutant LDL receptors to lysosomal degradation
Biochem Biophys Res Commun, 408 (4), 642-6
DOI 10.1016/j.bbrc.2011.04.077, PubMed 21531209
Characterization of residues in the cytoplasmic domain of the LDL receptor required for exit from the endoplasmic reticulum
Biochem Biophys Res Commun, 415 (4), 642-5
DOI 10.1016/j.bbrc.2011.10.127, PubMed 22079632
Interaction between the ligand-binding domain of the LDL receptor and the C-terminal domain of PCSK9 is required for PCSK9 to remain bound to the LDL receptor during endosomal acidification
Hum Mol Genet, 21 (6), 1402-9
DOI 10.1093/hmg/ddr578, PubMed 22156580
Characterization of a naturally occurring degradation product of the LDL receptor
Mol Genet Metab, 105 (1), 149-54
DOI 10.1016/j.ymgme.2011.10.008, PubMed 22078455
Publications 2010
Disrupted recycling of the low density lipoprotein receptor by PCSK9 is not mediated by residues of the cytoplasmic domain
Mol Genet Metab, 101 (1), 76-80
DOI 10.1016/j.ymgme.2010.05.003, PubMed 20659812
Publications 2009
Splice-site mutation c.313+1, G>A in intron 3 of the LDL receptor gene results in transcripts with skipping of exon 3 and inclusion of intron 3
Clin Chim Acta, 403 (1-2), 131-5
DOI 10.1016/j.cca.2009.02.001, PubMed 19361455
Tangier disease caused by compound heterozygosity for ABCA1 mutations R282X and Y1532C
Atherosclerosis, 209 (1), 163-6
DOI 10.1016/j.atherosclerosis.2009.08.039, PubMed 19765707
A chimeric LDL receptor containing the cytoplasmic domain of the transferrin receptor is degraded by PCSK9
Mol Genet Metab, 99 (2), 149-56
DOI 10.1016/j.ymgme.2009.09.012, PubMed 19828345
Loss-of-function mutation R46L in the PCSK9 gene has little impact on the levels of total serum cholesterol in familial hypercholesterolemia heterozygotes
Clin Chim Acta, 411 (3-4), 229-33
DOI 10.1016/j.cca.2009.11.008, PubMed 19917273
Publications 2008
PCSK9-mediated degradation of the LDL receptor
In Series of dissertations submitted to the Faculty of Medicine, University of Oslo, Unipub, Oslo, no. 649, 1 b. (flere pag.)
BIBSYS 081144954, ISBN 978-82-8072-276-8
Investigations on the evolutionary conservation of PCSK9 reveal a functionally important protrusion
FEBS J, 275 (16), 4121-33
DOI 10.1111/j.1742-4658.2008.06553.x, PubMed 18631360
Mutation S462P in the PCSK9 gene reduces secretion of mutant PCSK9 without affecting the autocatalytic cleavage
Atherosclerosis, 203 (1), 161-5
DOI 10.1016/j.atherosclerosis.2008.10.007, PubMed 19022446
Berberine decreases PCSK9 expression in HepG2 cells
Atherosclerosis, 201 (2), 266-73
DOI 10.1016/j.atherosclerosis.2008.02.004, PubMed 18355829
Publications 2007
Degradation of the LDL receptors by PCSK9 is not mediated by a secreted protein acted upon by PCSK9 extracellularly
BMC Cell Biol, 8, 9
DOI 10.1186/1471-2121-8-9, PubMed 17328821
Publications 2006
Effect of mutations in the PCSK9 gene on the cell surface LDL receptors
Hum Mol Genet, 15 (9), 1551-8
DOI 10.1093/hmg/ddl077, PubMed 16571601