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Cholesteryl ester transfer protein: A novel target for raising HDL and inhibiting atherosclerosis
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Role of apoA-II in lipid metabolism and atherosclerosis: Advances in the study of an enigmatic protein
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Blanco-Vaca F, Escola-Gil JC, Martin-Campos JM, Juive J. Role of apoA-II in lipid metabolism and atherosclerosis: advances in the study of an enigmatic protein. J Lipid Res 2001; 42:1727-1739.
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ApoA-II versus ApoA-I: Two for one is not always a good deal
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Castellani LW, Lusis AJ. ApoA-II versus ApoA-I: two for one is not always a good deal. Arterioscler Thromb Vasc Biol 2001; 21:1870-1872.
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ApoAV reduces plasma triglycerides by inhibiting very low density lipoprotein-triglyceride (VLDL-TG) production and stimulating lipoprotein lipase-mediated VLDL-TG hydrolysis
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Schaap FG, Rensen PC, Voshol PJ, et al. ApoAV reduces plasma triglycerides by inhibiting very low density lipoprotein-triglyceride (VLDL-TG) production and stimulating lipoprotein lipase-mediated VLDL-TG hydrolysis. J Biol Chem 2004; 279:27941-27947.
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Meir KS, Leitersdorf E. Atherosclerosis in the apolipoprotein-E-deficient mouse: a decade of progress. Arterioscler Thromb Vasc Biol 2004; 24:1006-1014.
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Human serum Paraoxonase/Arylesterase's retained hydrophobic N-terminal leader sequence associates with HDLs by binding phospholipids: Apolipoprotein A-I stabilizes activity
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Sorenson RC, Bisgaier CL, Aviram M, et al. Human serum Paraoxonase/Arylesterase's retained hydrophobic N-terminal leader sequence associates with HDLs by binding phospholipids: apolipoprotein A-I stabilizes activity. Arterioscler Thromb Vasc Biol 1999; 19:2214-2225.
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Sorenson, R.C.1
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Characterization of apoM in normal and genetically modified mice
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Faber K, Axler O, Dahlback B, Nielsen LB. Characterization of apoM in normal and genetically modified mice. J Lipid Res 2004; 45:1272-1278.
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Faber, K.1
Axler, O.2
Dahlback, B.3
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Specific tissue expression and cellular localization of human apolipoprotein M as determined by in situ hybridization
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Zhang XY, Dong X, Zheng L, et al. Specific tissue expression and cellular localization of human apolipoprotein M as determined by in situ hybridization. Acta Histochem 2003; 105:67-72.
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Expression pattern of apolipoprotein M during mouse and human embryogenesis
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Zhang XY, Jiao GQ, Hurtig M, et al. Expression pattern of apolipoprotein M during mouse and human embryogenesis. Acta Histochem 2004; 106:123-128.
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Zhang, X.Y.1
Jiao, G.Q.2
Hurtig, M.3
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Regulation of apolipoprotein M gene expression by MODY3 gene hepatocyte nuclear factor-1 alpha: Haploinsufficiency is associated with reduced serum apolipoprotein M levels
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Richter S, Shih DQ, Pearson ER, et al. Regulation of apolipoprotein M gene expression by MODY3 gene hepatocyte nuclear factor-1 alpha: haploinsufficiency is associated with reduced serum apolipoprotein M levels. Diabetes 2003; 52:2989-2995.
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Richter, S.1
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Transcriptional profiling reveals global defects in energy metabolism, lipoprotein, and bile acid synthesis and transport with reversal by leptin treatment in ob/ob mouse liver
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Liang CP, Tall AR. Transcriptional profiling reveals global defects in energy metabolism, lipoprotein, and bile acid synthesis and transport with reversal by leptin treatment in ob/ob mouse liver. J Biol Chem 2001; 276:49066-49076.
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Liang, C.P.1
Tall, A.R.2
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18
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3843114406
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Both leptin and leptin-receptor are essential for apolipoprotein M expression in vivo
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Xu N, Nilsson-Ehle P, Hurtig M, Ahren B. Both leptin and leptin-receptor are essential for apolipoprotein M expression in vivo. Biochem Biophys Res Commun 2004; 321:916-921.
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Xu, N.1
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Hurtig, M.3
Ahren, B.4
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19
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0036293085
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Effects of platelet-activating factor, tumor necrosis factor, and interleukin-1 alpha on the expression of apolipoprotein M in HepG2 cells
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Xu N, Zhang XY, Dong X, et al. Effects of platelet-activating factor, tumor necrosis factor, and interleukin-1 alpha on the expression of apolipoprotein M in HepG2 cells. Biochem Biophys Res Commun 2002; 292:944-950.
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Xu, N.1
Zhang, X.Y.2
Dong, X.3
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20
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Transforming growth factor-beta down-regulates apolipoprotein M in HepG2 cells
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Xu N, Hurtig M, Zhang XY, et al. Transforming growth factor-beta down-regulates apolipoprotein M in HepG2 cells. Biochim Biophys Acta 2004; 1683:33-37.
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Biochim Biophys Acta
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Xu, N.1
Hurtig, M.2
Zhang, X.Y.3
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21
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Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis
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Duan J, Dahlback B, Villoutreix BO. Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis. FEBS Lett 2001; 499:127-132.
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Duan, J.1
Dahlback, B.2
Villoutreix, B.O.3
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22
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0026475945
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Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography
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Bocskei Z, Groom CR, Flower DR, et al. Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography. Nature 1992; 360:186-188.
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Bocskei, Z.1
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Lipoproteomios I: Mapping of proteins in low-density lipoprotein using two-dimensional gel electrophoresis and mass spectrometry
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Karlsson H, Leanderson P, Tagesson C, Lindahl M. Lipoproteomios I: mapping of proteins in low-density lipoprotein using two-dimensional gel electrophoresis and mass spectrometry. Proteomics 2005; 5:551-565. The authors have used 2D gels and mass spectrometry to provide new insight into the apolipoprotein composition of LDL.
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Proteomics
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Karlsson, H.1
Leanderson, P.2
Tagesson, C.3
Lindahl, M.4
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24
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Apolipoprotein M is required for prebeta-HDL formation and cholesterol efflux to HDL and protects against atherosclerosis
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Wolfrum C, Poy MN, Stoffel M. Apolipoprotein M is required for prebeta-HDL formation and cholesterol efflux to HDL and protects against atherosclerosis. Nat Med 2005; 11:418-422. The authors used siRNA to reduce apoM expression in mice which resulted in the appearance of large HDL and the disappearance of preβ-HDL in plasma. Adenovirus-mediated overexpression of apoM resulted in decreased atherosclerosis in LDL-receptor deficient mice.
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(2005)
Nat Med
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Wolfrum, C.1
Poy, M.N.2
Stoffel, M.3
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25
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29444434760
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Megalin is a receptor for apolipoprotein M and kidney-specific megalin-deficiency confers urinary excretion of apolipoprotein M
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Epub ahead of print
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Faber K, Hvidberg V, Moestrup SK, et al. Megalin is a receptor for apolipoprotein M and kidney-specific megalin-deficiency confers urinary excretion of apolipoprotein M. Mol Endocrinol 2006; 20:212-218. [Epub ahead of print]. The authors demonstrate that apoM is a ligand for megalin in the proximal tubule of the kidney.
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(2006)
Mol Endocrinol
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, pp. 212-218
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Faber, K.1
Hvidberg, V.2
Moestrup, S.K.3
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