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Volumn 5, Issue 1, 2010, Pages 117-130

Mechanisms of lipase maturation

Author keywords

Chaperone; Endoplasmic reticulum; Endothelial lipase; Glycosylation; Hepatic lipase; Lipase maturation factor 1; Lipoprotein lipase; Protein folding

Indexed keywords

CALNEXIN; CALRETICULIN; ENDOTHELIAL LIPASE; LIPOPROTEIN LIPASE; LIVER TRIACYLGLYCEROL LIPASE; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 77649147852     PISSN: 17460875     EISSN: None     Source Type: Journal    
DOI: 10.2217/clp.09.84     Document Type: Review
Times cited : (24)

References (114)
  • 2
    • 0036317550 scopus 로고    scopus 로고
    • The lipase gene family
    • Wong H, Schotz MC: The lipase gene family. J. Lipid Res. 43, 993-999 (2002).
    • (2002) J. Lipid Res. , vol.43 , pp. 993-999
    • Wong, H.1    Schotz, M.C.2
  • 3
    • 0036460675 scopus 로고    scopus 로고
    • Lipoprotein lipase: Structure, function, regulation, and role in disease
    • Mead JR, Irvine SA, Ramji DP: Lipoprotein lipase: structure, function, regulation, and role in disease. J. Mol. Med. 80, 753-769 (2002).
    • (2002) J. Mol. Med. , vol.80 , pp. 753-769
    • Mead, J.R.1    Irvine, S.A.2    Ramji, D.P.3
  • 4
    • 0036906508 scopus 로고    scopus 로고
    • Lipoprotein lipase: Genetics, lipid uptake, and regulation
    • Merkel M, Eckel RH, Goldberg IJ: Lipoprotein lipase: genetics, lipid uptake, and regulation. J. Lipid Res. 43, 1997-2006 (2002).
    • (2002) J. Lipid Res. , vol.43 , pp. 1997-2006
    • Merkel, M.1    Eckel, R.H.2    Goldberg, I.J.3
  • 5
    • 0043197153 scopus 로고    scopus 로고
    • Lipoprotein lipase and atherosclerosis
    • Stein Y, Stein O: Lipoprotein lipase and atherosclerosis. Atherosclerosis 170, 1-9 (2003).
    • (2003) Atherosclerosis , vol.170 , pp. 1-9
    • Stein, Y.1    Stein, O.2
  • 6
    • 66349126859 scopus 로고    scopus 로고
    • Regulation of fatty acid uptake into tissues: Lipoprotein lipase-and CD36-mediated pathways
    • Goldberg IJ, Eckel RH, Abumrad NA: Regulation of fatty acid uptake into tissues: lipoprotein lipase-and CD36-mediated pathways. J. Lipid Res. 50(Suppl.) S86-S90 (2009).
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Goldberg, I.J.1    Eckel, R.H.2    Abumrad, N.A.3
  • 7
    • 5444233816 scopus 로고    scopus 로고
    • Lipoprotein lipase and its role in regulation of plasma lipoproteins and cardiac risk
    • Otarod JK, Goldberg IJ: Lipoprotein lipase and its role in regulation of plasma lipoproteins and cardiac risk. Curr. Atheroscler. Rep. 6, 335-342 (2004).
    • (2004) Curr. Atheroscler. Rep. , vol.6 , pp. 335-342
    • Otarod, J.K.1    Goldberg, I.J.2
  • 8
    • 0028129833 scopus 로고
    • Lipoprotein lipase. Molecular model based on the pancreatic lipase x-ray structure: Consequences for heparin binding and catalysis
    • van Tilbeurgh H, Roussel A, Lalouel JM, Cambillau C: Lipoprotein lipase. Molecular model based on the pancreatic lipase x-ray structure: consequences for heparin binding and catalysis. J. Biol. Chem. 269, 4626-4633 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 4626-4633
    • Van Tilbeurgh, H.1    Roussel, A.2    Lalouel, J.M.3    Cambillau, C.4
  • 12
    • 0032839019 scopus 로고    scopus 로고
    • Hepatic lipase: New insights from genetic and metabolic studies
    • Cohen JC, Vega GL, Grundy SM: Hepatic lipase: new insights from genetic and metabolic studies. Curr. Opin. Lipidol. 10, 259-267 (1999).
    • (1999) Curr. Opin. Lipidol. , vol.10 , pp. 259-267
    • Cohen, J.C.1    Vega, G.L.2    Grundy, S.M.3
  • 13
    • 0036739254 scopus 로고    scopus 로고
    • Hepatic lipase: A pro-or anti-atherogenic protein?
    • Jansen, H, Verhoeven AJ, Sijbrands EJ: Hepatic lipase: a pro-or anti-atherogenic protein? J. Lipid Res. 43, 1352-1362 (2002).
    • (2002) J. Lipid Res. , vol.43 , pp. 1352-1362
    • Jansen, H.1    Verhoeven, A.J.2    Sijbrands, E.J.3
  • 14
    • 0034007631 scopus 로고    scopus 로고
    • Endothelial lipase: A new member of the triglyceride lipase gene family
    • Rader DJ, Jaye M: Endothelial lipase: a new member of the triglyceride lipase gene family. Curr. Opin. Lipidol. 11, 141-147 (2000).
    • (2000) Curr. Opin. Lipidol. , vol.11 , pp. 141-147
    • Rader, D.J.1    Jaye, M.2
  • 15
    • 3242689803 scopus 로고    scopus 로고
    • Endothelial lipase: A modulator of lipoprotein metabolism upregulated by inflammation
    • Broedl UC, Jin W, Rader DJ: Endothelial lipase: a modulator of lipoprotein metabolism upregulated by inflammation. Trends Cardiovasc. Med. 14, 202-206 (2004).
    • (2004) Trends Cardiovasc. Med. , vol.14 , pp. 202-206
    • Broedl, U.C.1    Jin, W.2    Rader, D.J.3
  • 16
    • 3142683071 scopus 로고    scopus 로고
    • The role of endothelial lipase in high-density lipoprotein metabolism
    • Badellino KO, Rader DJ: The role of endothelial lipase in high-density lipoprotein metabolism. Curr. Opin. Cardiol. 19, 392-395 (2004).
    • (2004) Curr. Opin. Cardiol. , vol.19 , pp. 392-395
    • Badellino, K.O.1    Rader, D.J.2
  • 17
    • 0030848587 scopus 로고    scopus 로고
    • Lipase engineering: A window into structure-function relationships
    • Wong H, Davis RC, Hill JS, Yang D, Schotz MC: Lipase engineering: a window into structure-function relationships. Methods Enzymol. 284, 171-184 (1997).
    • (1997) Methods Enzymol , vol.284 , pp. 171-184
    • Wong, H.1    Davis, R.C.2    Hill, J.S.3    Yang, D.4    Schotz, M.C.5
  • 18
    • 0026355156 scopus 로고
    • Effects of gene mutations in lipoprotein and hepatic lipases as interpreted by a molecular model of the pancreatic triglyceride lipase
    • Derewenda ZS, Cambillau C: Effects of gene mutations in lipoprotein and hepatic lipases as interpreted by a molecular model of the pancreatic triglyceride lipase. J. Biol. Chem. 266, 23112-23119 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 23112-23119
    • Derewenda, Z.S.1    Cambillau, C.2
  • 19
    • 55849135236 scopus 로고    scopus 로고
    • Molecular processes that handle - And mishandle - Dietary lipids
    • Williams KJ: Molecular processes that handle - and mishandle - dietary lipids. J. Clin. Invest. 118, 3247-3259 (2008).
    • (2008) J. Clin. Invest. , vol.118 , pp. 3247-3259
    • Williams, K.J.1
  • 20
    • 34447314745 scopus 로고    scopus 로고
    • GPIHBP1: An endothelial cell molecule important for the lipolytic processing of chylomicrons
    • Young SG, Davies BS, Fong LG et al.: GPIHBP1: an endothelial cell molecule important for the lipolytic processing of chylomicrons. Curr. Opin. Lipidol. 18, 389-396 (2007).
    • (2007) Curr. Opin. Lipidol. , vol.18 , pp. 389-396
    • Young, S.G.1    Davies, B.S.2    Fong, L.G.3
  • 21
    • 33747861410 scopus 로고    scopus 로고
    • Vascular lipases, inflammation and atherosclerosis
    • Hasham SN, Pillarisetti S: Vascular lipases, inflammation and atherosclerosis. Clin. Chim. Acta 372, 179-183 (2006).
    • (2006) Clin. Chim. Acta , vol.372 , pp. 179-183
    • Hasham, S.N.1    Pillarisetti, S.2
  • 22
    • 15744401980 scopus 로고    scopus 로고
    • Pancreatic b-cell lipoprotein lipase independently regulates islet glucose metabolism and normal insulin secretion
    • Pappan KL, Pan Z, Kwon G et al.: Pancreatic b-cell lipoprotein lipase independently regulates islet glucose metabolism and normal insulin secretion. J. Biol. Chem. 280, 9023-9029 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 9023-9029
    • Pappan, K.L.1    Pan, Z.2    Kwon, G.3
  • 23
    • 33845564061 scopus 로고    scopus 로고
    • Endothelial lipase is associated with inflammation in humans
    • Paradis ME, Badellino KO, Rader DJ et al.: Endothelial lipase is associated with inflammation in humans. J. Lipid Res. 47, 2808-2813 (2006).
    • (2006) J. Lipid Res. , vol.47 , pp. 2808-2813
    • Paradis, M.E.1    Badellino, K.O.2    Rader, D.J.3
  • 25
    • 0036161909 scopus 로고    scopus 로고
    • Lipoprotein lipase in the arterial wall: Linking LDL to the arterial extracellular matrix and much more
    • Pentikainen MO, Oksjoki R, Oorni K, Kovanen PT: Lipoprotein lipase in the arterial wall: linking LDL to the arterial extracellular matrix and much more. Arterioscler. Thromb. Vasc. Biol. 22, 211-217 (2002).
    • (2002) Arterioscler. Thromb. Vasc. Biol. , vol.22 , pp. 211-217
    • Pentikainen, M.O.1    Oksjoki, R.2    Oorni, K.3    Kovanen, P.T.4
  • 26
    • 0036775676 scopus 로고    scopus 로고
    • Lipoprotein lipase: The regulation of tissue specific expression and its role in lipid and energy metabolism
    • Preiss-Landl K, Zimmermann R, Hammerle G, Zechner R: Lipoprotein lipase: the regulation of tissue specific expression and its role in lipid and energy metabolism. Curr. Opin. Lipidol. 13, 471-481 (2002).
    • (2002) Curr. Opin. Lipidol. , vol.13 , pp. 471-481
    • Preiss-Landl, K.1    Zimmermann, R.2    Hammerle, G.3    Zechner, R.4
  • 27
    • 0036729604 scopus 로고    scopus 로고
    • Overexpression of muscle lipoprotein lipase and insulin sensitivity
    • Pulawa LK, Eckel RH: Overexpression of muscle lipoprotein lipase and insulin sensitivity. Curr. Opin. Clin. Nutr. Metab. Care 5, 569-574 (2002).
    • (2002) Curr. Opin. Clin. Nutr. Metab. Care , vol.5 , pp. 569-574
    • Pulawa, L.K.1    Eckel, R.H.2
  • 28
    • 0025062291 scopus 로고
    • Structure of human pancreatic lipase
    • Winkler FK, D'Arcy A, Hunziker W: Structure of human pancreatic lipase. Nature 343, 771-774 (1990).
    • (1990) Nature , vol.343 , pp. 771-774
    • Winkler, F.K.1    D'Arcy, A.2    Hunziker, W.3
  • 29
    • 69949158815 scopus 로고    scopus 로고
    • Identification of the active form of endothelial lipase, a homodimer in a head-to-tail conformation
    • Griffon N, Jin W, Petty TJ et al.: Identification of the active form of endothelial lipase, a homodimer in a head-to-tail conformation. J. Biol. Chem. 284, 23322-23330 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 23322-23330
    • Griffon, N.1    Jin, W.2    Petty, T.J.3
  • 30
    • 0030874881 scopus 로고    scopus 로고
    • Lipases and a/b hydrolase fold
    • Schrag JD, Cygler M: Lipases and a/b hydrolase fold. Methods Enzymol. 284, 85-107 (1997).
    • (1997) Methods Enzymol , vol.284 , pp. 85-107
    • Schrag, J.D.1    Cygler, M.2
  • 32
    • 0036915668 scopus 로고    scopus 로고
    • The triglyceride lipases of the pancreas
    • Lowe ME: The triglyceride lipases of the pancreas. J. Lipid Res. 43, 2007-2016 (2002).
    • (2002) J. Lipid Res. , vol.43 , pp. 2007-2016
    • Lowe, M.E.1
  • 33
    • 0030828951 scopus 로고    scopus 로고
    • Hepatic lipase: High-level expression and subunit structure determination
    • Hill JS, Davis RC, Yang D, Schotz MC, Wong H: Hepatic lipase: high-level expression and subunit structure determination. Methods Enzymol. 284, 232-246 (1997).
    • (1997) Methods Enzymol , vol.284 , pp. 232-246
    • Hill, J.S.1    Davis, R.C.2    Yang, D.3    Schotz, M.C.4    Wong, H.5
  • 34
    • 0030951329 scopus 로고    scopus 로고
    • A molecular biology-based approach to resolve the subunit orientation of lipoprotein lipase
    • Wong H, Yang D, Hill JS, Davis RC, Nikazy J, Schotz MC: A molecular biology-based approach to resolve the subunit orientation of lipoprotein lipase. Proc. Natl Acad. Sci. USA 94, 5594-5598 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5594-5598
    • Wong, H.1    Yang, D.2    Hill, J.S.3    Davis, R.C.4    Nikazy, J.5    Schotz, M.C.6
  • 35
    • 0026572737 scopus 로고
    • Structure and evolution of the lipase superfamily
    • Hide WA, Chan L, Li WH: Structure and evolution of the lipase superfamily. J. Lipid Res. 33, 167-178 (1992).
    • (1992) J. Lipid Res. , vol.33 , pp. 167-178
    • Hide, W.A.1    Chan, L.2    Li, W.H.3
  • 36
    • 0001033625 scopus 로고
    • Familial lipoprotein lipase deficiency and other causes of chylomicronemia syndromes
    • Scriver RS, Beaudet AL, Sly WS (Eds). McGraw Hill, NY, USA
    • Brunzell JD: Familial lipoprotein lipase deficiency and other causes of chylomicronemia syndromes. In: The Metabolic Basis of Inherited Disease. Scriver RS, Beaudet AL, Sly WS (Eds). McGraw Hill, NY, USA, 1913-1932 (1995).
    • (1995) The Metabolic Basis of Inherited Disease , pp. 1913-1932
    • Brunzell, J.D.1
  • 37
    • 0028819754 scopus 로고
    • Severe hypertriglyceridemia, reduced high density lipoprotein, and neonatal death in lipoprotein lipase knockout mice. Mild hypertriglyceridemia with impaired very low density lipoprotein clearance in heterozygotes
    • Weinstock PH, Bisgaier CL, Aalto-Setala K et al.: Severe hypertriglyceridemia, reduced high density lipoprotein, and neonatal death in lipoprotein lipase knockout mice. Mild hypertriglyceridemia with impaired very low density lipoprotein clearance in heterozygotes. J. Clin. Invest. 96, 2555-2568 (1995).
    • (1995) J. Clin. Invest. , vol.96 , pp. 2555-2568
    • Weinstock, P.H.1    Bisgaier, C.L.2    Aalto-Setala, K.3
  • 38
    • 36549038120 scopus 로고    scopus 로고
    • Mutations in LMF1 cause combined lipase deficiency and severe hypertriglyceridemia
    • Peterfy M, Ben-Zeev O, Mao HZ et al.: Mutations in LMF1 cause combined lipase deficiency and severe hypertriglyceridemia. Nat. Genet. 39, 1483-1487 (2007).
    • (2007) Nat. Genet. , vol.39 , pp. 1483-1487
    • Peterfy, M.1    Ben-Zeev, O.2    Mao, H.Z.3
  • 39
    • 33947573537 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons
    • Beigneux AP, Davies BS, Gin P et al.: Glycosylphosphatidylinositol- anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons. Cell Metab. 5, 279-291 (2007).
    • (2007) Cell Metab , vol.5 , pp. 279-291
    • Beigneux, A.P.1    Davies, B.S.2    Gin, P.3
  • 40
    • 58149161560 scopus 로고    scopus 로고
    • Loci influencing lipid levels and coronary heart disease risk in 16 European population cohorts
    • Aulchenko YS, Ripatti S, Lindqvist I et al.: Loci influencing lipid levels and coronary heart disease risk in 16 European population cohorts. Nat. Genet. 41, 47-55 (2009).
    • (2009) Nat. Genet. , vol.41 , pp. 47-55
    • Aulchenko, Y.S.1    Ripatti, S.2    Lindqvist, I.3
  • 41
    • 58149163149 scopus 로고    scopus 로고
    • Common variants at 30 loci contribute to polygenic dyslipidemia
    • Kathiresan S, Willer CJ, Peloso GM et al.: Common variants at 30 loci contribute to polygenic dyslipidemia. Nat. Genet. 41, 56-65 (2009).
    • (2009) Nat. Genet. , vol.41 , pp. 56-65
    • Kathiresan, S.1    Willer, C.J.2    Peloso, G.M.3
  • 42
    • 58149159573 scopus 로고    scopus 로고
    • Genome-wide association analysis of metabolic traits in a birth cohort from a founder population
    • Sabatti C, Service SK, Hartikainen AL et al.: Genome-wide association analysis of metabolic traits in a birth cohort from a founder population. Nat. Genet. 41, 35-46 (2009).
    • (2009) Nat. Genet. , vol.41 , pp. 35-46
    • Sabatti, C.1    Service, S.K.2    Hartikainen, A.L.3
  • 43
    • 38649125868 scopus 로고    scopus 로고
    • Newly identified loci that influence lipid concentrations and risk of coronary artery disease
    • Willer CJ, Sanna S, Jackson AU et al.: Newly identified loci that influence lipid concentrations and risk of coronary artery disease. Nat. Genet. 40, 161-169 (2008).
    • (2008) Nat. Genet. , vol.40 , pp. 161-169
    • Willer, C.J.1    Sanna, S.2    Jackson, A.U.3
  • 46
    • 0034127845 scopus 로고    scopus 로고
    • Genetics of the metabolic syndrome
    • Groop L: Genetics of the metabolic syndrome. Br. J. Nutr. 83(Suppl. 1), S39-S48 (2000).
    • (2000) Br. J. Nutr. , vol.83 , Issue.SUPPL. 1
    • Groop, L.1
  • 47
    • 0037399286 scopus 로고    scopus 로고
    • The metabolic syndrome: Targeting dyslipidaemia to reduce coronary risk
    • Ginsberg HN, Stalenhoef AF: The metabolic syndrome: targeting dyslipidaemia to reduce coronary risk. J. Cardiovasc. Risk 10, 121-128 (2003).
    • (2003) J. Cardiovasc. Risk , vol.10 , pp. 121-128
    • Ginsberg, H.N.1    Stalenhoef, A.F.2
  • 48
    • 0033678739 scopus 로고    scopus 로고
    • The role of lipoprotein lipase in adipose tissue development and metabolism
    • Zechner R, Strauss J, Frank S et al.: The role of lipoprotein lipase in adipose tissue development and metabolism. Int. J. Obes. Relat. Metab. Disord. 24(Suppl. 4), S53-S56 (2000).
    • (2000) Int. J. Obes. Relat. Metab. Disord. , vol.24 , Issue.SUPPL. 4
    • Zechner, R.1    Strauss, J.2    Frank, S.3
  • 49
    • 0029142737 scopus 로고
    • Muscle-specific overexpression of lipoprotein lipase causes a severe myopathy characterized by proliferation of mitochondria and peroxisomes in transgenic mice
    • Levak-Frank S, Radner H, Walsh A et al.: Muscle-specific overexpression of lipoprotein lipase causes a severe myopathy characterized by proliferation of mitochondria and peroxisomes in transgenic mice. J. Clin. Invest. 96, 976-986 (1995).
    • (1995) J. Clin. Invest. , vol.96 , pp. 976-986
    • Levak-Frank, S.1    Radner, H.2    Walsh, A.3
  • 50
    • 0032169445 scopus 로고    scopus 로고
    • Lipoprotein lipase expression exclusively in liver. A mouse model for metabolism in the neonatal period and during cachexia
    • Merkel M, Weinstock PH, Chajek-Shaul T et al.: Lipoprotein lipase expression exclusively in liver. A mouse model for metabolism in the neonatal period and during cachexia. J. Clin. Invest. 102, 893-901 (1998)
    • (1998) J. Clin. Invest. , vol.102 , pp. 893-901
    • Merkel, M.1    Weinstock, P.H.2    Chajek-Shaul, T.3
  • 51
    • 0035032163 scopus 로고    scopus 로고
    • Overexpressing human lipoprotein lipase in mouse skeletal muscle is associated with insulin resistance
    • Ferreira LD, Pulawa LK, Jensen DR, Eckel RH: Overexpressing human lipoprotein lipase in mouse skeletal muscle is associated with insulin resistance. Diabetes 50, 1064-1068 (2001).
    • (2001) Diabetes , vol.50 , pp. 1064-1068
    • Ferreira, L.D.1    Pulawa, L.K.2    Jensen, D.R.3    Eckel, R.H.4
  • 52
    • 0035912744 scopus 로고    scopus 로고
    • Tissue-specific overexpression of lipoprotein lipase causes tissue-specific insulin resistance
    • Kim JK, Fillmore JJ, Chen Y et al.: Tissue-specific overexpression of lipoprotein lipase causes tissue-specific insulin resistance. Proc. Natl Acad. Sci. USA 98, 7522-7527 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 7522-7527
    • Kim, J.K.1    Fillmore, J.J.2    Chen, Y.3
  • 53
    • 0030853681 scopus 로고    scopus 로고
    • Prevention of diet-induced obesity in transgenic mice overexpressing skeletal muscle lipoprotein lipase
    • Jensen DR, Schlaepfer IR, Morin CL et al.: Prevention of diet-induced obesity in transgenic mice overexpressing skeletal muscle lipoprotein lipase. Am. J. Physiol. 273, R683-R689 (1997).
    • (1997) Am. J. Physiol. , vol.273
    • Jensen, D.R.1    Schlaepfer, I.R.2    Morin, C.L.3
  • 54
    • 0347990586 scopus 로고    scopus 로고
    • Lipoprotein lipase is a gene for insulin resistance in Mexican Americans
    • Goodarzi MO, Guo X, Taylor KD et al.: Lipoprotein lipase is a gene for insulin resistance in Mexican Americans. Diabetes 53, 214-220 (2004).
    • (2004) Diabetes , vol.53 , pp. 214-220
    • Goodarzi, M.O.1    Guo, X.2    Taylor, K.D.3
  • 55
    • 0036210617 scopus 로고    scopus 로고
    • Insulin sensitivity is impaired in heterozygous carriers of lipoprotein lipase deficiency
    • Holzl B, Iglseder B, Sandhofer A et al.: Insulin sensitivity is impaired in heterozygous carriers of lipoprotein lipase deficiency. Diabetologia 45, 378-384 (2002).
    • (2002) Diabetologia , vol.45 , pp. 378-384
    • Holzl, B.1    Iglseder, B.2    Sandhofer, A.3
  • 56
  • 57
    • 34249725662 scopus 로고    scopus 로고
    • Association of lipoprotein lipase gene polymorphisms with obesity and Type 2 diabetes in an Asian Indian population
    • Radha V, Vimaleswaran KS, Ayyappa KA, Mohan V: Association of lipoprotein lipase gene polymorphisms with obesity and Type 2 diabetes in an Asian Indian population. Int. J. Obes. (Lond.) 31, 913-918 (2007).
    • (2007) Int. J. Obes. (Lond.) , vol.31 , pp. 913-918
    • Radha, V.1    Vimaleswaran, K.S.2    Ayyappa, K.A.3    Mohan, V.4
  • 58
    • 0037316670 scopus 로고    scopus 로고
    • Lipoprotein lipase (LpL) on the surface of cardiomyocytes increases lipid uptake and produces a cardiomyopathy
    • Yagyu H, Chen G, Yokoyama M et al.: Lipoprotein lipase (LpL) on the surface of cardiomyocytes increases lipid uptake and produces a cardiomyopathy. J. Clin. Invest. 111, 419-426 (2003).
    • (2003) J. Clin. Invest. , vol.111 , pp. 419-426
    • Yagyu, H.1    Chen, G.2    Yokoyama, M.3
  • 59
    • 54249093047 scopus 로고    scopus 로고
    • Ceramide is a cardiotoxin in lipotoxic cardiomyopathy
    • Park TS, Hu Y, Noh HL et al.: Ceramide is a cardiotoxin in lipotoxic cardiomyopathy. J. Lipid Res. 49, 2101-2112 (2008).
    • (2008) J. Lipid Res. , vol.49 , pp. 2101-2112
    • Park, T.S.1    Hu, Y.2    Noh, H.L.3
  • 60
    • 34548385838 scopus 로고    scopus 로고
    • Cardiac steatosis in diabetes mellitus: A 1H-magnetic resonance spectroscopy study
    • McGavock JM, Lingvay I, Zib I et al.: Cardiac steatosis in diabetes mellitus: a 1H-magnetic resonance spectroscopy study. Circulation 116, 1170-1175 (2007).
    • (2007) Circulation , vol.116 , pp. 1170-1175
    • McGavock, J.M.1    Lingvay, I.2    Zib, I.3
  • 61
    • 2442492971 scopus 로고    scopus 로고
    • Effect of obesity and insulin resistance on myocardial substrate metabolism and efficiency in young women
    • Peterson LR, Herrero P, Schechtman KB et al.: Effect of obesity and insulin resistance on myocardial substrate metabolism and efficiency in young women. Circulation 109, 2191-2196 (2004).
    • (2004) Circulation , vol.109 , pp. 2191-2196
    • Peterson, L.R.1    Herrero, P.2    Schechtman, K.B.3
  • 62
    • 7744234747 scopus 로고    scopus 로고
    • Intramyocardial lipid accumulation in the failing human heart resembles the lipotoxic rat heart
    • Sharma S, Adrogue JV, Golfman L et al.: Intramyocardial lipid accumulation in the failing human heart resembles the lipotoxic rat heart. FASEB J. 18, 1692-1700 (2004).
    • (2004) FASEB J. , vol.18 , pp. 1692-1700
    • Sharma, S.1    Adrogue, J.V.2    Golfman, L.3
  • 64
    • 0035571614 scopus 로고    scopus 로고
    • Macrophage-specific expression of human lipoprotein lipase accelerates atherosclerosis in transgenic apolipoprotein e knockout mice but not in C57BL/6 mice
    • Wilson K, Fry GL, Chappell DA, Sigmund CD, Medh JD: Macrophage-specific expression of human lipoprotein lipase accelerates atherosclerosis in transgenic apolipoprotein E knockout mice but not in C57BL/6 mice. Arterioscler. Thromb. Vasc. Biol. 21, 1809-1815 (2001).
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 1809-1815
    • Wilson, K.1    Fry, G.L.2    Chappell, D.A.3    Sigmund, C.D.4    Medh, J.D.5
  • 65
    • 67349239041 scopus 로고    scopus 로고
    • Association of lipoprotein lipase D9N polymorphism with myocardial infarction in Type 2 diabetes: The genetics, outcomes, and lipids in Type 2 diabetes (GOLD) study
    • Izar MC, Helfenstein T, Ihara SS et al.: Association of lipoprotein lipase D9N polymorphism with myocardial infarction in Type 2 diabetes: the genetics, outcomes, and lipids in Type 2 diabetes (GOLD) study. Atherosclerosis 204, 165-170 (2009).
    • (2009) Atherosclerosis , vol.204 , pp. 165-170
    • Izar, M.C.1    Helfenstein, T.2    Ihara, S.S.3
  • 66
    • 0027162816 scopus 로고
    • Hepatic lipase deficiency. Clinical, biochemical, and molecular genetic characteristics
    • Hegele RA, Little JA, Vezina C et al.: Hepatic lipase deficiency. Clinical, biochemical, and molecular genetic characteristics. Arterioscler. Thromb. 13, 720-728 (1993).
    • (1993) Arterioscler. Thromb. , vol.13 , pp. 720-728
    • Hegele, R.A.1    Little, J.A.2    Vezina, C.3
  • 67
    • 0031052632 scopus 로고    scopus 로고
    • Heterozygous hepatic lipase deficiency, due to two missense mutations R186H and L334F, in the HL gene
    • Knudsen P, Antikainen M, Uusi-Oukari M et al.: Heterozygous hepatic lipase deficiency, due to two missense mutations R186H and L334F, in the HL gene. Atherosclerosis 128, 165-174 (1997).
    • (1997) Atherosclerosis , vol.128 , pp. 165-174
    • Knudsen, P.1    Antikainen, M.2    Uusi-Oukari, M.3
  • 68
    • 0037316555 scopus 로고    scopus 로고
    • Inhibition of endothelial lipase causes increased HDL cholesterol levels in vivo
    • Jin W, Millar JS, Broedl U, Glick JM, Rader DJ: Inhibition of endothelial lipase causes increased HDL cholesterol levels in vivo. J. Clin. Invest. 111, 357-362 (2003).
    • (2003) J. Clin. Invest. , vol.111 , pp. 357-362
    • Jin, W.1    Millar, J.S.2    Broedl, U.3    Glick, J.M.4    Rader, D.J.5
  • 69
    • 3042702876 scopus 로고    scopus 로고
    • Endothelial lipase promotes the catabolism of ApoB-containing lipoproteins
    • Broedl UC, Maugeais C, Millar JS et al.: Endothelial lipase promotes the catabolism of ApoB-containing lipoproteins. Circ. Res. 94, 1554-1561 (2004).
    • (2004) Circ. Res. , vol.94 , pp. 1554-1561
    • Broedl, U.C.1    Maugeais, C.2    Millar, J.S.3
  • 70
    • 65249186429 scopus 로고    scopus 로고
    • Loss-of-function variants in endothelial lipase are a cause of elevated HDL cholesterol in humans
    • Edmondson AC, Brown RJ, Kathiresan S et al.: Loss-of-function variants in endothelial lipase are a cause of elevated HDL cholesterol in humans. J. Clin. Invest. 119, 1042-1050 (2009).
    • (2009) J. Clin. Invest. , vol.119 , pp. 1042-1050
    • Edmondson, A.C.1    Brown, R.J.2    Kathiresan, S.3
  • 71
    • 21744447192 scopus 로고    scopus 로고
    • The glycan code of the endoplasmic reticulum: Asparagine-linked carbohydrates as protein maturation and quality-control tags
    • Hebert DN, Garman SC, Molinari M: The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags. Trends Cell Biol. 15, 364-370 (2005).
    • (2005) Trends Cell Biol. , vol.15 , pp. 364-370
    • Hebert, D.N.1    Garman, S.C.2    Molinari, M.3
  • 72
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: Protein folding, quality control, degradation, and related human diseases
    • Hebert DN, Molinari M: In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol. Rev. 87, 1377-1408 (2007).
    • (2007) Physiol. Rev. , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 73
    • 0034689022 scopus 로고    scopus 로고
    • Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulum
    • DOI 10.1083/jcb.148.6.1123
    • Trombetta ES, Helenius A: Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulum. J. Cell Biol. 148, 1123-1129 (2000). (Pubitemid 30688121)
    • (2000) Journal of Cell Biology , vol.148 , Issue.6 , pp. 1123-1129
    • Trombetta, E.S.1    Helenius, A.2
  • 74
    • 44849102178 scopus 로고    scopus 로고
    • Getting in and out from calnexin/calreticulin cycles
    • Caramelo JJ, Parodi AJ: Getting in and out from calnexin/calreticulin cycles. J. Biol. Chem. 283, 10221-10225 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 10221-10225
    • Caramelo, J.J.1    Parodi, A.J.2
  • 75
    • 1242316950 scopus 로고    scopus 로고
    • Maturation of hepatic lipase. Formation of functional enzyme in the endoplasmic reticulum is the rate-limiting step in its secretion
    • Ben-Zeev O, Doolittle MH: Maturation of hepatic lipase. Formation of functional enzyme in the endoplasmic reticulum is the rate-limiting step in its secretion. J. Biol. Chem. 279, 6171-6181 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 6171-6181
    • Ben-Zeev, O.1    Doolittle, M.H.2
  • 77
    • 0027931405 scopus 로고
    • Lipoprotein lipase and hepatic lipase: The role of asparagine-linked glycosylation in the expression of a functional enzyme
    • Ben-Zeev O, Stahnke G, Liu G, Davis RC, Doolittle MH: Lipoprotein lipase and hepatic lipase: the role of asparagine-linked glycosylation in the expression of a functional enzyme. J. Lipid Res. 35, 1511-1523 (1994).
    • (1994) J. Lipid Res. , vol.35 , pp. 1511-1523
    • Ben-Zeev, O.1    Stahnke, G.2    Liu, G.3    Davis, R.C.4    Doolittle, M.H.5
  • 78
    • 21344444691 scopus 로고    scopus 로고
    • Role of N-linked glycosylation in the secretion and activity of endothelial lipase
    • Miller GC, Long CJ, Bojilova ED et al.: Role of N-linked glycosylation in the secretion and activity of endothelial lipase. J. Lipid Res. 45, 2080-2087 (2004).
    • (2004) J. Lipid Res. , vol.45 , pp. 2080-2087
    • Miller, G.C.1    Long, C.J.2    Bojilova, E.D.3
  • 79
    • 0027139176 scopus 로고
    • Functional role of N-linked glycosylation in human hepatic lipase: Asparagine-56 is important for both enzyme activity and secretion
    • Wolle J, Jansen H, Smith LC, Chan L: Functional role of N-linked glycosylation in human hepatic lipase: asparagine-56 is important for both enzyme activity and secretion. J. Lipid Res. 34, 2169-2176 (1993).
    • (1993) J. Lipid Res. , vol.34 , pp. 2169-2176
    • Wolle, J.1    Jansen, H.2    Smith, L.C.3    Chan, L.4
  • 80
    • 30044442785 scopus 로고    scopus 로고
    • Calcium triggers folding of lipoprotein lipase into active dimmers
    • Zhang L, Lookene A, Wu G, Olivecrona G: Calcium triggers folding of lipoprotein lipase into active dimers. J. Biol. Chem. 280, 42580-42591 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 42580-42591
    • Zhang, L.1    Lookene, A.2    Wu, G.3    Olivecrona, G.4
  • 81
    • 0026697404 scopus 로고
    • Maturation of lipoprotein lipase. Expression of full catalytic activity requires glucose trimming but not translocation to the cis-Golgi compartment
    • Ben-Zeev O, Doolittle MH, Davis RC, Elovson J, Schotz MC: Maturation of lipoprotein lipase. Expression of full catalytic activity requires glucose trimming but not translocation to the cis-Golgi compartment. J. Biol. Chem. 267, 6219-6227 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 6219-6227
    • Ben-Zeev, O.1    Doolittle, M.H.2    Davis, R.C.3    Elovson, J.4    Schotz, M.C.5
  • 82
    • 0037155921 scopus 로고    scopus 로고
    • Maturation of lipoprotein lipase in the endoplasmic reticulum. Concurrent formation of functional dimers and inactive aggregates
    • Ben-Zeev O, Mao HZ, Doolittle MH: Maturation of lipoprotein lipase in the endoplasmic reticulum. Concurrent formation of functional dimers and inactive aggregates. J. Biol. Chem. 277, 10727-10738 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 10727-10738
    • Ben-Zeev, O.1    Mao, H.Z.2    Doolittle, M.H.3
  • 83
    • 0032738092 scopus 로고    scopus 로고
    • Cld and lec23 are disparate mutations that affect maturation of lipoprotein lipase in the endoplasmic reticulum
    • Briquet-Laugier V, Ben-Zeev O, White A, Doolittle MH: cld and lec23 are disparate mutations that affect maturation of lipoprotein lipase in the endoplasmic reticulum. J. Lipid Res. 40, 2044-2058 (1999).
    • (1999) J. Lipid Res. , vol.40 , pp. 2044-2058
    • Briquet-Laugier, V.1    Ben-Zeev, O.2    White, A.3    Doolittle, M.H.4
  • 85
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia R, Braakman I: Quality control in the endoplasmic reticulum protein factory. Nature 426, 891-894 (2003).
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 86
    • 0344393021 scopus 로고    scopus 로고
    • Quality control and protein folding in the secretory pathway
    • Trombetta ES, Parodi AJ: Quality control and protein folding in the secretory pathway. Annu. Rev. Cell. Dev. Biol. 19, 649-676 (2003).
    • (2003) Annu. Rev. Cell. Dev. Biol. , vol.19 , pp. 649-676
    • Trombetta, E.S.1    Parodi, A.J.2
  • 87
    • 33751508817 scopus 로고    scopus 로고
    • N-glycan processing in ER quality control
    • Ruddock LW, Molinari M: N-glycan processing in ER quality control. J. Cell Sci. 119, 4373-4380 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 4373-4380
    • Ruddock, L.W.1    Molinari, M.2
  • 88
    • 10444226462 scopus 로고    scopus 로고
    • ER stress and the unfolded protein response
    • Schroder M, Kaufman RJ: ER stress and the unfolded protein response. Mutat. Res. 569, 29-63 (2005).
    • (2005) Mutat. Res. , vol.569 , pp. 29-63
    • Schroder, M.1    Kaufman, R.J.2
  • 89
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier L, Usherwood YK, Chung KT, Hendershot LM: A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol. Biol. Cell 13, 4456-4469 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 90
    • 0035195782 scopus 로고    scopus 로고
    • Differential effect of combined lipase deficiency (cld/cld) on human hepatic lipase and lipoprotein lipase secretion
    • Boedeker JC, Doolittle MH, White AL: Differential effect of combined lipase deficiency (cld/cld) on human hepatic lipase and lipoprotein lipase secretion. J. Lipid Res. 42, 1858-1864 (2001).
    • (2001) J. Lipid Res. , vol.42 , pp. 1858-1864
    • Boedeker, J.C.1    Doolittle, M.H.2    White, A.L.3
  • 91
    • 0042206422 scopus 로고    scopus 로고
    • Calreticulin promotes folding/ dimerization of human lipoprotein lipase expressed in insect cells (sf21)
    • Zhang L, Wu G, Tate CG, Lookene A, Olivecrona G: Calreticulin promotes folding/ dimerization of human lipoprotein lipase expressed in insect cells (sf21). J. Biol. Chem. 278, 29344-29351 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 29344-29351
    • Zhang, L.1    Wu, G.2    Tate, C.G.3    Lookene, A.4    Olivecrona, G.5
  • 92
    • 36248973177 scopus 로고    scopus 로고
    • The activities and function of molecular chaperones in the endoplasmic reticulum
    • Buck TM, Wright CM, Brodsky JL: The activities and function of molecular chaperones in the endoplasmic reticulum. Semin. Cell Dev. Biol. 18, 751-761 (2007).
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 751-761
    • Buck, T.M.1    Wright, C.M.2    Brodsky, J.L.3
  • 93
    • 34447558236 scopus 로고    scopus 로고
    • ER chaperones in mammalian development and human diseases
    • Ni M, Lee AS: ER chaperones in mammalian development and human diseases. FEBS Lett. 581, 3641-3651 (2007).
    • (2007) FEBS Lett , vol.581 , pp. 3641-3651
    • Ni, M.1    Lee, A.S.2
  • 94
    • 0033208953 scopus 로고    scopus 로고
    • Role and regulation of the ER chaperone BiP
    • Gething MJ: Role and regulation of the ER chaperone BiP. Semin. Cell Dev. Biol. 10, 465-472 (1999).
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 465-472
    • Gething, M.J.1
  • 95
    • 0027484417 scopus 로고
    • Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
    • Blond-Elguindi S, Cwirla SE, Dower WJ et al.: Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 75, 717-728 (1993).
    • (1993) Cell , vol.75 , pp. 717-728
    • Blond-Elguindi, S.1    Cwirla, S.E.2    Dower, W.J.3
  • 96
    • 0020533322 scopus 로고
    • Combined lipase deficiency (cld): A lethal mutation on chromosome 17 of the mouse
    • Paterniti JR Jr, Brown WV, Ginsberg HN, Artzt K: Combined lipase deficiency (cld): a lethal mutation on chromosome 17 of the mouse. Science 221, 167-169 (1983).
    • (1983) Science , vol.221 , pp. 167-169
    • Paterniti Jr., J.R.1    Brown, W.V.2    Ginsberg, H.N.3    Artzt, K.4
  • 97
    • 0029971197 scopus 로고    scopus 로고
    • Naturally occurring mutations in mice affecting lipid transport and metabolism
    • Reue K, Doolittle MH: Naturally occurring mutations in mice affecting lipid transport and metabolism. J. Lipid Res. 37, 1387-1405 (1996).
    • (1996) J. Lipid Res. , vol.37 , pp. 1387-1405
    • Reue, K.1    Doolittle, M.H.2
  • 98
    • 0025115935 scopus 로고
    • Combined lipase deficiency in the mouse. Evidence of impaired lipase processing and secretion
    • Davis RC, Ben-Zeev O, Martin D, Doolittle MH: Combined lipase deficiency in the mouse. Evidence of impaired lipase processing and secretion. J. Biol. Chem. 265, 17960-17966 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 17960-17966
    • Davis, R.C.1    Ben-Zeev, O.2    Martin, D.3    Doolittle, M.H.4
  • 99
    • 0032103763 scopus 로고    scopus 로고
    • Combined lipase deficiency (cld/cld) in mice affects differently post-translational processing of lipoprotein lipase, hepatic lipase and pancreatic lipase
    • Scow RO, Schultz CJ, Park JW, Blanchette-Mackie EJ: Combined lipase deficiency (cld/cld) in mice affects differently post-translational processing of lipoprotein lipase, hepatic lipase and pancreatic lipase. Chem. Phys. Lipids 93, 149-155 (1998).
    • (1998) Chem. Phys. Lipids , vol.93 , pp. 149-155
    • Scow, R.O.1    Schultz, C.J.2    Park, J.W.3    Blanchette-Mackie, E.J.4
  • 101
    • 0022521074 scopus 로고
    • Effect of the combined lipase deficiency mutation (cld/cld) on ultrastructure of tissues in mice. Diaphragm, heart, brown adipose tissue, lung, and liver
    • Blanchette-Mackie EJ, Wetzel MG, Chernick SS, Paterniti JR Jr, Brown WV, Scow RO: Effect of the combined lipase deficiency mutation (cld/cld) on ultrastructure of tissues in mice. Diaphragm, heart, brown adipose tissue, lung, and liver. Lab. Invest. 55, 347-362 (1986).
    • (1986) Lab. Invest. , vol.55 , pp. 347-362
    • Blanchette-Mackie, E.J.1    Wetzel, M.G.2    Chernick, S.S.3    Paterniti Jr., J.R.4    Brown, W.V.5    Scow, R.O.6
  • 102
    • 33749578038 scopus 로고    scopus 로고
    • The cld mutation: Narrowing the critical chromosomal region and selecting candidate genes
    • Peterfy M, Mao HZ, Doolittle MH: The cld mutation: narrowing the critical chromosomal region and selecting candidate genes. Mamm. Genome 17, 1013-1024 (2006).
    • (2006) Mamm. Genome , vol.17 , pp. 1013-1024
    • Peterfy, M.1    Mao, H.Z.2    Doolittle, M.H.3
  • 103
    • 70449116131 scopus 로고    scopus 로고
    • Novel LMF1 nonsense mutation in a patient with severe hypertriglyceridemia
    • Cefalu AB, Noto D, Arpi ML et al.: Novel LMF1 nonsense mutation in a patient with severe hypertriglyceridemia. J. Clin. Endocrin. Metab. 94, 4584-4590 (2009).
    • (2009) J. Clin. Endocrin. Metab. , vol.94 , pp. 4584-4590
    • Cefalu, A.B.1    Noto, D.2    Arpi, M.L.3
  • 104
    • 70450239546 scopus 로고    scopus 로고
    • Lipase maturation factor 1 (LMF1): Membrane topology and interaction with lipase proteins in the endoplasmic reticulum
    • Doolittle MH, Neher SB, Ben-Zeev O et al.: Lipase maturation factor 1 (LMF1): Membrane topology and interaction with lipase proteins in the endoplasmic reticulum. J. Biol. Chem. 284, 33623-33633 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 33623-33633
    • Doolittle, M.H.1    Neher, S.B.2    Ben-Zeev, O.3
  • 105
    • 0030925920 scopus 로고    scopus 로고
    • Pfam: A comprehensive database of protein domain families based on seed alignments
    • Sonnhammer EL, Eddy SR, Durbin R: Pfam: a comprehensive database of protein domain families based on seed alignments. Proteins 28, 405-420 (1997).
    • (1997) Proteins , vol.28 , pp. 405-420
    • Sonnhammer, E.L.1    Eddy, S.R.2    Durbin, R.3
  • 106
    • 1342334746 scopus 로고    scopus 로고
    • Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control
    • Molinari M, Eriksson KK, Calanca V et al.: Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control. Mol. Cell 13, 125-135 (2004).
    • (2004) Mol. Cell , vol.13 , pp. 125-135
    • Molinari, M.1    Eriksson, K.K.2    Calanca, V.3
  • 107
    • 0034646876 scopus 로고    scopus 로고
    • Chaperone selection during glycoprotein translocation into the endoplasmic reticulum
    • DOI 10.1126/science.288.5464.331
    • Molinari M, Helenius A: Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. Science 288, 331-333 (2000). (Pubitemid 30226193)
    • (2000) Science , vol.288 , Issue.5464 , pp. 331-333
    • Molinari, M.1    Helenius, A.2
  • 108
    • 9644302478 scopus 로고    scopus 로고
    • Rapid subunit exchange in dimeric lipoprotein lipase and properties of the inactive monomer
    • Lookene A, Zhang L, Hultin M, Olivecrona G: Rapid subunit exchange in dimeric lipoprotein lipase and properties of the inactive monomer. J. Biol. Chem. 279, 49964-49972 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 49964-49972
    • Lookene, A.1    Zhang, L.2    Hultin, M.3    Olivecrona, G.4
  • 109
    • 0141510028 scopus 로고    scopus 로고
    • 1,1́-bis(anilino)-4-,4́-bis(naphtalene)-8, 8́-disulfonate acts as an inhibitor of lipoprotein lipase and competes for binding with apolipoprotein CII
    • Lookene A, Zhang L, Tougu V, Olivecrona G: 1,1́-bis(anilino)-4-, 4́-bis(naphtalene)-8,8́-disulfonate acts as an inhibitor of lipoprotein lipase and competes for binding with apolipoprotein CII. J. Biol. Chem. 278, 37183-37194 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 37183-37194
    • Lookene, A.1    Zhang, L.2    Tougu, V.3    Olivecrona, G.4
  • 110
    • 33646806797 scopus 로고    scopus 로고
    • Mitochondria maintain maturation and secretion of lipoprotein lipase in the endoplasmic reticulum
    • Osibow K, Frank S, Malli R, Zechner R, Graier WF: Mitochondria maintain maturation and secretion of lipoprotein lipase in the endoplasmic reticulum. Biochem. J. 396, 173-182 (2006).
    • (2006) Biochem. J. , vol.396 , pp. 173-182
    • Osibow, K.1    Frank, S.2    Malli, R.3    Zechner, R.4    Graier, W.F.5
  • 111
    • 0029774156 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of denatured-reduced lysozyme: Modulation of the competition between renaturation and aggregation
    • Rozema D, Gellman SH: Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation. Biochemistry 35, 15760-15771 (1996).
    • (1996) Biochemistry , vol.35 , pp. 15760-15771
    • Rozema, D.1    Gellman, S.H.2
  • 112
    • 0033168581 scopus 로고    scopus 로고
    • Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes
    • Chevet E, Wong HN, Gerber D et al.: Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes. Embo. J. 18, 3655-3666 (1999).
    • (1999) Embo. J. , vol.18 , pp. 3655-3666
    • Chevet, E.1    Wong, H.N.2    Gerber, D.3
  • 113
    • 18944395787 scopus 로고    scopus 로고
    • Minor folding defects trigger local modification of glycoproteins by the ER folding sensor GT
    • Ritter C, Quirin K, Kowarik M, Helenius A: Minor folding defects trigger local modification of glycoproteins by the ER folding sensor GT. Embo. J. 24, 1730-1738 (2005).
    • (2005) Embo. J. , vol.24 , pp. 1730-1738
    • Ritter, C.1    Quirin, K.2    Kowarik, M.3    Helenius, A.4
  • 114
    • 0742322956 scopus 로고    scopus 로고
    • The ER protein folding sensor UDP-glucose glycoprotein glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation
    • Taylor SC, Ferguson AD, Bergeron JJ, Thomas DY: The ER protein folding sensor UDP-glucose glycoprotein glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation. Nat. Struct. Mol. Biol. 11, 128-134 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 128-134
    • Taylor, S.C.1    Ferguson, A.D.2    Bergeron, J.J.3    Thomas, D.Y.4


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