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Volumn 44, Issue 5, 2003, Pages 978-985

Blocking microsomal triglyceride transfer protein interferes with apoB secretion without causing retention or stress in the ER

Author keywords

Apolipoprotein B; Endoplasmic reticulum; Hyperlipidemia; Inflammation; Liver; Unfolded protein response

Indexed keywords

APOLIPOPROTEIN B; CHAPERONE; CHOLESTEROL; GLUCOSE REGULATED PROTEIN; GLUCOSE REGULATED PROTEIN 78; GLUCOSE REGULATED PROTEIN 94; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; ISOPROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR; MICROSOMAL TRIGLYCERIDE TRANSFER PROTEIN; PROTEIN DISULFIDE ISOMERASE; PROTEIN INHIBITOR; TRIACYLGLYCEROL; UNCLASSIFIED DRUG;

EID: 0142042348     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: 10.1194/jlr.M300020-JLR200     Document Type: Article
Times cited : (96)

References (56)
  • 1
    • 0037031061 scopus 로고    scopus 로고
    • MRC/BHF Heart Protection Study of cholesterol lowering with simvastatin in 20,536 high-risk individuals: A randomised placebo-controlled trial
    • MRC/BHF Heart Protection Study Group. 2002. MRC/BHF Heart Protection Study of cholesterol lowering with simvastatin in 20,536 high-risk individuals: a randomised placebo-controlled trial. Lancet. 360: 7-22.
    • (2002) Lancet , vol.360 , pp. 7-22
  • 2
    • 0015466387 scopus 로고
    • Abetalipoproteinemia
    • Kayden, H. J. 1972. Abetalipoproteinemia. Annu. Rev. Med. 23: 285-296.
    • (1972) Annu. Rev. Med. , vol.23 , pp. 285-296
    • Kayden, H.J.1
  • 3
    • 0023027983 scopus 로고
    • Clinical, nutritional and biochemical consequences of apolipoprotein B deficiency
    • Kayden, H. J., and M. G. Traber. 1986. Clinical, nutritional and biochemical consequences of apolipoprotein B deficiency. Adv. Exp. Med. Biol. 201: 67-81.
    • (1986) Adv. Exp. Med. Biol. , vol.201 , pp. 67-81
    • Kayden, H.J.1    Traber, M.G.2
  • 5
    • 0028330133 scopus 로고
    • The molecular basis of abetalipoproteineimia
    • Gregg, R. E., and J. R. Wetterau. 1994. The molecular basis of abetalipoproteineimia. Curr. Opin. Lipidol. 5: 81-86.
    • (1994) Curr. Opin. Lipidol. , vol.5 , pp. 81-86
    • Gregg, R.E.1    Wetterau, J.R.2
  • 6
    • 0021995612 scopus 로고
    • Purification and characterization of microsomal triglyceride and cholesteryl ester transfer protein from bovine liver microsomes
    • Wetterau, J. R., and D. B. Zilversmit. 1985. Purification and characterization of microsomal triglyceride and cholesteryl ester transfer protein from bovine liver microsomes. Chem. Phys. Lipids. 38: 205-222.
    • (1985) Chem. Phys. Lipids , vol.38 , pp. 205-222
    • Wetterau, J.R.1    Zilversmit, D.B.2
  • 7
    • 0025329901 scopus 로고
    • Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex
    • Wetterau, J. R., K. A. Combs, S. N. Spinner, and B. J. Joiner. 1990. Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J. Biol. Chem. 265: 9801-9807.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9801-9807
    • Wetterau, J.R.1    Combs, K.A.2    Spinner, S.N.3    Joiner, B.J.4
  • 8
    • 0022752718 scopus 로고
    • Vitamin E deficiency in neuropathy of abetalipoproteinemia
    • Iannaccone, S. T., and R. J. Sokol. 1986. Vitamin E deficiency in neuropathy of abetalipoproteinemia. Neurology. 36: 1009.
    • (1986) Neurology , vol.36 , pp. 1009
    • Iannaccone, S.T.1    Sokol, R.J.2
  • 10
    • 0034712665 scopus 로고    scopus 로고
    • Decreased secretion of ApoB follows inhibition of ApoB-MTP binding by a novel antagonist
    • Bakillah, A., N. Nayak, U. Saxena, R. M. Medford, and M. M. Hussain. 2000. Decreased secretion of ApoB follows inhibition of ApoB-MTP binding by a novel antagonist. Biochemistry. 39: 4892-4899.
    • (2000) Biochemistry , vol.39 , pp. 4892-4899
    • Bakillah, A.1    Nayak, N.2    Saxena, U.3    Medford, R.M.4    Hussain, M.M.5
  • 12
    • 0036653640 scopus 로고    scopus 로고
    • Microsomal triglyceride transfer protein (MTP) inhibitors: Discovery of clinically active inhibitors using high-throughput screening and parallel synthesis paradigms
    • Chang, G., R. B. Ruggeri, and H. J. Harwood, Jr. 2002. Microsomal triglyceride transfer protein (MTP) inhibitors: discovery of clinically active inhibitors using high-throughput screening and parallel synthesis paradigms. Curr. Opin. Drug Discov. Devel. 5: 562-570.
    • (2002) Curr. Opin. Drug Discov. Devel. , vol.5 , pp. 562-570
    • Chang, G.1    Ruggeri, R.B.2    Harwood H.J., Jr.3
  • 14
    • 0023772380 scopus 로고
    • Lovastatin therapy in receptor-negative homozygous familial hypercholesterolemia: Lack of effect on low-density lipoprotein concentrations or turnover
    • Uauy, R., G. L. Vega, S. M. Grundy, and D. M. Bilheimer. 1988. Lovastatin therapy in receptor-negative homozygous familial hypercholesterolemia: lack of effect on low-density lipoprotein concentrations or turnover. J. Pediatr. 113: 387-392.
    • (1988) J. Pediatr. , vol.113 , pp. 387-392
    • Uauy, R.1    Vega, G.L.2    Grundy, S.M.3    Bilheimer, D.M.4
  • 15
    • 0021717457 scopus 로고
    • Liver transplantation to provide low-density-lipoprotein receptors and lower plasma cholesterol in a child with homozygous familial hypercholesterolemia
    • Bilheimer, D. W., J. L. Goldstein, S. M. Grundy, T. E. Starzl, and M. S. Brown. 1984. Liver transplantation to provide low-density-lipoprotein receptors and lower plasma cholesterol in a child with homozygous familial hypercholesterolemia. N. Engl. J. Med. 311: 1658-1664.
    • (1984) N. Engl. J. Med. , vol.311 , pp. 1658-1664
    • Bilheimer, D.W.1    Goldstein, J.L.2    Grundy, S.M.3    Starzl, T.E.4    Brown, M.S.5
  • 16
    • 0030725291 scopus 로고    scopus 로고
    • Intracellular degradation of newly synthesized apolipoprotein B
    • Yao, Z., K. Tran, and R. S. McLeod. 1997. Intracellular degradation of newly synthesized apolipoprotein B. J. Lipid Res. 38: 1937-1953.
    • (1997) J. Lipid Res. , vol.38 , pp. 1937-1953
    • Yao, Z.1    Tran, K.2    McLeod, R.S.3
  • 17
    • 0032865070 scopus 로고    scopus 로고
    • Cell and molecular biology of the assembly and secretion of apolipoprotein B-containing lipoproteins by the liver
    • Davis, R. A. 1999. Cell and molecular biology of the assembly and secretion of apolipoprotein B-containing lipoproteins by the liver. Biochim. Biophys. Acta. 1440: 1-31.
    • (1999) Biochim. Biophys. Acta , vol.1440 , pp. 1-31
    • Davis, R.A.1
  • 18
    • 0032861798 scopus 로고    scopus 로고
    • The assembly and secretion of apolipoprotein B-containing lipoproteins
    • Olofsson, S. O., L. Asp, and J. Boren. 1999. The assembly and secretion of apolipoprotein B-containing lipoproteins. Curr. Opin. Lipidol. 10: 341-346.
    • (1999) Curr. Opin. Lipidol. , vol.10 , pp. 341-346
    • Olofsson, S.O.1    Asp, L.2    Boren, J.3
  • 19
    • 0033827087 scopus 로고    scopus 로고
    • Apolipoprotein B: mRNA editing, lipoprotein assembly, and presecretory degradation
    • Davidson, N. O., and G. S. Shelness. 2000. Apolipoprotein B: mRNA editing, lipoprotein assembly, and presecretory degradation. Annu. Rev. Nutr. 20: 169-193.
    • (2000) Annu. Rev. Nutr. , vol.20 , pp. 169-193
    • Davidson, N.O.1    Shelness, G.S.2
  • 20
    • 0037124084 scopus 로고    scopus 로고
    • Complexity in the secretory pathway: The assembly and secretion of apolipoprotein B-containing lipoproteins
    • Fisher, E. A., and H. N. Ginsberg. 2002. Complexity in the secretory pathway: the assembly and secretion of apolipoprotein B-containing lipoproteins. J. Biol. Chem. 277: 17377-17380.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17377-17380
    • Fisher, E.A.1    Ginsberg, H.N.2
  • 21
    • 0028170409 scopus 로고
    • Proteolysis-coupled secretion of the N-terminus of apolipoprotein B: Characterization of a transient, translocation arrested intermediate
    • Du, E., J. Kurth, S-L. Wang, P. Humiston, and R. A. Davis. 1994. Proteolysis-coupled secretion of the N-terminus of apolipoprotein B: characterization of a transient, translocation arrested intermediate. J. Biol. Chem. 269: 24169-24176.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24169-24176
    • Du, E.1    Kurth, J.2    Wang, S.-L.3    Humiston, P.4    Davis, R.A.5
  • 23
    • 0033525712 scopus 로고    scopus 로고
    • Liver-specific inactivation of the abetalipoproteinemia gene completely abrogates very low density lipoprotein/low density lipoprotein production in a viable conditional knockout mouse
    • Chang, B. H., W. Liao, L. Li, M. Nakamuta, D. Mack, and L. Chan. 1999. Liver-specific inactivation of the abetalipoproteinemia gene completely abrogates very low density lipoprotein/low density lipoprotein production in a viable conditional knockout mouse. J. Biol. Chem. 274: 6051-6055.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6051-6055
    • Chang, B.H.1    Liao, W.2    Li, L.3    Nakamuta, M.4    Mack, D.5    Chan, L.6
  • 24
    • 0029904269 scopus 로고    scopus 로고
    • Translocation of apolipoprotein B across the endoplasmic reticulum is blocked in abetalipoproteinemia
    • Du, E. Z., S-L. Wang, H. J. Kayden, R. Sokol, L. K. Curtiss, and R. A. Davis. 1996. Translocation of apolipoprotein B across the endoplasmic reticulum is blocked in abetalipoproteinemia. J. Lipid Res. 37: 1309-1315.
    • (1996) J. Lipid Res. , vol.37 , pp. 1309-1315
    • Du, E.Z.1    Wang, S.-L.2    Kayden, H.J.3    Sokol, R.4    Curtiss, L.K.5    Davis, R.A.6
  • 25
    • 0030800343 scopus 로고    scopus 로고
    • Co-translational degradation of apolipoprotein B100 by the proteasome is prevented by microsomal triglyceride transfer protein. Synchronized translation studies on HepG2 cells treated with an inhibitor of microsomal triglyceride transfer protein
    • Benoist, F., and P. T. Grand. 1997. Co-translational degradation of apolipoprotein B100 by the proteasome is prevented by microsomal triglyceride transfer protein. Synchronized translation studies on HepG2 cells treated with an inhibitor of microsomal triglyceride transfer protein. J. Biol. Chem. 272: 20435-20442.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20435-20442
    • Benoist, F.1    Grand, P.T.2
  • 26
    • 0030783252 scopus 로고    scopus 로고
    • The enzymatic and non-enzymatic roles of protein-disulfide isomerase in apolipoprotein B secretion
    • Wang, L., D. G. Fast, and A. D. Attie. 1997. The enzymatic and non-enzymatic roles of protein-disulfide isomerase in apolipoprotein B secretion. J. Biol. Chem. 272: 27644-27651.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27644-27651
    • Wang, L.1    Fast, D.G.2    Attie, A.D.3
  • 27
    • 0030660157 scopus 로고    scopus 로고
    • Apolipoprotein B binding to microsomal triglyceride transfer protein decreases with increases in length and lipidation: Implications in lipoprotein biosynthesis
    • Hussain, M. M., A. Bakillah, and H. Jamil. 1997. Apolipoprotein B binding to microsomal triglyceride transfer protein decreases with increases in length and lipidation: implications in lipoprotein biosynthesis. Biochemistry. 36: 13060-13067.
    • (1997) Biochemistry , vol.36 , pp. 13060-13067
    • Hussain, M.M.1    Bakillah, A.2    Jamil, H.3
  • 28
    • 0032567356 scopus 로고    scopus 로고
    • Translocation efficiency, susceptibility to proteasomal degradation, and lipid responsiveness of apolipoprotein B are determined by the presence of beta sheet domains
    • Liang, J. S., X. Wu, H. Jiang, M. Zhou, H. Yang, P. Angkeow, L. S. Huang, S. L. Sturley, and H. Ginsberg. 1998. Translocation efficiency, susceptibility to proteasomal degradation, and lipid responsiveness of apolipoprotein B are determined by the presence of beta sheet domains. J. Biol. Chem. 273: 35216-35221.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35216-35221
    • Liang, J.S.1    Wu, X.2    Jiang, H.3    Zhou, M.4    Yang, H.5    Angkeow, P.6    Huang, L.S.7    Sturley, S.L.8    Ginsberg, H.9
  • 29
    • 0032570590 scopus 로고    scopus 로고
    • The microsomal triglyceride transfer protein catalyzes the post-translational assembly of apolipoprotein B-100 very low density lipoprotein in McA-RH7777 cells
    • Rustaeus, S., P. Stillemark, K. Lindberg, D. Gordon, and S. O. Olofsson. A998. The microsomal triglyceride transfer protein catalyzes the post-translational assembly of apolipoprotein B-100 very low density lipoprotein in McA-RH7777 cells. J. Biol. Chem. 273: 5196-5203.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5196-5203
    • Rustaeus, S.1    Stillemark, P.2    Lindberg, K.3    Gordon, D.4    Olofsson, S.O.5
  • 30
    • 0032410930 scopus 로고    scopus 로고
    • Apoprotein B100 has a prolonged interaction with the translocon during which its lipidation and translocation change from dependence on the microsomal triglyceride transfer protein to independence
    • Mitchell, D. M., M. Zhou, R. Pariyarath, H. Wang, J. D. Aitchison, H. N. Ginsberg, and E. A. Fisher. 1998. Apoprotein B100 has a prolonged interaction with the translocon during which its lipidation and translocation change from dependence on the microsomal triglyceride transfer protein to independence. Proc. Natl. Acad. Sci. USA. 95: 14733-14738.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14733-14738
    • Mitchell, D.M.1    Zhou, M.2    Pariyarath, R.3    Wang, H.4    Aitchison, J.D.5    Ginsberg, H.N.6    Fisher, E.A.7
  • 31
    • 0033593209 scopus 로고    scopus 로고
    • Identification of domains in apolipoprotein B100 that confer a high requirement for the microsomal triglyceride transfer-protein
    • Nicodeme, E., F. Benoist, R. McLeod, Z. Yao, J. Scott, C. C. Shoulders, and P. T. Grand. 1999. Identification of domains in apolipoprotein B100 that confer a high requirement for the microsomal triglyceride transfer-protein. J. Biol. Chem. 274: 1986-1993.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1986-1993
    • Nicodeme, E.1    Benoist, F.2    McLeod, R.3    Yao, Z.4    Scott, J.5    Shoulders, C.C.6    Grand, P.T.7
  • 32
    • 0037199962 scopus 로고    scopus 로고
    • Microsomal triacylglycerol transfer protein is required for lumenal accretion of triacylglycerol not associated with ApoB, as well as for ApoB lipidation
    • Kulinski, A., S. Rustaeus, and J. E. Vance. 2002. Microsomal triacylglycerol transfer protein is required for lumenal accretion of triacylglycerol not associated with ApoB, as well as for ApoB lipidation. J. Biol. Chem. 277: 31516-31525.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31516-31525
    • Kulinski, A.1    Rustaeus, S.2    Vance, J.E.3
  • 33
    • 0025347436 scopus 로고
    • Apolipoprotein B is both integrated into and translocated across the endoplasmic reticulum membrane. Evidence for two functionally distinct pools
    • Davis, R. A., R. N. Thrift, C. C. Wu, and K. E. Howell. 1990. Apolipoprotein B is both integrated into and translocated across the endoplasmic reticulum membrane. Evidence for two functionally distinct pools. J. Biol. Chem. 265: 10005-10011.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10005-10011
    • Davis, R.A.1    Thrift, R.N.2    Wu, C.C.3    Howell, K.E.4
  • 34
    • 10244270656 scopus 로고    scopus 로고
    • Ubiquitin-proteasome pathway mediates intracellular degradation of apolipoprotein B
    • Yeung, S. J., S. H. Chen, and L. Chan. 1996. Ubiquitin-proteasome pathway mediates intracellular degradation of apolipoprotein B. Biochemistry. 35: 13843-13848.
    • (1996) Biochemistry , vol.35 , pp. 13843-13848
    • Yeung, S.J.1    Chen, S.H.2    Chan, L.3
  • 35
    • 0030860899 scopus 로고    scopus 로고
    • The degradation of apolipoprotein B100 is mediated by the ubiquitin-proteasome pathway and involves heat shock protein 70
    • Fisher, E. A., M. Zhou, D. M. Mitchell, X. Wu, S. Omura, H. Wang, A. L. Goldberg, and H. N. Ginsberg. 1997. The degradation of apolipoprotein B100 is mediated by the ubiquitin-proteasome pathway and involves heat shock protein 70. J. Biol. Chem. 272: 20427-20434.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20427-20434
    • Fisher, E.A.1    Zhou, M.2    Mitchell, D.M.3    Wu, X.4    Omura, S.5    Wang, H.6    Goldberg, A.L.7    Ginsberg, H.N.8
  • 36
    • 0034644688 scopus 로고    scopus 로고
    • The amino-terminal domain of apolipoprotein B does not undergo retrograde translocation from the endoplasmic reticulum to the cytosol. Proteasomal degradation of nascent apolipoprotein b begins at the carboxyl terminus of the protein, while apolipoprotein b is still in its original translocon
    • Liang, J., X. Wu, E. A. Fisher, and H. N. Ginsberg. 2000. The amino-terminal domain of apolipoprotein B does not undergo retrograde translocation from the endoplasmic reticulum to the cytosol. Proteasomal degradation of nascent apolipoprotein b begins at the carboxyl terminus of the protein, while apolipoprotein b is still in its original translocon. J. Biol. Chem. 275: 32003-32010.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32003-32010
    • Liang, J.1    Wu, X.2    Fisher, E.A.3    Ginsberg, H.N.4
  • 37
    • 0028811670 scopus 로고
    • In HepG2 cells, translocation, not degradation, determines the fate of de novo synthesized apolipoprotein B
    • Bonnardel, J. A., and R. A. Davis. 1995. In HepG2 cells, translocation, not degradation, determines the fate of de novo synthesized apolipoprotein B. J. Biol. Chem. 270: 28892-28896.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28892-28896
    • Bonnardel, J.A.1    Davis, R.A.2
  • 38
    • 0034644111 scopus 로고    scopus 로고
    • ER stress response: Getting the UPR hand on misfolded proteins
    • Hampton, R. Y. 2000. ER stress response: getting the UPR hand on misfolded proteins. Curr. Biol. 10: R518-R521.
    • (2000) Curr. Biol. , vol.10
    • Hampton, R.Y.1
  • 39
    • 0033693855 scopus 로고    scopus 로고
    • IRE1 and efferent signaling from the endoplasmic reticulum
    • Urano, F., A. Bertolotti, and D. Ron. 2000. IRE1 and efferent signaling from the endoplasmic reticulum. J. Cell Sci. 113: 3697-3702.
    • (2000) J. Cell Sci. , vol.113 , pp. 3697-3702
    • Urano, F.1    Bertolotti, A.2    Ron, D.3
  • 40
    • 0035370949 scopus 로고    scopus 로고
    • Intracellular signaling from the endoplasmic reticulum to the nucleus: The unfolded protein response in yeast and mammals
    • Patil, C., and P. Walter. 2001. Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr. Opin. Cell Biol. 13: 349-355.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 349-355
    • Patil, C.1    Walter, P.2
  • 43
    • 0026702590 scopus 로고
    • Translocation of apolipoprotein B across the endoplasmic reticulum is blocked in a nonhepatic cell line
    • Thrift, R. N., J. Drisko, S. Dueland, J. D. Trawick, and R. A. Davis. 1992. Translocation of apolipoprotein B across the endoplasmic reticulum is blocked in a nonhepatic cell line. Proc. Natl. Acad. Sci. USA. 89: 9161-9165.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9161-9165
    • Thrift, R.N.1    Drisko, J.2    Dueland, S.3    Trawick, J.D.4    Davis, R.A.5
  • 44
    • 0033556026 scopus 로고    scopus 로고
    • Translocation-arrested apolipoprotein B evades proteasome degradation via a sterol-sensitive block in ubiquitin conjugation
    • Du, E. Z., J. F. Fleming, S-L. Wang, G. M. Spitzen, and R. A. Davis. 1999. Translocation-arrested apolipoprotein B evades proteasome degradation via a sterol-sensitive block in ubiquitin conjugation. J. Biol. Chem. 274: 1856-1862.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1856-1862
    • Du, E.Z.1    Fleming, J.F.2    Wang, S.-L.3    Spitzen, G.M.4    Davis, R.A.5
  • 45
    • 0029975626 scopus 로고    scopus 로고
    • The microsomal triglyceride transfer protein facilitates assembly and secretion of apolipoprotein B-containing lipoproteins and decreases cotranslational degradation of apolipoprotein B in transfected COS-7 cells
    • Wang, S., R. S. McLeod, D. A. Gordon, and Z. Yao. 1996. The microsomal triglyceride transfer protein facilitates assembly and secretion of apolipoprotein B-containing lipoproteins and decreases cotranslational degradation of apolipoprotein B in transfected COS-7 cells. J. Biol. Chem. 271: 12124-12133.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12124-12133
    • Wang, S.1    McLeod, R.S.2    Gordon, D.A.3    Yao, Z.4
  • 46
    • 0032538638 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of apolipoprotein B targets both nascent peptides cotranslationally before translocation and full-length apolipoprotein B after translocation into the endoplasmic reticulum
    • Liao, W., S. Yeung, and L. Chan. 1998. Proteasome-mediated degradation of apolipoprotein B targets both nascent peptides cotranslationally before translocation and full-length apolipoprotein B after translocation into the endoplasmic reticulum. J. Biol. Chem. 273: 27225-27230.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27225-27230
    • Liao, W.1    Yeung, S.2    Chan, L.3
  • 47
    • 0035808302 scopus 로고    scopus 로고
    • Co-translational interactions of apoprotein B with the ribosome and translocon during lipoprotein assembly or targeting to the proteasome
    • Pariyarath, R., H. Wang, J. D. Aitchison, H. N. Ginsberg, W. J. Welch, A. E. Johnson, and E. A. Fisher. 2001. Co-translational interactions of apoprotein B with the ribosome and translocon during lipoprotein assembly or targeting to the proteasome. J. Biol. Chem. 276: 541-550.
    • (2001) J. Biol. Chem. , vol.276 , pp. 541-550
    • Pariyarath, R.1    Wang, H.2    Aitchison, J.D.3    Ginsberg, H.N.4    Welch, W.J.5    Johnson, A.E.6    Fisher, E.A.7
  • 48
    • 0037085471 scopus 로고    scopus 로고
    • Blocking the secretion of hepatic very low density lipoproteins renders the liver more susceptible to toxin-induced injury
    • Bjorkegren, J., A. Beigneux, M. O. Bergo, J. J. Maher, and S. G. Young. 2002. Blocking the secretion of hepatic very low density lipoproteins renders the liver more susceptible to toxin-induced injury. J. Biol. Chem. 277: 5476-5483.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5476-5483
    • Bjorkegren, J.1    Beigneux, A.2    Bergo, M.O.3    Maher, J.J.4    Young, S.G.5
  • 50
    • 0037007109 scopus 로고    scopus 로고
    • Endoplasmic reticulum localization of the low density lipoprotein receptor mediates presecretory degradation of apolipoprotein B
    • Gillian-Daniel, D. L., P. W. Bates, A. Tebon, and A. D. Attie. 2002. Endoplasmic reticulum localization of the low density lipoprotein receptor mediates presecretory degradation of apolipoprotein B. Proc. Natl. Acad. Sci. USA. 99: 4337-4342.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4337-4342
    • Gillian-Daniel, D.L.1    Bates, P.W.2    Tebon, A.3    Attie, A.D.4
  • 51
    • 0020724143 scopus 로고
    • Recycling receptors: The round-trip itinerary of migrant membrane proteins
    • Brown, M. S., R. G. Anderson, and J. L. Goldstein. 1983. Recycling receptors: the round-trip itinerary of migrant membrane proteins. Cell. 32: 663-667.
    • (1983) Cell , vol.32 , pp. 663-667
    • Brown, M.S.1    Anderson, R.G.2    Goldstein, J.L.3
  • 56
    • 0019977738 scopus 로고
    • Pathology of chronic vitamin E deficiency in fatal familial intrahepatic cholestasis (Byler disease)
    • Saito, K. S. Matsumoto, T. Yokoyama, M. Okaniwa, and S. Kamoshita. 1982. Pathology of chronic vitamin E deficiency in fatal familial intrahepatic cholestasis (Byler disease). Virchows Arch. 396: 319-330.
    • (1982) Virchows Arch. , vol.396 , pp. 319-330
    • Saito, K.1    Matsumoto, S.2    Yokoyama, T.3    Okaniwa, M.4    Kamoshita, S.5


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