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Volumn 153, Issue 1, 2012, Pages 426-437

Ubiquitin-proteasomal degradation of COX-2 in TGF-β stimulated human endometrial cells is mediated through endoplasmic reticulum mannosidase I

Author keywords

[No Author keywords available]

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CYCLOOXYGENASE 2; ENDOPLASMIC RETICULUM MANNOSIDASE 1; MANNOSIDASE; PROSTAGLANDIN; PROTEASOME; SMAD2 PROTEIN; SMAD3 PROTEIN; TRANSFORMING GROWTH FACTOR BETA; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84455185071     PISSN: 00137227     EISSN: 19457170     Source Type: Journal    
DOI: 10.1210/en.2011-1438     Document Type: Article
Times cited : (14)

References (53)
  • 1
    • 0033590207 scopus 로고    scopus 로고
    • The role of cyclooxygenases in inflammation, cancer, and development
    • Williams CS, Mann M, DuBois RN 1999 The role of cyclooxygenases in inflammation, cancer, and development. Oncogene 18: 7908-7916. (Pubitemid 30066236)
    • (1999) Oncogene , vol.18 , Issue.55 , pp. 7908-7916
    • Williams, C.S.1    Mann, M.2    DuBois, R.N.3
  • 2
    • 0033791318 scopus 로고    scopus 로고
    • Cyclooxygenases: Structural, cellular, and molecular biology
    • Smith WL, DeWitt DL, Garavito RM 2000 Cyclooxygenases: structural, cellular, and molecular biology. Annu Rev Biochem 69:145-182
    • (2000) Annu Rev Biochem , vol.69 , pp. 145-182
    • Smith, W.L.1    DeWitt, D.L.2    Garavito, R.M.3
  • 3
    • 0032701224 scopus 로고    scopus 로고
    • The cyclooxygenase isoforms: Structural insights into the conversion of arachidonic acid to prostaglandins
    • DOI 10.1016/S1388-1981(99)00147-X, PII S138819819900147X
    • Garavito RM, DeWitt DL 1999 The cyclooxygenase isoforms: structural insights into the conversion of arachidonic acid to prostaglandins. Biochim Biophys Acta 1441:278-287 (Pubitemid 29537747)
    • (1999) Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids , vol.1441 , Issue.2-3 , pp. 278-287
    • Garavito, R.M.1    Dewitt, D.L.2
  • 4
    • 0037898985 scopus 로고    scopus 로고
    • Mechanism of free radical oxygenation of polyunsaturated fatty acids by cyclooxygenases
    • Rouzer CA, Marnett LJ 2003 Mechanism of free radical oxygenation of polyunsaturated fatty acids by cyclooxygenases. Chem Rev 103:2239-2304
    • (2003) Chem Rev , vol.103 , pp. 2239-2304
    • Rouzer, C.A.1    Marnett, L.J.2
  • 5
    • 0036669611 scopus 로고    scopus 로고
    • Cyclooxygenase isozymes and their gene structures and expression
    • DOI 10.1016/S0090-6980(02)00024-2, PII S0090698002000242
    • Tanabe T, Tohnai N 2002 Cyclooxygenase isozymes and their gene structures and expression. Prostaglandins Other Lipid Mediat 68-69:95-114 (Pubitemid 35247390)
    • (2002) Prostaglandins and Other Lipid Mediators , vol.68-69 , pp. 95-114
    • Tanabe, T.1    Tohnai, N.2
  • 6
    • 11144238299 scopus 로고    scopus 로고
    • Control of cyclooxygenase-2 transcriptional activation by pro-inflammatory mediators
    • DOI 10.1016/j.plefa.2004.11.001, PII S0952327804001863
    • Wu KK 2005 Control of cyclooxygenase-2 transcriptional activation by pro-inflammatory mediators. Prostaglandins Leukot Essent Fatty Acids 72:89-93 (Pubitemid 40051225)
    • (2005) Prostaglandins Leukotrienes and Essential Fatty Acids , vol.72 , Issue.2 SPEC. ISS. , pp. 89-93
    • Wu, K.K.1
  • 8
    • 33845991203 scopus 로고    scopus 로고
    • The 19-amino acid cassette of cyclooxygenase-2 mediates entry of the protein into the endoplasmic reticulum-associated degradation system
    • DOI 10.1074/jbc.M608281200
    • Mbonye UR, Wada M, Rieke CJ, Tang HY, Dewitt DL, Smith WL 2006 The 19-amino acid cassette of cyclooxygenase-2 mediates entry of the protein into the endoplasmic reticulum-associated degradation system. J Biol Chem 281:35770-35778 (Pubitemid 46041308)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.47 , pp. 35770-35778
    • Mbonye, U.R.1    Wada, M.2    Rieke, C.J.3    Tang, H.-Y.4    DeWitt, D.L.5    Smith, W.L.6
  • 9
    • 34548030442 scopus 로고    scopus 로고
    • The ubiquitin- and proteasome-dependent degradation of COX-2 is regulated by the COP9 signalosome and differentially influenced by coxibs
    • DOI 10.1007/s00109-007-0197-y
    • Neuss H, Huang X, Hetfeld BK, Deva R, Henklein P, Nigam S, Mall JW, Schwenk W, Dubiel W 2007 The ubiquitin- and proteasome-dependent degradation of COX-2 is regulated by the COP9 signalosome and differentially influenced by coxibs. J Mol Med 85:961-970 (Pubitemid 47282790)
    • (2007) Journal of Molecular Medicine , vol.85 , Issue.9 , pp. 961-970
    • Neuss, H.1    Huang, X.2    Hetfeld, B.K.J.3    Deva, R.4    Henklein, P.5    Nigam, S.6    Mall, J.W.7    Schwenk, W.8    Dubiel, W.9
  • 10
    • 0033168382 scopus 로고    scopus 로고
    • Retrograde protein translocation: ERADication of secretory proteins in health and disease
    • DOI 10.1016/S0968-0004(99)01420-6, PII S0968000499014206
    • Plemper RK, Wolf DH 1999 Retrograde protein translocation: ERADication of secretory proteins in health and disease. Trends Biochem Sci 24:266-270 (Pubitemid 29301690)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.7 , pp. 266-270
    • Plemper, R.K.1    Wolf, D.H.2
  • 11
    • 0032441479 scopus 로고    scopus 로고
    • Ubiquitin and the control of protein fate in the secretory and endocytic pathway
    • DOI 10.1146/annurev.cellbio.14.1.19
    • Bonifacino JS, Weissman AM 1998 Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu Rev Cell Dev Biol 14:19-57 (Pubitemid 29001448)
    • (1998) Annual Review of Cell and Developmental Biology , vol.14 , pp. 19-57
    • Bonifacino, J.S.1    Weissman, A.M.2
  • 12
    • 63649161943 scopus 로고    scopus 로고
    • The ubiquitylation machinery of the endoplasmic reticulum
    • Hirsch C, Gauss R, Horn SC, Neuber O, Sommer T 2009 The ubiquitylation machinery of the endoplasmic reticulum. Nature 458:453-460
    • (2009) Nature , vol.458 , pp. 453-460
    • Hirsch, C.1    Gauss, R.2    Horn, S.C.3    Neuber, O.4    Sommer, T.5
  • 13
    • 0032494135 scopus 로고    scopus 로고
    • Degradation of misfolded endoplasmic reticulum glycoproteins in saccharomyces cerevisiae is determined by a specific oligosaccharide structure
    • DOI 10.1083/jcb.142.5.1223
    • Jakob CA, Burda P, Roth J, Aebi M 1998 Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J Cell Biol 142:1223-1233 (Pubitemid 28429104)
    • (1998) Journal of Cell Biology , vol.142 , Issue.5 , pp. 1223-1233
    • Jakob, C.A.1    Burda, P.2    Roth, J.3    Aebi, M.4
  • 14
    • 0033605219 scopus 로고    scopus 로고
    • Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome
    • DOI 10.1074/jbc.274.9.5861
    • Liu Y, Choudhury P, Cabral CM, Sifers RN 1999 Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. J Biol Chem 274:5861-5867 (Pubitemid 29109243)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.9 , pp. 5861-5867
    • Liu, Y.1    Choudhury, P.2    Cabral, C.M.3    Sifers, R.N.4
  • 15
    • 9644300910 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated protein degradation - One model fits all?
    • DOI 10.1016/j.bbamcr.2004.10.006, PII S0167488904002575, The Ubiquitin-Proteasome System
    • Hirsch C, Jarosch E, Sommer T, Wolf DH 2004 Endoplasmic reticulum-associated protein degradation-one model fits all? Biochim Biophys Acta 1695:215-223 (Pubitemid 39574975)
    • (2004) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1695 , Issue.1-3 , pp. 215-223
    • Hirsch, C.1    Jarosch, E.2    Sommer, T.3    Wolf, D.H.4
  • 17
    • 70449706453 scopus 로고    scopus 로고
    • Posttranscriptional and posttranslational determinants of cyclooxygenase expression
    • Mbonye UR, Song I 2009 Posttranscriptional and posttranslational determinants of cyclooxygenase expression. BMB Rep 42:552-560
    • (2009) BMB Rep , vol.42 , pp. 552-560
    • Mbonye, U.R.1    Song, I.2
  • 18
    • 0034534697 scopus 로고    scopus 로고
    • Induction of prostaglandin endoperoxide synthase 2 by mitogen-activated protein kinase cascades
    • DOI 10.1042/0264-6021:3520419
    • Mcginty A, Foschi M, Chang YW, Han J, Dunn MJ, Sorokin A 2000 Induction of prostaglandin endoperoxide synthase 2 by mitogen-activated protein kinase cascades. Biochem J 352(Pt 2):419-424 (Pubitemid 32011435)
    • (2000) Biochemical Journal , vol.352 , Issue.2 , pp. 419-424
    • McGinty, A.1    Foschi, M.2    Chang, Y.-W.E.3    Han, J.4    Dunn, M.J.5    Sorokin, A.6
  • 19
    • 0142104985 scopus 로고    scopus 로고
    • Smad-dependent and Smad-independent pathways in TGF-β family signalling
    • DOI 10.1038/nature02006
    • Derynck R, Zhang YE 2003 Smad-dependent and Smad-independent pathways in TGF-β family signalling. Nature 425:577-584 (Pubitemid 37280136)
    • (2003) Nature , vol.425 , Issue.6958 , pp. 577-584
    • Derynck, R.1    Zhang, Y.E.2
  • 20
    • 68549123472 scopus 로고    scopus 로고
    • New regulatory mechanisms of TGF-β receptor function
    • Kang JS, Liu C, Derynck R 2009 New regulatory mechanisms of TGF-β receptor function. Trends Cell Biol 19:385-394
    • (2009) Trends Cell Biol , vol.19 , pp. 385-394
    • Kang, J.S.1    Liu, C.2    Derynck, R.3
  • 21
    • 33747734121 scopus 로고    scopus 로고
    • TGF-β superfamily expression and actions in the endometrium and placenta
    • DOI 10.1530/rep.1.01076
    • Jones RL, Stoikos C, Findlay JK, Salamonsen LA 2006 TGF-β superfamily expression and actions in the endometrium and placenta. Reproduction 132:217-232 (Pubitemid 44269704)
    • (2006) Reproduction , vol.132 , Issue.2 , pp. 217-232
    • Jones, R.L.1    Stoikos, C.2    Findlay, J.K.3    Salamonsen, L.A.4
  • 24
    • 0028358770 scopus 로고
    • Expression of transforming growth factor-β (TGFβ) isoforms and TGF β type II receptor messenger ribonucleic acid and protein, and the effect of TGF β s on endometrial stromal cell growth and protein degradation in vitro
    • Tang XM, Zhao Y, Rossi MJ, Abu-Rustum RS, Ksander GA, Chegini N 1994 Expression of transforming growth factor-β (TGFβ) isoforms and TGF β type II receptor messenger ribonucleic acid and protein, and the effect of TGF β s on endometrial stromal cell growth and protein degradation in vitro. Endocrinology 135:450-459
    • (1994) Endocrinology , vol.135 , pp. 450-459
    • Tang, X.M.1    Zhao, Y.2    Rossi, M.J.3    Abu-Rustum, R.S.4    Ksander, G.A.5    Chegini, N.6
  • 25
    • 0029949756 scopus 로고    scopus 로고
    • Developmental expression of the cyclo-oxygenase-1 and cyclo-oxygenase-2 genes in the peri-implantation mouse uterus and their differential regulation by the blastocyst and ovarian steroids
    • Chakraborty I, Das SK, Wang J, Dey SK 1996 Developmental expression of the cyclo-oxygenase-1 and cyclo-oxygenase-2 genes in the peri-implantation mouse uterus and their differential regulation by the blastocyst and ovarian steroids. J Mol Endocrinol 16:107-122 (Pubitemid 26157010)
    • (1996) Journal of Molecular Endocrinology , vol.16 , Issue.2 , pp. 107-122
    • Chakraborty, I.1    Das, S.K.2    Wang, J.3    Dey, S.K.4
  • 26
    • 0032860902 scopus 로고    scopus 로고
    • 2 isomer B during N-glycan biosynthesis
    • DOI 10.1093/glycob/9.10.1073
    • Tremblay LO, Herscovics A 1999 Cloning and expression of a specific human α 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis. Glycobiology 9:1073-1078 (Pubitemid 29473965)
    • (1999) Glycobiology , vol.9 , Issue.10 , pp. 1073-1078
    • Tremblay, L.O.1    Herscovics, A.2
  • 27
  • 28
    • 2942517377 scopus 로고    scopus 로고
    • Akt regulates COX-2 mRNA and protein expression in mutated-PTEN human endometrial cancer cells
    • St-Germain ME, Gagnon V, Mathieu I, Parent S, Asselin E 2004 Akt regulates COX-2 mRNA and protein expression in mutated-PTEN human endometrial cancer cells. Int J Oncol 24:1311-1324
    • (2004) Int J Oncol , vol.24 , pp. 1311-1324
    • St-Germain, M.E.1    Gagnon, V.2    Mathieu, I.3    Parent, S.4    Asselin, E.5
  • 29
    • 3843129470 scopus 로고    scopus 로고
    • Negative feedback regulation of phosphatidylinositol 3-kinase/Akt pathway by over-expressed cyclooxygenase-2 in human epidermal cancer cells
    • Takeda K, Kanekura T, Kanzaki T 2004 Negative feedback regulation of phosphatidylinositol 3-kinase/Akt pathway by over-expressed cyclooxygenase-2 in human epidermal cancer cells. J Dermatol 31:516-523 (Pubitemid 39045006)
    • (2004) Journal of Dermatology , vol.31 , Issue.7 , pp. 516-523
    • Takeda, K.1    Kanekura, T.2    Kanzaki, T.3
  • 30
    • 0032479977 scopus 로고    scopus 로고
    • Differential regulation of c-Jun by ERK and JNK during PC12 cell differentiation
    • DOI 10.1093/emboj/17.15.4404
    • Leppä S, Saffrich R, Ansorge W, Bohmann D 1998 Differential regulation of c-Jun by ERK and JNK during PC12 cell differentiation. EMBO J 17:4404-4413 (Pubitemid 28362630)
    • (1998) EMBO Journal , vol.17 , Issue.15 , pp. 4404-4413
    • Leppa, S.1    Saffrich, R.2    Ansorge, W.3    Bohmann, D.4
  • 31
    • 0025788098 scopus 로고
    • Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73
    • Smeal T, Binetruy B, Mercola DA, Birrer M, Karin M 1991 Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73. Nature 354:494-496 (Pubitemid 21896867)
    • (1991) Nature , vol.354 , Issue.6353 , pp. 494-496
    • Smeal, T.1    Binetruy, B.2    Mercola, D.A.3    Birrer, M.4    Karin, M.5
  • 32
    • 38749122389 scopus 로고    scopus 로고
    • 2 in glycoprotein ER-associated degradation
    • DOI 10.1091/mbc.E07-05-0505
    • Avezov E, Frenkel Z, Ehrlich M, Herscovics A, Lederkremer GZ 2008 Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation. Mol Biol Cell 19:216-225 (Pubitemid 351186147)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.1 , pp. 216-225
    • Avezov, E.1    Frenkel, Z.2    Ehrlich, M.3    Herscovics, A.4    Lederkremer, G.Z.5
  • 33
    • 70349855203 scopus 로고    scopus 로고
    • Glycoprotein folding, quality control and ER-associated degradation
    • Lederkremer GZ 2009 Glycoprotein folding, quality control and ER-associated degradation. Curr Opin Struct Biol 19:515-523
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 515-523
    • Lederkremer, G.Z.1
  • 36
    • 0035918223 scopus 로고    scopus 로고
    • Glycoprotein quality control in the endoplasmic reticulum. Mannose trimming by endoplasmic reticulum mannosidase I times the proteasomal degradation of unassembled immunoglobulin subunits
    • Fagioli C, Sitia R 2001 Glycoprotein quality control in the endoplasmic reticulum. Mannose trimming by endoplasmic reticulum mannosidase I times the proteasomal degradation of unassembled immunoglobulin subunits. J Biol Chem 276:12885-12892
    • (2001) J Biol Chem , vol.276 , pp. 12885-12892
    • Fagioli, C.1    Sitia, R.2
  • 37
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • DOI 10.1038/35008096
    • Schubert U, Antón LC, Gibbs J, Norbury CC, Yewdell JW, Bennink JR 2000 Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404:770-774 (Pubitemid 30212405)
    • (2000) Nature , vol.404 , Issue.6779 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 39
    • 33744775013 scopus 로고    scopus 로고
    • Decidualization and maintenance of a functional prostaglandin system in human endometrial cell lines following transformation with SV40 large T antigen
    • DOI 10.1093/molehr/gal034
    • Chapdelaine P, Kang J, Boucher-Kovalik S, Caron N, Tremblay JP, Fortier MA 2006 Decidualization and maintenance of a functional prostaglandin system in human endometrial cell lines following transformation with SV40 large T antigen. Mol Hum Reprod 12: 309-319 (Pubitemid 43821794)
    • (2006) Molecular Human Reproduction , vol.12 , Issue.5 , pp. 309-319
    • Chapdelaine, P.1    Kang, J.2    Boucher-Kovalik, S.3    Caron, N.4    Tremblay, J.P.5    Fortier, M.A.6
  • 41
    • 0034489934 scopus 로고    scopus 로고
    • Posttranscriptional regulation of cyclooxygenase-2 in rat intestinal epithelial cells
    • Zhang Z, Sheng H, Shao J, Beauchamp RD, DuBois RN 2000 Post-transcriptional regulation of cyclooxygenase-2 in rat intestinal epithelial cells. Neoplasia 2:523-530 (Pubitemid 32098687)
    • (2000) Neoplasia , vol.2 , Issue.6 , pp. 523-530
    • Zhang, Z.1    Sheng, H.2    Shao, J.3    Beauchampt, R.D.4    DuBois, R.N.5
  • 42
    • 0035866755 scopus 로고    scopus 로고
    • K-Ras-mediated increase in cyclooxygenase 2 mRNA stability involves activation of the protein kinase B
    • Sheng H, Shao J, Dubois RN 2001 K-Ras-mediated increase in cyclooxygenase 2 mRNA stability involves activation of the protein kinase B1. Cancer Res 61:2670-2675 (Pubitemid 32691132)
    • (2001) Cancer Research , vol.61 , Issue.6 , pp. 2670-2675
    • Sheng, H.1    Shao, J.2    DuBois, R.N.3
  • 43
    • 0032582347 scopus 로고    scopus 로고
    • 2-terminal kinase and p38 MAPK signal pathways in rat renal mesangial cells
    • DOI 10.1074/jbc.273.44.28670
    • Guan Z, Buckman SY, Miller BW, Springer LD, Morrison AR 1998 Interleukin-1β-induced cyclooxygenase-2 expression requires activation of both c-Jun NH2-terminal kinase and p38 MAPK signal pathways in rat renal mesangial cells. J Biol Chem 273:28670-28676 (Pubitemid 28507552)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.44 , pp. 28670-28676
    • Guan, Z.1    Buckman, S.Y.2    Miller, B.W.3    Springer, L.D.4    Morrison, A.R.5
  • 44
    • 0037031854 scopus 로고    scopus 로고
    • Requirement of BMP-2-induced phosphatidylinositol 3-kinase and Akt serine/threonine kinase in osteoblast differentiation and Smad-dependent BMP-2 gene transcription
    • DOI 10.1074/jbc.M205053200
    • Ghosh-Choudhury N, Abboud SL, Nishimura R, Celeste A, Mahimainathan L, Choudhury GG 2002 Requirement of BMP-2-induced phosphatidylinositol 3-kinase and Akt serine/threonine kinase in osteoblast differentiation and Smad-dependent BMP-2 gene transcription. J Biol Chem 277:33361-33368 (Pubitemid 34984859)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 33361-33368
    • Ghosh-Choudhury, N.1    Abboud, S.L.2    Nishimura, R.3    Celeste, A.4    Mahimainathan, L.5    Choudhury, G.G.6
  • 45
    • 0032868499 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is required for growth factor-induced amino acid uptake by vascular smooth muscle cells
    • Higaki M, Shimokado K 1999 Phosphatidylinositol 3-kinase is required for growth factor-induced amino acid uptake by vascular smooth muscle cells. Arterioscler Thromb Vasc Biol 19:2127-2132 (Pubitemid 29422244)
    • (1999) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.19 , Issue.9 , pp. 2127-2132
    • Higaki, M.1    Shimokado, K.2
  • 48
    • 0033605559 scopus 로고    scopus 로고
    • MEKK-1, a component of the stress (stress-activated protein kinase/c- jun N-terminal kinase) pathway, can selectively activate Smad2-mediated transcriptional activation in endothelial cells
    • DOI 10.1074/jbc.274.13.8797
    • Brown JD, DiChiara MR, Anderson KR, Gimbrone Jr MA, Topper JN 1999 MEKK-1, a component of the stress (stress-activated protein kinase/c-Jun N-terminal kinase) pathway, can selectively activate Smad2-mediated transcriptional activation in endothelial cells. J Biol Chem 274:8797-8805 (Pubitemid 29164678)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.13 , pp. 8797-8805
    • Brown, J.D.1    DiChiara, M.R.2    Anderson, K.R.3    Gimbrone Jr., M.A.4    Topper, J.N.5
  • 50
    • 0028037571 scopus 로고
    • The orientation of prostaglandin endoperoxide synthases-1 and -2 in the endoplasmic reticulum
    • Otto JC, Smith WL 1994 The orientation of prostaglandin endoperoxide synthases-1 and -2 in the endoplasmic reticulum. J Biol Chem 269:19868-19875 (Pubitemid 24250901)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.31 , pp. 19868-19875
    • Otto, J.C.1    Smith, W.L.2
  • 51
    • 33749183647 scopus 로고    scopus 로고
    • N-linked glycan recognition and processing: The molecular basis of endoplasmic reticulum quality control
    • DOI 10.1016/j.sbi.2006.08.005, PII S0959440X06001400, Carbohydrates and Glycoconjugates / Biophysical Methods
    • Moremen KW, Molinari M 2006 N-linked glycan recognition and processing: the molecular basis of endoplasmic reticulum quality control. Curr Opin Struct Biol 16:592-599 (Pubitemid 44472609)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.5 , pp. 592-599
    • Moremen, K.W.1    Molinari, M.2
  • 52
    • 0035450192 scopus 로고    scopus 로고
    • Ubiquitin-dependent 26S proteasomal pathway: A role in the degradation of native human liver CYP3A4 expressed in Saccharomyces cerevisiae?
    • DOI 10.1006/abbi.2001.2482
    • Murray BP, Correia MA 2001 Ubiquitin-dependent 26S proteasomal pathway: a role in the degradation of native human liver CYP3A4 expressed in Saccharomyces cerevisiae? Arch Biochem Biophys 393:106-116 (Pubitemid 32808365)
    • (2001) Archives of Biochemistry and Biophysics , vol.393 , Issue.1 , pp. 106-116
    • Murray, B.P.1    Correia, M.A.2
  • 53
    • 0141532211 scopus 로고    scopus 로고
    • 2+
    • DOI 10.1074/jbc.M305600200
    • Webster JM, Tiwari S, Weissman AM, Wojcikiewicz RJ 2003 Inositol 1,4,5-trisphosphate receptor ubiquitination is mediated by mammalian Ubc7, a component of the endoplasmic reticulum-associated degradation pathway, and is inhibited by chelation of intracellular Zn2+. J Biol Chem 278:38238-38246 (Pubitemid 37221713)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.40 , pp. 38238-38246
    • Webster, J.M.1    Tiwari, S.2    Weissman, A.M.3    Wojcikiewicz, R.J.H.4


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