메뉴 건너뛰기




Volumn 9789400743519, Issue , 2012, Pages 3-22

Biology of the endoplasmic reticulum

Author keywords

apoptosis; autophagy; Calcium storage; carbohydrate metabolism; cell stress; drug detoxification; Endoplasmic reticulum; ERAD; glycosylation; Golgi; lipid biosynthesis; membrane trafficking; physiology; protein folding; protein secretion; unfolded protein response

Indexed keywords


EID: 84931332432     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-94-007-4351-9_1     Document Type: Chapter
Times cited : (19)

References (88)
  • 1
    • 85025399883 scopus 로고
    • A study of tissue culture cells by electron microscopy: Methods and preliminary observations
    • Porter KR, Claude A, Fullam EF (1945) A Study of Tissue Culture Cells by Electron Microscopy: Methods and Preliminary Observations. J Exp Med 81 (3):233-246
    • (1945) J Exp Med , vol.81 , Issue.3 , pp. 233-246
    • Porter, K.R.1    Claude, A.2    Fullam, E.F.3
  • 2
    • 0036776098 scopus 로고    scopus 로고
    • Structural organization of the endoplasmic reticulum
    • Voeltz GK, Rolls MM, Rapoport TA (2002) Structural organization of the endoplasmic reticulum. EMBO Rep 3 (10):944-950. doi: 10.1093/embo-reports/kvf202, 3/10/944 [pii]
    • (2002) EMBO Rep , vol.3 , Issue.10 , pp. 944-950
    • Voeltz, G.K.1    Rolls, M.M.2    Rapoport, T.A.3
  • 3
    • 77954218288 scopus 로고    scopus 로고
    • Further assembly required: Construction and dynamics of the endoplasmic reticulum network
    • Park SH, Blackstone C (2010) Further assembly required: construction and dynamics of the endoplasmic reticulum network. EMBO Rep 11 (7):515-521. doi: embor201092 [pii], 10.1038/embor.2010.92
    • (2010) EMBO Rep , vol.11 , Issue.7 , pp. 515-521
    • Park, S.H.1    Blackstone, C.2
  • 4
    • 79251471434 scopus 로고    scopus 로고
    • Mechanisms determining the morphology of the peripheral E.R
    • Shibata Y, Shemesh T, Prinz WA, Palazzo AF, Kozlov MM, Rapoport TA (2010) Mechanisms determining the morphology of the peripheral ER. Cell 143 (5):774-788. doi: S0092-8674(10)01251-1 [pii], 10.1016/j.cell.2010.11.007
    • (2010) Cell , vol.143 , Issue.5 , pp. 774-788
    • Shibata, Y.1    Shemesh, T.2    Prinz, W.A.3    Palazzo, A.F.4    Kozlov, M.M.5    Rapoport, T.A.6
  • 5
    • 78449294189 scopus 로고    scopus 로고
    • Molecular characterization of the endoplasmic reticulum: Insights from proteomic studies
    • Chen X, Karnovsky A, Sans MD, Andrews PC, Williams JA (2010) Molecular characterization of the endoplasmic reticulum: insights from proteomic studies. Proteomics 10 (22):4040-4052. doi: 10.1002/pmic.201000234
    • (2010) Proteomics , vol.10 , Issue.22 , pp. 4040-4052
    • Chen, X.1    Karnovsky, A.2    Sans, M.D.3    Andrews, P.C.4    Williams, J.A.5
  • 7
    • 0017858332 scopus 로고
    • Proteins of rough microsomal membranes related to ribosome binding I. Identification of ribophorins i and II, membrane proteins characteristics of rough microsomes
    • Kreibich G, Ulrich BL, Sabatini DD (1978) Proteins of rough microsomal membranes related to ribosome binding. I. Identification of ribophorins I and II, membrane proteins characteristics of rough microsomes. J Cell Biol 77 (2):464-487
    • (1978) J Cell Biol , vol.77 , Issue.2 , pp. 464-487
    • Kreibich, G.1    Ulrich, B.L.2    Sabatini, D.D.3
  • 8
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • Zimmerberg J, Kozlov MM (2006) How proteins produce cellular membrane curvature. Nat Rev Mol Cell Biol 7 (1):9-19. doi: nrm1784 [pii], 10.1038/nrm1784
    • (2006) Nat Rev Mol Cell Biol , vol.7 , Issue.1 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.M.2
  • 9
    • 70350230232 scopus 로고    scopus 로고
    • Mechanisms shaping the membranes of cellular organelles
    • Shibata Y, Hu J, Kozlov MM, Rapoport TA (2009) Mechanisms shaping the membranes of cellular organelles. Annu Rev Cell Dev Biol 25 329-354. doi: 10.1146/annurev.cellbio. 042308.113324
    • (2009) Annu Rev Cell Dev Biol , vol.25 , pp. 329-354
    • Shibata, Y.1    Hu, J.2    Kozlov, M.M.3    Rapoport, T.A.4
  • 10
    • 44349157134 scopus 로고    scopus 로고
    • Atlastin GTPases are required for Golgi apparatus and ER morphogenesis
    • Rismanchi N, Soderblom C, Stadler J, Zhu PP, Blackstone C (2008) Atlastin GTPases are required for Golgi apparatus and ER morphogenesis. Hum Mol Genet 17 (11):1591-1604. doi: ddn046 [pii], 10.1093/hmg/ddn046
    • (2008) Hum Mol Genet , vol.17 , Issue.11 , pp. 1591-1604
    • Rismanchi, N.1    Soderblom, C.2    Stadler, J.3    Zhu, P.P.4    Blackstone, C.5
  • 11
    • 67749102520 scopus 로고    scopus 로고
    • Cisternal organization of the endoplasmic reticulum during mitosis
    • Lu L, Ladinsky MS, Kirchhausen T (2009) Cisternal organization of the endoplasmic reticulum during mitosis. Mol Biol Cell 20 (15):3471-3480. doi: E09-04-0327 [pii], 10.1091/mbc. E09-04-0327
    • (2009) Mol Biol Cell , vol.20 , Issue.15 , pp. 3471-3480
    • Lu, L.1    Ladinsky, M.S.2    Kirchhausen, T.3
  • 12
    • 67949115773 scopus 로고    scopus 로고
    • Peripheral ER structure and function
    • English AR, Zurek N, Voeltz GK (2009) Peripheral ER structure and function. Curr Opin Cell Biol 21 (4):596-602. doi: S0955-0674(09)00090-8 [pii], 10.1016/j.ceb.2009.04.004
    • (2009) Curr Opin Cell Biol , vol.21 , Issue.4 , pp. 596-602
    • English, A.R.1    Zurek, N.2    Voeltz, G.K.3
  • 13
    • 67749122635 scopus 로고    scopus 로고
    • An ER-mitochondria tethering complex revealed by a synthetic biology screen
    • Kornmann B, Currie E, Collins SR, Schuldiner M, Nunnari J, Weissman JS, Walter P (2009) An ER-mitochondria tethering complex revealed by a synthetic biology screen. Science 325 (5939):477-481. doi: 1175088 [pii], 10.1126/science.1175088
    • (2009) Science , vol.325 , Issue.5939 , pp. 477-481
    • Kornmann, B.1    Currie, E.2    Collins, S.R.3    Schuldiner, M.4    Nunnari, J.5    Weissman, J.S.6    Walter, P.7
  • 14
    • 0021099854 scopus 로고
    • Rapid appearance of newly synthesized phosphatidylethanolamine at the plasma membrane
    • Sleight RG, Pagano RE (1983) Rapid appearance of newly synthesized phosphatidylethanolamine at the plasma membrane. J Biol Chem 258 (15):9050-9058
    • (1983) J Biol Chem , vol.258 , Issue.15 , pp. 9050-9058
    • Sleight, R.G.1    Pagano, R.E.2
  • 15
    • 34547175313 scopus 로고    scopus 로고
    • Live-cell imaging reveals sequential oligomerization and local plasma membrane targeting of stromal interaction molecule 1 after Ca2 + store depletion
    • Liou J, Fivaz M, Inoue T, Meyer T (2007) Live-cell imaging reveals sequential oligomerization and local plasma membrane targeting of stromal interaction molecule 1 after Ca2 + store depletion. Proc Natl Acad Sci U S A 104 (22):9301-9306. doi: 0702866104 [pii], 10.1073/ pnas.0702866104
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.22 , pp. 9301-9306
    • Liou, J.1    Fivaz, M.2    Inoue, T.3    Meyer, T.4
  • 16
    • 0033281074 scopus 로고    scopus 로고
    • The translocon: A dynamic gateway at the ER membrane
    • Johnson AE, van Waes MA (1999) The translocon: a dynamic gateway at the ER membrane. Annu Rev Cell Dev Biol 15 799-842. doi: 10.1146/annurev.cellbio.15.1.799
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 799-842
    • Johnson, A.E.1    Van Waes, M.A.2
  • 17
    • 27844485836 scopus 로고    scopus 로고
    • Protein translocation by the Sec61/SecY channel
    • Osborne AR, Rapoport TA, Van Den Berg B (2005) Protein translocation by the Sec61/SecY channel. Annu Rev Cell Dev Biol 21 529-550. doi: 10.1146/annurev.cellbio.21.012704.133214
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 529-550
    • Osborne, A.R.1    Rapoport, T.A.2    Van Den Berg, B.3
  • 18
    • 23744457478 scopus 로고    scopus 로고
    • Versatility of the endoplasmic reticulum protein folding factory
    • van Anken E, Braakman I (2005) Versatility of the endoplasmic reticulum protein folding factory. Crit Rev Biochem Mol Biol 40 (4):191-228. doi: W22V8337800PH27 J [pii], 10.1080/10409230591008161
    • (2005) Crit Rev Biochem Mol Biol , vol.40 , Issue.4 , pp. 191-228
    • Van Anken, E.1    Braakman, I.2
  • 19
    • 33749183647 scopus 로고    scopus 로고
    • N-linked glycan recognition and processing: The molecular basis of endoplasmic reticulum quality control
    • Moremen KW, Molinari M (2006) N-linked glycan recognition and processing: the molecular basis of endoplasmic reticulum quality control. Curr Opin Struct Biol 16 (5):592-599. doi: S0959-440X(06)00140-0 [pii], 10.1016/j.sbi.2006.08.005
    • (2006) Curr Opin Struct Biol , vol.16 , Issue.5 , pp. 592-599
    • Moremen, K.W.1    Molinari, M.2
  • 20
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia R, Braakman I (2003) Quality control in the endoplasmic reticulum protein factory. Nature 426 (6968):891-894. doi: 10.1038/nature02262, nature02262 [pii]
    • (2003) Nature , vol.426 , Issue.6968 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 21
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert DN, Foellmer B, Helenius A (1995) Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81 (3):425-433. doi: 0092-8674(95)90395-X [pii]
    • (1995) Cell , vol.81 , Issue.3 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 22
    • 0033210210 scopus 로고    scopus 로고
    • GRP94, an ER chaperone with protein and peptide binding properties
    • Argon Y, Simen BB (1999) GRP94, an ER chaperone with protein and peptide binding properties. Semin Cell Dev Biol 10 (5):495-505. doi: S1084-9521(99)90320-8 [pii], 10.1006/ scdb.1999.0320
    • (1999) Semin Cell Dev Biol , vol.10 , Issue.5 , pp. 495-505
    • Argon, Y.1    Simen, B.B.2
  • 23
    • 0035423875 scopus 로고    scopus 로고
    • The glucose-regulated proteins: Stress induction and clinical applications
    • Lee AS (2001) The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem Sci 26 (8):504-510. doi: S0968-0004(01)01908-9 [pii]
    • (2001) Trends Biochem Sci , vol.26 , Issue.8 , pp. 504-510
    • Lee, A.S.1
  • 24
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn GC, Pohl J, Flocco MT, Rothman JE (1991) Peptide-binding specificity of the molecular chaperone BiP. Nature 353 (6346):726-730. doi: 10.1038/353726a0
    • (1991) Nature , vol.353 , Issue.6346 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 25
    • 4444318357 scopus 로고    scopus 로고
    • ER chaperone functions during normal and stress conditions
    • Ma Y, Hendershot LM (2004) ER chaperone functions during normal and stress conditions. J Chem Neuroanat 28 (1-2):51-65. doi: 10.1016/j.jchemneu.2003.08.007, S0891061804000031 [pii]
    • (2004) J Chem Neuroanat , vol.28 , Issue.1-2 , pp. 51-65
    • Ma, Y.1    Hendershot, L.M.2
  • 26
    • 0347033285 scopus 로고    scopus 로고
    • BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP
    • Chung KT, Shen Y, Hendershot LM (2002) BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP. J Biol Chem 277 (49):47557-47563. doi: 10.1074/jbc.M208377200, M208377200 [pii]
    • (2002) J Biol Chem , vol.277 , Issue.49 , pp. 47557-47563
    • Chung, K.T.1    Shen, Y.2    Hendershot, L.M.3
  • 27
    • 0029890917 scopus 로고    scopus 로고
    • Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants
    • Hendershot L, Wei J, Gaut J, Melnick J, Aviel S, Argon Y (1996) Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants. Proc Natl Acad Sci U S A 93 (11):5269-5274
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.11 , pp. 5269-5274
    • Hendershot, L.1    Wei, J.2    Gaut, J.3    Melnick, J.4    Aviel, S.5    Argon, Y.6
  • 28
    • 0033612302 scopus 로고    scopus 로고
    • BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane
    • Matlack KE, Misselwitz B, Plath K, Rapoport TA (1999) BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell 97 (5):553-564. doi: S0092-8674(00)80767-9 [pii]
    • (1999) Cell , vol.97 , Issue.5 , pp. 553-564
    • Matlack, K.E.1    Misselwitz, B.2    Plath, K.3    Rapoport, T.A.4
  • 29
    • 77952580752 scopus 로고    scopus 로고
    • Life and death of a BiP substrate
    • Otero JH, Lizak B, Hendershot LM (2010) Life and death of a BiP substrate. Semin Cell Dev Biol 21 (5):472-478. doi: S1084-9521(09)00253-5 [pii], 10.1016/j.semcdb.2009.12.008
    • (2010) Semin Cell Dev Biol , vol.21 , Issue.5 , pp. 472-478
    • Otero, J.H.1    Lizak, B.2    Hendershot, L.M.3
  • 30
    • 77952583297 scopus 로고    scopus 로고
    • Protein quality control in the ER: The recognition of misfolded proteins
    • Maattanen P, Gehring K, Bergeron JJ, Thomas DY (2010) Protein quality control in the ER: the recognition of misfolded proteins. Semin Cell Dev Biol 21 (5):500-511. doi: S1084-9521(10)00068-6 [pii], 10.1016/j.semcdb.2010.03.006
    • (2010) Semin Cell Dev Biol , vol.21 , Issue.5 , pp. 500-511
    • Maattanen, P.1    Gehring, K.2    Bergeron, J.J.3    Thomas, D.Y.4
  • 31
    • 0026604334 scopus 로고
    • Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum
    • Braakman I, Helenius J, Helenius A (1992) Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. Embo J 11 (5):1717-1722
    • (1992) Embo J , vol.11 , Issue.5 , pp. 1717-1722
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 32
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: Mechanisms and consequences
    • Tu BP, Weissman JS (2004) Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol 164 (3):341-346. doi: 10.1083/jcb.200311055, jcb.200311055 [pii]
    • (2004) J Cell Biol , vol.164 , Issue.3 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 33
    • 70849101711 scopus 로고    scopus 로고
    • Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins
    • Jessop CE, Watkins RH, Simmons JJ, Tasab M, Bulleid NJ (2009) Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins. J Cell Sci 122 (Pt 23):4287-4295. doi: jcs.059154 [pii], 10.1242/jcs.059154
    • (2009) J Cell Sci , vol.122 , pp. 4287-4295
    • Jessop, C.E.1    Watkins, R.H.2    Simmons, J.J.3    Tasab, M.4    Bulleid, N.J.5
  • 34
    • 0028131648 scopus 로고
    • Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds
    • Cai H, Wang CC, Tsou CL (1994) Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds. J Biol Chem 269 (40):24550-24552
    • (1994) J Biol Chem , vol.269 , Issue.40 , pp. 24550-24552
    • Cai, H.1    Wang, C.C.2    Tsou, C.L.3
  • 35
    • 0032079359 scopus 로고    scopus 로고
    • Thiol-independent interaction of protein disulphide isomerase with type X collagen during intra-cellular folding and assembly
    • McLaughlin SH, Bulleid NJ (1998) Thiol-independent interaction of protein disulphide isomerase with type X collagen during intra-cellular folding and assembly. Biochem J 331 (Pt 3) 793-800
    • (1998) Biochem J , vol.331 , pp. 793-800
    • McLaughlin, S.H.1    Bulleid, N.J.2
  • 36
    • 75049084045 scopus 로고    scopus 로고
    • Protein disulphide isomerase is required for signal peptide peptidase-mediated protein degradation
    • Lee SO, Cho K, Cho S, Kim I, Oh C, Ahn K (2010) Protein disulphide isomerase is required for signal peptide peptidase-mediated protein degradation. Embo J 29 (2):363-375. doi: emboj2009359 [pii], 10.1038/emboj.2009.359
    • (2010) Embo J , vol.29 , Issue.2 , pp. 363-375
    • Lee, S.O.1    Cho, K.2    Cho, S.3    Kim, I.4    Oh, C.5    Ahn, K.6
  • 37
    • 65149091065 scopus 로고    scopus 로고
    • Structure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72
    • Kozlov G, Maattanen P, Schrag JD, Hura GL, Gabrielli L, Cygler M, Thomas DY, Gehring K (2009) Structure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72. Structure 17 (5):651-659. doi: S0969-2126(09)00149-X [pii], 10.1016/j. str.2009.02.016
    • (2009) Structure , vol.17 , Issue.5 , pp. 651-659
    • Kozlov, G.1    Maattanen, P.2    Schrag, J.D.3    Hura, G.L.4    Gabrielli, L.5    Cygler, M.6    Thomas, D.Y.7    Gehring, K.8
  • 38
    • 33846192436 scopus 로고    scopus 로고
    • ERp57 is essential for efficient folding of glycoproteins sharing common structural domains
    • Jessop CE, Chakravarthi S, Garbi N, Hammerling GJ, Lovell S, Bulleid NJ (2007) ERp57 is essential for efficient folding of glycoproteins sharing common structural domains. Embo J 26 (1):28-40. doi: 7601505 [pii], 10.1038/sj.emboj.7601505
    • (2007) Embo J , vol.26 , Issue.1 , pp. 28-40
    • Jessop, C.E.1    Chakravarthi, S.2    Garbi, N.3    Hammerling, G.J.4    Lovell, S.5    Bulleid, N.J.6
  • 39
    • 0036862532 scopus 로고    scopus 로고
    • The FAD-and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum
    • Tu BP, Weissman JS (2002) The FAD-and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum. Mol Cell 10 (5):983-994. doi: S1097276502006962 [pii]
    • (2002) Mol Cell , vol.10 , Issue.5 , pp. 983-994
    • Tu, B.P.1    Weissman, J.S.2
  • 41
    • 34147126077 scopus 로고    scopus 로고
    • Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1
    • Sevier CS, Qu H, Heldman N, Gross E, Fass D, Kaiser CA (2007) Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1. Cell 129 (2):333-344. doi: S0092-8674(07)00325-X [pii], 10.1016/j.cell.2007.02.039
    • (2007) Cell , vol.129 , Issue.2 , pp. 333-344
    • Sevier, C.S.1    Qu, H.2    Heldman, N.3    Gross, E.4    Fass, D.5    Kaiser, C.A.6
  • 42
    • 59049105293 scopus 로고    scopus 로고
    • Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin
    • Jessop CE, Tavender TJ, Watkins RH, Chambers JE, Bulleid NJ (2009) Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin. J Biol Chem 284 (4):2194-2202. doi: M808054200 [pii], 10.1074/jbc.M808054200
    • (2009) J Biol Chem , vol.284 , Issue.4 , pp. 2194-2202
    • Jessop, C.E.1    Tavender, T.J.2    Watkins, R.H.3    Chambers, J.E.4    Bulleid, N.J.5
  • 43
    • 0032513212 scopus 로고    scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
    • Zapun A, Darby NJ, Tessier DC, Michalak M, Bergeron JJ, Thomas DY (1998) Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J Biol Chem 273 (11):6009-6012
    • (1998) J Biol Chem , vol.273 , Issue.11 , pp. 6009-6012
    • Zapun, A.1    Darby, N.J.2    Tessier, D.C.3    Michalak, M.4    Bergeron, J.J.5    Thomas, D.Y.6
  • 44
    • 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 (7237):453-460. doi: nature07962 [pii], 10.1038/ nature07962
    • (2009) Nature , vol.458 , Issue.7237 , pp. 453-460
    • Hirsch, C.1    Gauss, R.2    Horn, S.C.3    Neuber, O.4    Sommer, T.5
  • 45
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • Vembar SS, Brodsky JL (2008) One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 9 (12):944-957. doi: nrm2546 [pii], 10.1038/nrm2546
    • (2008) Nat Rev Mol Cell Biol , vol.9 , Issue.12 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 46
  • 47
    • 79851515002 scopus 로고    scopus 로고
    • Protein dislocation from the E.R
    • Bagola K, Mehnert M, Jarosch E, Sommer T (2011) Protein dislocation from the ER. Biochim Biophys Acta 1808 (3):925-936. doi: S0005-2736(10)00223-3 [pii], 10.1016/j. bbamem.2010.06.025
    • (2011) Biochim Biophys Acta , vol.1808 , Issue.3 , pp. 925-936
    • Bagola, K.1    Mehnert, M.2    Jarosch, E.3    Sommer, T.4
  • 48
    • 46249094620 scopus 로고    scopus 로고
    • Role of Sec61p in the ER-associated degradation of short-lived transmembrane proteins
    • Scott DC, Schekman R (2008) Role of Sec61p in the ER-associated degradation of short-lived transmembrane proteins. J Cell Biol 181 (7):1095-1105. doi: jcb.200804053 [pii], 10.1083/ jcb.200804053
    • (2008) J Cell Biol , vol.181 , Issue.7 , pp. 1095-1105
    • Scott, D.C.1    Schekman, R.2
  • 49
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the E.R
    • Lilley BN, Ploegh HL (2004) A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429 (6994):834-840. doi: 10.1038/nature02592, nature02592 [pii]
    • (2004) Nature , vol.429 , Issue.6994 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 50
    • 33845939821 scopus 로고    scopus 로고
    • Cdc48(p97): A "molecular gearbox" in the ubiquitin pathway
    • Jentsch S, Rumpf S (2007) Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway? Trends Biochem Sci 32 (1):6-11. doi: S0968-0004(06)00322-7 [pii], 10.1016/j. tibs.2006.11.005
    • (2007) Trends Biochem Sci , vol.32 , Issue.1 , pp. 6-11
    • Jentsch, S.1    Rumpf, S.2
  • 51
    • 0033938963 scopus 로고    scopus 로고
    • Transport between ER and Golgi
    • Klumperman J (2000) Transport between ER and Golgi. Curr Opin Cell Biol 12 (4):445-449. doi: S0955-0674(00)00115-0 [pii]
    • (2000) Curr Opin Cell Biol , vol.12 , Issue.4 , pp. 445-449
    • Klumperman, J.1
  • 53
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment(ERGIC): In search of its identity and function
    • Appenzeller-Herzog C, Hauri HP (2006) The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. J Cell Sci 119 (Pt 11):2173-2183. doi: 119/11/2173 [pii], 10.1242/jcs.03019
    • (2006) J Cell Sci , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.P.2
  • 54
    • 0036877142 scopus 로고    scopus 로고
    • The endoplasmic reticulum: A multifunctional signaling organelle
    • Berridge MJ (2002) The endoplasmic reticulum: a multifunctional signaling organelle. Cell Calcium 32 (5-6):235-249. doi: S0143416002001823 [pii]
    • (2002) Cell Calcium , vol.32 , Issue.5-6 , pp. 235-249
    • Berridge, M.J.1
  • 55
    • 0036877146 scopus 로고    scopus 로고
    • Ca2 + signaling and calcium binding chaperones of the endoplasmic reticulum
    • Michalak M, Robert Parker JM, Opas M (2002) Ca2 + signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium 32 (5-6):269-278. doi: S0143416002001884 [pii]
    • (2002) Cell Calcium , vol.32 , Issue.5-6 , pp. 269-278
    • Michalak, M.1    Robert, P.J.M.2    Opas, M.3
  • 56
    • 0038125598 scopus 로고    scopus 로고
    • Calcium signalling: Dynamics, homeostasis and remodelling
    • Berridge MJ, Bootman MD, Roderick HL (2003) Calcium signalling: dynamics, homeostasis and remodelling. Nat Rev Mol Cell Biol 4 (7):517-529. doi: 10.1038/nrm1155 [pii]
    • (2003) Nat Rev Mol Cell Biol , vol.4 , Issue.7 , pp. 517-529
    • Berridge, M.J.1    Bootman, M.D.2    Roderick, H.L.3
  • 57
    • 26444529021 scopus 로고    scopus 로고
    • The endoplasmic reticulum in xenobiotic toxicity
    • Cribb AE, Peyrou M, Muruganandan S, Schneider L (2005) The endoplasmic reticulum in xenobiotic toxicity. Drug Metab Rev 37 (3):405-442. doi: V55U40395RU7671 M [pii], 10.1080/03602530500205135
    • (2005) Drug Metab Rev , vol.37 , Issue.3 , pp. 405-442
    • Cribb, A.E.1    Peyrou, M.2    Muruganandan, S.3    Schneider, L.4
  • 58
    • 0023898817 scopus 로고
    • The immunocytochemical localisation and distribution of cytochrome P-450 in normal human hepatic and extrahepatic tissues with a monoclonal antibody to human cytochrome P-450
    • Murray GI, Barnes TS, Sewell HF, Ewen SW, Melvin WT, Burke MD (1988) The immunocytochemical localisation and distribution of cytochrome P-450 in normal human hepatic and extrahepatic tissues with a monoclonal antibody to human cytochrome P-450. Br J Clin Pharmacol 25 (4):465-475
    • (1988) Br J Clin Pharmacol , vol.25 , Issue.4 , pp. 465-475
    • Murray, G.I.1    Barnes, T.S.2    Sewell, H.F.3    Ewen, S.W.4    Melvin, W.T.5    Burke, M.D.6
  • 59
    • 0026651273 scopus 로고
    • Human cytochromes P450: Problems and prospects
    • Gonzalez FJ (1992) Human cytochromes P450: problems and prospects. Trends Pharmacol Sci 13 (9):346-352
    • (1992) Trends Pharmacol Sci , vol.13 , Issue.9 , pp. 346-352
    • Gonzalez, F.J.1
  • 60
    • 0028272001 scopus 로고
    • Role of human cytochromes P450 in the metabolic activation of chemical carcinogens and toxins
    • Gonzalez FJ, Gelboin HV (1994) Role of human cytochromes P450 in the metabolic activation of chemical carcinogens and toxins. Drug Metab Rev 26 (1-2):165-183. doi: 10.3109/03602539409029789
    • (1994) Drug Metab Rev , vol.26 , Issue.1-2 , pp. 165-183
    • Gonzalez, F.J.1    Gelboin, H.V.2
  • 61
    • 0028945438 scopus 로고
    • Structural and catalytic properties of the mammalian flavin-containing monooxygenase
    • Cashman JR (1995) Structural and catalytic properties of the mammalian flavin-containing monooxygenase. Chem Res Toxicol 8 (2):166-181
    • (1995) Chem Res Toxicol , vol.8 , Issue.2 , pp. 166-181
    • Cashman, J.R.1
  • 62
    • 0023835220 scopus 로고
    • Human microsomal xenobiotic epoxide hydrolase Complementary DNA sequence, complementary DNA-directed expression in COS-1 cells, and chromosomal localization
    • Skoda RC, Demierre A, McBride OW, Gonzalez FJ, Meyer UA (1988) Human microsomal xenobiotic epoxide hydrolase. Complementary DNA sequence, complementary DNA-directed expression in COS-1 cells, and chromosomal localization. J Biol Chem 263 (3):1549-1554
    • (1988) J Biol Chem , vol.263 , Issue.3 , pp. 1549-1554
    • Skoda, R.C.1    Demierre, A.2    McBride, O.W.3    Gonzalez, F.J.4    Meyer, U.A.5
  • 63
    • 0025344378 scopus 로고
    • Cytochrome P 450 isoenzymes, epoxide hydrolase and glutathione transferases in rat and human hepatic and extrahepatic tissues
    • de Waziers I, Cugnenc PH, Yang CS, Leroux JP, Beaune PH (1990) Cytochrome P 450 isoenzymes, epoxide hydrolase and glutathione transferases in rat and human hepatic and extrahepatic tissues. J Pharmacol Exp Ther 253 (1):387-394
    • (1990) J Pharmacol Exp Ther , vol.253 , Issue.1 , pp. 387-394
    • De Waziers, I.1    Cugnenc, P.H.2    Yang, C.S.3    Leroux, J.P.4    Beaune, P.H.5
  • 64
    • 0031800635 scopus 로고    scopus 로고
    • The mammalian carboxylesterases: From molecules to functions
    • Satoh T, Hosokawa M (1998) The mammalian carboxylesterases: from molecules to functions. Annu Rev Pharmacol Toxicol 38 257-288. doi: 10.1146/annurev.pharmtox.38.1.257
    • (1998) Annu Rev Pharmacol Toxicol , vol.38 , pp. 257-288
    • Satoh, T.1    Hosokawa, M.2
  • 66
    • 0021677474 scopus 로고
    • The distribution of microsomal glutathione transferase among different organelles, different organs, and different organisms
    • Morgenstern R, Lundqvist G, Andersson G, Balk L, DePierre JW (1984) The distribution of microsomal glutathione transferase among different organelles, different organs, and different organisms. Biochem Pharmacol 33 (22):3609-3614. doi: 0006-2952(84)90145-X [pii]
    • (1984) Biochem Pharmacol , vol.33 , Issue.22 , pp. 3609-3614
    • Morgenstern, R.1    Lundqvist, G.2    Andersson, G.3    Balk, L.4    Depierre, J.W.5
  • 67
    • 0030923439 scopus 로고    scopus 로고
    • Identification and characterization of a novel microsomal enzyme with glutathione-dependent transferase and peroxidase activities
    • Jakobsson PJ, Mancini JA, Riendeau D, Ford-Hutchinson AW (1997) Identification and characterization of a novel microsomal enzyme with glutathione-dependent transferase and peroxidase activities. J Biol Chem 272 (36):22934-22939
    • (1997) J Biol Chem , vol.272 , Issue.36 , pp. 22934-22939
    • Jakobsson, P.J.1    Mancini, J.A.2    Riendeau, D.3    Ford-Hutchinson, A.W.4
  • 68
    • 79952083050 scopus 로고    scopus 로고
    • Genetic polymorphism and toxicology-with emphasis on cytochrome p450
    • Johansson I, Ingelman-Sundberg M (2011) Genetic polymorphism and toxicology-with emphasis on cytochrome p450. Toxicol Sci 120 (1):1-13. doi: kfq374 [pii], 10.1093/toxsci/ kfq374
    • (2011) Toxicol Sci , vol.120 , Issue.1 , pp. 1-13
    • Johansson, I.1    Ingelman-Sundberg, M.2
  • 69
    • 85006172820 scopus 로고
    • Differentiation of endoplasmic reticulum in hepatocytes: I glucose-6-phosphatase distribution in situ
    • Leskes A, Siekevitz P, Palade GE (1971) Differentiation of Endoplasmic Reticulum in Hepatocytes: I. Glucose-6-Phosphatase Distribution In Situ. J Cell Biol 49 (2):264-287
    • (1971) J Cell Biol , vol.49 , Issue.2 , pp. 264-287
    • Leskes, A.1    Siekevitz, P.2    Palade, G.E.3
  • 70
    • 0019200193 scopus 로고
    • Control of hepatic glycogenolysis
    • Hems DA, Whitton PD (1980) Control of hepatic glycogenolysis. Physiol Rev 60 (1):1-50
    • (1980) Physiol Rev , vol.60 , Issue.1 , pp. 1-50
    • Hems, D.A.1    Whitton, P.D.2
  • 71
    • 0037086660 scopus 로고    scopus 로고
    • The glucose-6-phosphatase system
    • van Schaftingen E, Gerin I (2002) The glucose-6-phosphatase system. Biochem J 362 (Pt 3):513-532
    • (2002) Biochem J , vol.362 , pp. 513-532
    • Van Schaftingen, E.1    Gerin, I.2
  • 72
    • 66349117317 scopus 로고    scopus 로고
    • Membrane phospholipid synthesis and endoplasmic reticulum function
    • Fagone P, Jackowski S (2009) Membrane phospholipid synthesis and endoplasmic reticulum function. J Lipid Res Suppl 50 S 311-316 doi: R800049-JLR200 [pii], 10.1194/jlr.R800049-JLR200
    • (2009) J Lipid Res Suppl , vol.50 , pp. S311-316
    • Fagone, P.1    Jackowski, S.2
  • 73
    • 0019863261 scopus 로고
    • Analytical fractionation of human liver microsomal fractions: Localization of cholesterol and of the enzymes relevant to its metabolism
    • Balasubramaniam S, Mitropoulos KA, Venkatesan S, Myant NB, Peters TJ, Postiglione A, Mancini M (1981) Analytical fractionation of human liver microsomal fractions: localization of cholesterol and of the enzymes relevant to its metabolism. Clin Sci (Lond) 60 (4):435-439
    • (1981) Clin Sci(Lond) , vol.60 , Issue.4 , pp. 435-439
    • Balasubramaniam, S.1    Mitropoulos, K.A.2    Venkatesan, S.3    Myant, N.B.4    Peters, T.J.5    Postiglione, A.6    Mancini, M.7
  • 74
    • 0036251153 scopus 로고    scopus 로고
    • SREBPs: Activators of the complete program of cholesterol and fatty acid synthesis in the liver
    • Horton JD, Goldstein JL, Brown MS (2002) SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver. J Clin Invest 109 (9):1125-1131. doi: 10.1172/ JCI15593
    • (2002) J Clin Invest , vol.109 , Issue.9 , pp. 1125-1131
    • Horton, J.D.1    Goldstein, J.L.2    Brown, M.S.3
  • 75
    • 79953757255 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and lipid dysregulation
    • Colgan SM, Hashimi AA, Austin RC (2011) Endoplasmic reticulum stress and lipid dysregulation. Expert Rev Mol Med 13 e4. doi: S1462399410001742 [pii], 10.1017/S1462399410001742
    • (2011) Expert Rev Mol Med , vol.13 , pp. e4
    • Colgan, S.M.1    Hashimi, A.A.2    Austin, R.C.3
  • 76
    • 78049518892 scopus 로고    scopus 로고
    • An overview of sphingolipid metabolism: From synthesis to breakdown
    • Gault CR, Obeid LM, Hannun YA (2010) An overview of sphingolipid metabolism: from synthesis to breakdown. Adv Exp Med Biol 688:1-23
    • (2010) Adv Exp Med Biol , vol.688 , pp. 1-23
    • Gault, C.R.1    Obeid, L.M.2    Hannun, Y.A.3
  • 77
    • 79957605136 scopus 로고    scopus 로고
    • Aberrant lipid metabolism disrupts calcium homeostasis causing liver endoplasmic reticulum stress in obesity
    • Fu S, Yang L, Li P, Hofmann O, Dicker L, Hide W, Lin X, Watkins SM, Ivanov AR, Hotamisligil GS (2011) Aberrant lipid metabolism disrupts calcium homeostasis causing liver endoplasmic reticulum stress in obesity. Nature 473 (7348):528-531. doi: nature09968 [pii] 10.1038/nature09968
    • (2011) Nature , vol.473 , Issue.7348 , pp. 528-531
    • Fu, S.1    Yang, L.2    Li, P.3    Hofmann, O.4    Dicker, L.5    Hide, W.6    Lin, X.7    Watkins, S.M.8    Ivanov, A.R.9    Hotamisligil, G.S.10
  • 78
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder M, Kaufman RJ (2005) The mammalian unfolded protein response. Annu Rev Biochem 74:739-789 doi: 10.1146/annurev.biochem.73.011303.074134
    • (2005) Annu Rev Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 79
    • 0026611735 scopus 로고
    • Brefeldin A, thapsigargin, and AIF4-stimulate the accumulation of GRP78 mRNA in a cycloheximide dependent manner, whilst induction by hypoxia is independent of protein synthesis
    • Price BD, Mannheim-Rodman LA, Calderwood SK (1992) Brefeldin A, thapsigargin, and AIF4-stimulate the accumulation of GRP78 mRNA in a cycloheximide dependent manner, whilst induction by hypoxia is independent of protein synthesis. J Cell Physiol 152 (3):545-552 doi: 10.1002/jcp.1041520314
    • (1992) J Cell Physiol , vol.152 , Issue.3 , pp. 545-552
    • Price, B.D.1    Mannheim-Rodman, L.A.2    Calderwood, S.K.3
  • 80
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • Obeng EA, Carlson LM, Gutman DM, Harrington WJ Jr, Lee KP, Boise LH (2006) Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. Blood 107 (12):4907-4916. doi: 2005-08-3531 [pii], 10.1182/blood-2005-08-3531
    • (2006) Blood , vol.107 , Issue.12 , pp. 4907-4916
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3    Harrington, W.J.4    Lee, K.P.5    Boise, L.H.6
  • 81
    • 38449087466 scopus 로고    scopus 로고
    • The role of the UPS in cystic fibrosis
    • Turnbull EL, Rosser MF, Cyr DM (2007) The role of the UPS in cystic fibrosis. BMC Biochem 8 Suppl1:S 11 doi: 1471-2091-8-S1-S11 [pii], 10.1186/1471-2091-8-S1-S11
    • (2007) BMC Biochem , vol.8 , Issue.1 , pp. 11
    • Turnbull, E.L.1    Rosser, M.F.2    Cyr, D.M.3
  • 82
    • 27744542188 scopus 로고    scopus 로고
    • Cell toxicity and conformational disease
    • Carrell RW (2005) Cell toxicity and conformational disease. Trends Cell Biol 15 (11):574-580. doi: S0962-8924(05)00229-1 [pii], 10.1016/j.tcb.2005.09.005
    • (2005) Trends Cell Biol , vol.15 , Issue.11 , pp. 574-580
    • Carrell, R.W.1
  • 83
    • 39449111277 scopus 로고    scopus 로고
    • Sequestration of mutated alpha1-antitrypsin into inclusion bodies is a cell-protective mechanism to maintain endoplasmic reticulum function
    • Granell S, Baldini G, Mohammad S, Nicolin V, Narducci P, Storrie B (2008) Sequestration of mutated alpha1-antitrypsin into inclusion bodies is a cell-protective mechanism to maintain endoplasmic reticulum function. Mol Biol Cell 19 (2):572-586. doi: E07-06-0587 [pii], 10.1091/mbc.E07-06-0587
    • (2008) Mol Biol Cell , vol.19 , Issue.2 , pp. 572-586
    • Granell, S.1    Baldini, G.2    Mohammad, S.3    Nicolin, V.4    Narducci, P.5    Storrie, B.6
  • 84
    • 33748789479 scopus 로고    scopus 로고
    • Mediators of endoplasmic reticulum stress-induced apoptosis
    • Szegezdi E, Logue SE, Gorman AM, Samali A (2006) Mediators of endoplasmic reticulum stress-induced apoptosis. EMBO Reports 7 (9):880-885. doi: 7400779 [pii], 10.1038/ sj.embor.7400779
    • (2006) EMBO Reports , vol.7 , Issue.9 , pp. 880-885
    • Szegezdi, E.1    Logue, S.E.2    Gorman, A.M.3    Samali, A.4
  • 85
    • 0036091476 scopus 로고    scopus 로고
    • The PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas
    • Zhang P, McGrath B, Li S, Frank A, Zambito F, Reinert J, Gannon M, Ma K, McNaughton K, Cavener DR (2002) The PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas. Mol Cell Biol 22 (11):3864-3874
    • (2002) Mol Cell Biol , vol.22 , Issue.11 , pp. 3864-3874
    • Zhang, P.1    McGrath, B.2    Li, S.3    Frank, A.4    Zambito, F.5    Reinert, J.6    Gannon, M.7    Ma, K.8    McNaughton, K.9    Cavener, D.R.10
  • 87
    • 77958590030 scopus 로고    scopus 로고
    • IRE1alpha disruption causes histological abnormality of exocrine tissues, increase of blood glucose level, and decrease of serum immunoglobulin level
    • Iwawaki T, Akai R, Kohno K (2010) IRE1alpha disruption causes histological abnormality of exocrine tissues, increase of blood glucose level, and decrease of serum immunoglobulin level. PLoS One 5 (9):e13052. doi: e13052 [pii], 10.1371/journal.pone.0013052
    • (2010) PLoS One , vol.5 , Issue.9 , pp. e13052
    • Iwawaki, T.1    Akai, R.2    Kohno, K.3
  • 88
    • 14944371187 scopus 로고    scopus 로고
    • The unfolded protein response sensor IRE1alpha is required at 2 distinct steps in B cell lymphopoiesis
    • Zhang K, Wong HN, Song B, Miller CN, Scheuner D, Kaufman RJ (2005) The unfolded protein response sensor IRE1alpha is required at 2 distinct steps in B cell lymphopoiesis. J Clin Invest 115 (2):268-281.doi: 10.1172/JCI21848
    • (2005) J Clin Invest , vol.115 , Issue.2 , pp. 268-281
    • Zhang, K.1    Wong, H.N.2    Song, B.3    Miller, C.N.4    Scheuner, D.5    Kaufman, R.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.