메뉴 건너뛰기




Volumn 23, Issue 2, 2011, Pages 167-175

Disulfide bonds in ER protein folding and homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 79954417748     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2010.10.012     Document Type: Review
Times cited : (148)

References (94)
  • 1
    • 38549103628 scopus 로고    scopus 로고
    • Protein quality control in the early secretory pathway
    • Anelli T., Sitia R. Protein quality control in the early secretory pathway. EMBO J 2008, 27:315-327.
    • (2008) EMBO J , vol.27 , pp. 315-327
    • Anelli, T.1    Sitia, R.2
  • 2
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: protein folding, quality control, degradation, and related human diseases
    • Hebert D.N., Molinari M. In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol Rev 2007, 87:1377-1408.
    • (2007) Physiol Rev , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 3
    • 77950675123 scopus 로고    scopus 로고
    • Evasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality control
    • Wang S., Ng D.T. Evasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality control. Mol Biol Cell 2010, 21:1153-1165.
    • (2010) Mol Biol Cell , vol.21 , pp. 1153-1165
    • Wang, S.1    Ng, D.T.2
  • 5
    • 79954424872 scopus 로고    scopus 로고
    • Participation of lectin chaperones and thiol oxidoreductases in protein folding within the endoplasmic reticulum
    • Rutkevich L.A., Williams D.B. Participation of lectin chaperones and thiol oxidoreductases in protein folding within the endoplasmic reticulum. Curr Opin Cell Biol 2011, 23:157-166.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 157-166
    • Rutkevich, L.A.1    Williams, D.B.2
  • 6
    • 79954423161 scopus 로고    scopus 로고
    • The role of disulfide bonds in protein folding and stability
    • Luis Moroder, Johannes Buchner (Eds.)
    • Feige M.J., Buchner J. The role of disulfide bonds in protein folding and stability. Oxidative Folding of Peptides and Proteins 2010, Luis Moroder, Johannes Buchner (Eds.).
    • (2010) Oxidative Folding of Peptides and Proteins
    • Feige, M.J.1    Buchner, J.2
  • 7
    • 0029049090 scopus 로고
    • Cotranslational folding and calnexin binding during glycoprotein synthesis
    • Chen W., Helenius J., Braakman I., Helenius A. Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc Natl Acad Sci USA 1995, 92:6229-6233.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6229-6233
    • Chen, W.1    Helenius, J.2    Braakman, I.3    Helenius, A.4
  • 8
    • 0020479440 scopus 로고
    • The biosynthesis of rat serum albumin, In vivo studies on the formation of the disulfide bonds
    • Peters T., Davidson L.K. The biosynthesis of rat serum albumin, In vivo studies on the formation of the disulfide bonds. J Biol Chem 1982, 257:8847-8853.
    • (1982) J Biol Chem , vol.257 , pp. 8847-8853
    • Peters, T.1    Davidson, L.K.2
  • 9
    • 0025816663 scopus 로고
    • Folding of influenza hemagglutinin in the endoplasmic reticulum
    • Braakman I., Hoover-Litty H., Wagner K.R., Helenius A. Folding of influenza hemagglutinin in the endoplasmic reticulum. J Cell Biol 1991, 114:401-411.
    • (1991) J Cell Biol , vol.114 , pp. 401-411
    • Braakman, I.1    Hoover-Litty, H.2    Wagner, K.R.3    Helenius, A.4
  • 10
    • 0018679846 scopus 로고
    • Formation of an intrachain disulfide bond on nascent immunoglobulin light chains
    • Bergman L.W., Kuehl W.M. Formation of an intrachain disulfide bond on nascent immunoglobulin light chains. J Biol Chem 1979, 254:8869-8876.
    • (1979) J Biol Chem , vol.254 , pp. 8869-8876
    • Bergman, L.W.1    Kuehl, W.M.2
  • 11
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • Daniels R., Kurowski B., Johnson A.E., Hebert D.N. N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol Cell 2003, 11:79-90.
    • (2003) Mol Cell , vol.11 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4
  • 12
    • 0032838622 scopus 로고    scopus 로고
    • BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly
    • Lee Y.K., Brewer J.W., Hellman R., Hendershot L.M. BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly. Mol Biol Cell 1999, 10:2209-2219.
    • (1999) Mol Biol Cell , vol.10 , pp. 2209-2219
    • Lee, Y.K.1    Brewer, J.W.2    Hellman, R.3    Hendershot, L.M.4
  • 13
    • 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 Y.K., Chung K.T., Hendershot L.M. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 2002, 13:4456-4469.
    • (2002) Mol Biol Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 15
    • 0037458652 scopus 로고    scopus 로고
    • Disulfide folding pathways of cystine knot proteins. Tying the knot within the circular backbone of the cyclotides
    • Daly N.L., Clark R.J., Craik D.J. Disulfide folding pathways of cystine knot proteins. Tying the knot within the circular backbone of the cyclotides. J Biol Chem 2003, 278:6314-6322.
    • (2003) J Biol Chem , vol.278 , pp. 6314-6322
    • Daly, N.L.1    Clark, R.J.2    Craik, D.J.3
  • 16
    • 2142764423 scopus 로고    scopus 로고
    • Disulfide bond rearrangement during formation of the chorionic gonadotropin beta-subunit cystine knot in vivo
    • Wilken J.A., Bedows E. Disulfide bond rearrangement during formation of the chorionic gonadotropin beta-subunit cystine knot in vivo. Biochemistry 2004, 43:5109-5118.
    • (2004) Biochemistry , vol.43 , pp. 5109-5118
    • Wilken, J.A.1    Bedows, E.2
  • 17
    • 0037147191 scopus 로고    scopus 로고
    • Coordinated nonvectorial folding in a newly synthesized multidomain protein
    • Jansens A., van Duijn E., Braakman I. Coordinated nonvectorial folding in a newly synthesized multidomain protein. Science 2002, 298:2401-2403.
    • (2002) Science , vol.298 , pp. 2401-2403
    • Jansens, A.1    van Duijn, E.2    Braakman, I.3
  • 18
    • 77953148190 scopus 로고    scopus 로고
    • ERp44 and ERGIC-53 synergize in coupling efficiency and fidelity of IgM polymerization and secretion
    • Cortini M., Sitia R. ERp44 and ERGIC-53 synergize in coupling efficiency and fidelity of IgM polymerization and secretion. Traffic 2010, 11:651-659.
    • (2010) Traffic , vol.11 , pp. 651-659
    • Cortini, M.1    Sitia, R.2
  • 19
    • 0030265732 scopus 로고    scopus 로고
    • Ig light chains are secreted predominantly as monomers
    • Dul J.L., Aviel S., Melnick J., Argon Y. Ig light chains are secreted predominantly as monomers. J Immunol 1996, 157:2969-2975.
    • (1996) J Immunol , vol.157 , pp. 2969-2975
    • Dul, J.L.1    Aviel, S.2    Melnick, J.3    Argon, Y.4
  • 20
    • 70649093102 scopus 로고    scopus 로고
    • Intracellular assembly and trafficking of MHC class I molecules
    • Donaldson J.G., Williams D.B. Intracellular assembly and trafficking of MHC class I molecules. Traffic 2009, 10:1745-1752.
    • (2009) Traffic , vol.10 , pp. 1745-1752
    • Donaldson, J.G.1    Williams, D.B.2
  • 21
    • 0031038002 scopus 로고    scopus 로고
    • Assembly of immunoglobulin light chains as a prerequisite for secretion. A model for oligomerization-dependent subunit folding
    • Leitzgen K., Knittler M.R., Haas I.G. Assembly of immunoglobulin light chains as a prerequisite for secretion. A model for oligomerization-dependent subunit folding. J Biol Chem 1997, 272:3117-3123.
    • (1997) J Biol Chem , vol.272 , pp. 3117-3123
    • Leitzgen, K.1    Knittler, M.R.2    Haas, I.G.3
  • 22
    • 58249094358 scopus 로고    scopus 로고
    • HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein β2-microglobulin upon release from the MHC-1
    • Hodkinson J.P., Jahn T.R., Radford S.E., Ashcroft A.E. HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein β2-microglobulin upon release from the MHC-1. J Am Soc Mass Spectrom 2009, 20:278-286.
    • (2009) J Am Soc Mass Spectrom , vol.20 , pp. 278-286
    • Hodkinson, J.P.1    Jahn, T.R.2    Radford, S.E.3    Ashcroft, A.E.4
  • 23
    • 0023096246 scopus 로고
    • Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein
    • Hendershot L., Bole D., Kohler G., Kearney J.F. Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein. J Cell Biol 1987, 104:761-767.
    • (1987) J Cell Biol , vol.104 , pp. 761-767
    • Hendershot, L.1    Bole, D.2    Kohler, G.3    Kearney, J.F.4
  • 24
    • 0027081774 scopus 로고
    • Analysis in vivo of GRP78-BiP/substrate interactions and their role in induction of the GRP78-BiP gene
    • Ng D.T., Watowich S.S., Lamb R.A. Analysis in vivo of GRP78-BiP/substrate interactions and their role in induction of the GRP78-BiP gene. Mol Biol Cell 1992, 3:143-155.
    • (1992) Mol Biol Cell , vol.3 , pp. 143-155
    • Ng, D.T.1    Watowich, S.S.2    Lamb, R.A.3
  • 25
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: endoplasmic reticulum-associated degradation
    • Vembar S.S., Brodsky J.L. One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 2008, 9:944-957.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 26
    • 9044240065 scopus 로고
    • Low cyst(e)ine content of bacterial extracellular proteins: its possible physiological significance
    • Pollocl M.R., Richmond M.H. Low cyst(e)ine content of bacterial extracellular proteins: its possible physiological significance. Nature 1962, 194:446-449.
    • (1962) Nature , vol.194 , pp. 446-449
    • Pollocl, M.R.1    Richmond, M.H.2
  • 27
    • 0017747006 scopus 로고
    • On the cysteine and cystine content of proteins. Differences between intracellular and extracellular proteins
    • Fahey R.C., Hunt J.S., Windham G.C. On the cysteine and cystine content of proteins. Differences between intracellular and extracellular proteins. J Mol Evol 1977, 10:155-160.
    • (1977) J Mol Evol , vol.10 , pp. 155-160
    • Fahey, R.C.1    Hunt, J.S.2    Windham, G.C.3
  • 28
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C., Sinskey A.J., Lodish H.F. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 1992, 257:1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 29
    • 77954173918 scopus 로고    scopus 로고
    • Oxidative folding in the endoplasmic reticulum: towards a multiple oxidant hypothesis?
    • Margittai E., Banhegyi G. Oxidative folding in the endoplasmic reticulum: towards a multiple oxidant hypothesis?. FEBS Lett 2010, 584:2995-2998.
    • (2010) FEBS Lett , vol.584 , pp. 2995-2998
    • Margittai, E.1    Banhegyi, G.2
  • 30
    • 1242294484 scopus 로고    scopus 로고
    • A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein
    • Bass R., Ruddock L.W., Klappa P., Freedman R.B. A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein. J Biol Chem 2004, 279:5257-5262.
    • (2004) J Biol Chem , vol.279 , pp. 5257-5262
    • Bass, R.1    Ruddock, L.W.2    Klappa, P.3    Freedman, R.B.4
  • 31
    • 0036862532 scopus 로고    scopus 로고
    • The FAD- and O2-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum
    • Tu B.P., Weissman J.S. The FAD- and O2-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum. Mol Cell 2002, 10:983-994.
    • (2002) Mol Cell , vol.10 , pp. 983-994
    • Tu, B.P.1    Weissman, J.S.2
  • 32
    • 41449116766 scopus 로고    scopus 로고
    • Ero1 and redox homeostasis in the endoplasmic reticulum
    • Sevier C.S., Kaiser C.A. Ero1 and redox homeostasis in the endoplasmic reticulum. Biochim Biophys Acta 2008, 1783:549-556.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 549-556
    • Sevier, C.S.1    Kaiser, C.A.2
  • 33
    • 41549159471 scopus 로고    scopus 로고
    • The human PDI family: versatility packed into a single fold
    • Appenzeller-Herzog C., Ellgaard L. The human PDI family: versatility packed into a single fold. Biochim Biophys Acta 2008, 1783:535-548.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 535-548
    • Appenzeller-Herzog, C.1    Ellgaard, L.2
  • 35
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: substrate interactions and functional properties
    • Ellgaard L., Ruddock L.W. The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep 2005, 6:28-32.
    • (2005) EMBO Rep , vol.6 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 36
    • 71549132149 scopus 로고    scopus 로고
    • Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation
    • Hatahet F., Ruddock L.W. Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxid Redox Signal 2009, 11:2807-2850.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2807-2850
    • Hatahet, F.1    Ruddock, L.W.2
  • 37
    • 0035890070 scopus 로고    scopus 로고
    • Manipulation of oxidative protein folding and PDI redox state in mammalian cells
    • Mezghrani A., Fassio A., Benham A., Simmen T., Braakman I., Sitia R. Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J 2001, 20:6288-6296.
    • (2001) EMBO J , vol.20 , pp. 6288-6296
    • Mezghrani, A.1    Fassio, A.2    Benham, A.3    Simmen, T.4    Braakman, I.5    Sitia, R.6
  • 38
    • 33645784167 scopus 로고    scopus 로고
    • The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress
    • Chakravarthi S., Jessop C.E., Bulleid N.J. The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress. EMBO Rep 2006, 7:271-275.
    • (2006) EMBO Rep , vol.7 , pp. 271-275
    • Chakravarthi, S.1    Jessop, C.E.2    Bulleid, N.J.3
  • 39
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: building bridges in protein folding
    • Freedman R.B., Hirst T.R., Tuite M.F. Protein disulphide isomerase: building bridges in protein folding. Trends Biochem Sci 1994, 19:331-336.
    • (1994) Trends Biochem Sci , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 40
    • 0033213605 scopus 로고    scopus 로고
    • Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
    • Frand A.R., Kaiser C.A. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 1999, 4:469-477.
    • (1999) Mol Cell , vol.4 , pp. 469-477
    • Frand, A.R.1    Kaiser, C.A.2
  • 41
  • 42
    • 0034604675 scopus 로고    scopus 로고
    • Endoplasmic reticulum oxidoreductin 1-lβ (ERO1-Lβ), a human gene induced in the course of the unfolded protein response
    • Pagani M., Fabbri M., Benedetti C., Fassio A., Pilati S., Bulleid N.J., Cabibbo A., Sitia R. Endoplasmic reticulum oxidoreductin 1-lβ (ERO1-Lβ), a human gene induced in the course of the unfolded protein response. J Biol Chem 2000, 275:23685-23692.
    • (2000) J Biol Chem , vol.275 , pp. 23685-23692
    • Pagani, M.1    Fabbri, M.2    Benedetti, C.3    Fassio, A.4    Pilati, S.5    Bulleid, N.J.6    Cabibbo, A.7    Sitia, R.8
  • 43
    • 77957773053 scopus 로고    scopus 로고
    • Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI
    • Inaba K., Masui S., Iida H., Vavassori S., Sitia R., Suzuki M. Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI. EMBO J 2010.
    • (2010) EMBO J
    • Inaba, K.1    Masui, S.2    Iida, H.3    Vavassori, S.4    Sitia, R.5    Suzuki, M.6
  • 46
    • 33846192436 scopus 로고    scopus 로고
    • ERp57 is essential for efficient folding of glycoproteins sharing common structural domains
    • Jessop C.E., Chakravarthi S., Garbi N., Hammerling G.J., Lovell S., Bulleid N.J. ERp57 is essential for efficient folding of glycoproteins sharing common structural domains. EMBO J 2007, 26:28-40.
    • (2007) EMBO J , vol.26 , pp. 28-40
    • Jessop, C.E.1    Chakravarthi, S.2    Garbi, N.3    Hammerling, G.J.4    Lovell, S.5    Bulleid, N.J.6
  • 47
    • 59049105293 scopus 로고    scopus 로고
    • Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin
    • Jessop C.E., Tavender T.J., Watkins R.H., Chambers J.E., Bulleid N.J. Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin. J Biol Chem 2009, 284:2194-2202.
    • (2009) J Biol Chem , vol.284 , pp. 2194-2202
    • Jessop, C.E.1    Tavender, T.J.2    Watkins, R.H.3    Chambers, J.E.4    Bulleid, N.J.5
  • 49
    • 77951230456 scopus 로고    scopus 로고
    • Novel thioredoxin-related transmembrane protein TMX4 has reductase activity
    • Sugiura Y., Araki K., Iemura S., Natsume T., Hoseki J., Nagata K. Novel thioredoxin-related transmembrane protein TMX4 has reductase activity. J Biol Chem 2010, 285:7135-7142.
    • (2010) J Biol Chem , vol.285 , pp. 7135-7142
    • Sugiura, Y.1    Araki, K.2    Iemura, S.3    Natsume, T.4    Hoseki, J.5    Nagata, K.6
  • 50
    • 77956514975 scopus 로고    scopus 로고
    • The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α
    • Chambers J.E., Tavender T.J., Oka O.B., Warwood S., Knight D., Bulleid N.J. The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α. J Biol Chem 2010, 285:29200-29207.
    • (2010) J Biol Chem , vol.285 , pp. 29200-29207
    • Chambers, J.E.1    Tavender, T.J.2    Oka, O.B.3    Warwood, S.4    Knight, D.5    Bulleid, N.J.6
  • 51
    • 12544251988 scopus 로고    scopus 로고
    • PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum
    • van Lith M., Hartigan N., Hatch J., Benham A.M. PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum. J Biol Chem 2005, 280:1376-1383.
    • (2005) J Biol Chem , vol.280 , pp. 1376-1383
    • van Lith, M.1    Hartigan, N.2    Hatch, J.3    Benham, A.M.4
  • 52
    • 0030068301 scopus 로고    scopus 로고
    • Characterization and chromosomal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas
    • Desilva M.G., Lu J., Donadel G., Modi W.S., Xie H., Notkins A.L., Lan M.S. Characterization and chromosomal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas. DNA Cell Biol 1996, 15:9-16.
    • (1996) DNA Cell Biol , vol.15 , pp. 9-16
    • Desilva, M.G.1    Lu, J.2    Donadel, G.3    Modi, W.S.4    Xie, H.5    Notkins, A.L.6    Lan, M.S.7
  • 53
    • 48249117110 scopus 로고    scopus 로고
    • ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
    • Ushioda R, Hoseki J., Araki K., Jansen G., Thomas D.Y., Nagata K. ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 2008, 321:569-572.
    • (2008) Science , vol.321 , pp. 569-572
    • Ushioda, R.1    Hoseki, J.2    Araki, K.3    Jansen, G.4    Thomas, D.Y.5    Nagata, K.6
  • 54
    • 0032807338 scopus 로고    scopus 로고
    • ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin
    • Oliver J.D., Roderick H.L., Llewellyn D.H., High S. ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol Biol Cell 1999, 10:2573-2582.
    • (1999) Mol Biol Cell , vol.10 , pp. 2573-2582
    • Oliver, J.D.1    Roderick, H.L.2    Llewellyn, D.H.3    High, S.4
  • 55
    • 0035805615 scopus 로고    scopus 로고
    • Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells
    • Korotkov K.V., Kumaraswamy E., Zhou Y., Hatfield D.L., Gladyshev V.N. Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells. J Biol Chem 2001, 276:15330-15336.
    • (2001) J Biol Chem , vol.276 , pp. 15330-15336
    • Korotkov, K.V.1    Kumaraswamy, E.2    Zhou, Y.3    Hatfield, D.L.4    Gladyshev, V.N.5
  • 56
    • 69749100361 scopus 로고    scopus 로고
    • Sep15, a thioredoxin-like selenoprotein, is involved in the unfolded protein response and differentially regulated by adaptive and acute ER stresses
    • Labunskyy V.M., Yoo M.H., Hatfield D.L., Gladyshev V.N. Sep15, a thioredoxin-like selenoprotein, is involved in the unfolded protein response and differentially regulated by adaptive and acute ER stresses. Biochemistry 2009, 48:8458-8465.
    • (2009) Biochemistry , vol.48 , pp. 8458-8465
    • Labunskyy, V.M.1    Yoo, M.H.2    Hatfield, D.L.3    Gladyshev, V.N.4
  • 57
    • 70849101711 scopus 로고    scopus 로고
    • Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins
    • Jessop C.E., Watkins R.H., Simmons J.J., Tasab M., Bulleid N.J. Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins. J Cell Sci 2009, 122:4287-4295.
    • (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
  • 58
    • 77956684691 scopus 로고    scopus 로고
    • Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins
    • Rutkevich L.A., Cohen-Doyle M.F., Brockmeier U., Williams D.B. Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins. Mol Biol Cell 2010, 21:3093-3105.
    • (2010) Mol Biol Cell , vol.21 , pp. 3093-3105
    • Rutkevich, L.A.1    Cohen-Doyle, M.F.2    Brockmeier, U.3    Williams, D.B.4
  • 59
    • 70349855203 scopus 로고    scopus 로고
    • Glycoprotein folding, quality control and ER-associated degradation
    • Lederkremer G.Z. Glycoprotein folding, quality control and ER-associated degradation. Curr Opin Struct Biol 2009, 19:515-523.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 515-523
    • Lederkremer, G.Z.1
  • 63
    • 0025146994 scopus 로고
    • Secretion of immunoglobulin M assembly intermediates in the presence of reducing agents
    • Alberini C.M., Bet P., Milstein C., Sitia R. Secretion of immunoglobulin M assembly intermediates in the presence of reducing agents. Nature 1990, 347:485-487.
    • (1990) Nature , vol.347 , pp. 485-487
    • Alberini, C.M.1    Bet, P.2    Milstein, C.3    Sitia, R.4
  • 64
    • 0028588562 scopus 로고
    • The differential effects of dithiothreitol and 2-mercaptoethanol on the secretion of partially and completely assembled immunoglobulins suggest that thiol-mediated retention does not take place in or beyond the Golgi
    • Valetti C., Sitia R. The differential effects of dithiothreitol and 2-mercaptoethanol on the secretion of partially and completely assembled immunoglobulins suggest that thiol-mediated retention does not take place in or beyond the Golgi. Mol Biol Cell 1994, 5:1311-1324.
    • (1994) Mol Biol Cell , vol.5 , pp. 1311-1324
    • Valetti, C.1    Sitia, R.2
  • 65
    • 0037083869 scopus 로고    scopus 로고
    • ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family
    • Anelli T., Alessio M., Mezghrani A., Simmen T., Talamo F., Bachi A., Sitia R. ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J 2002, 21:835-844.
    • (2002) EMBO J , vol.21 , pp. 835-844
    • Anelli, T.1    Alessio, M.2    Mezghrani, A.3    Simmen, T.4    Talamo, F.5    Bachi, A.6    Sitia, R.7
  • 66
    • 44449129593 scopus 로고    scopus 로고
    • ERp44 mediates a thiol-independent retention of formylglycine-generating enzyme in the endoplasmic reticulum
    • Mariappan M., Radhakrishnan K., Dierks T., Schmidt B., von Figura K. ERp44 mediates a thiol-independent retention of formylglycine-generating enzyme in the endoplasmic reticulum. J Biol Chem 2008, 283:6375-6383.
    • (2008) J Biol Chem , vol.283 , pp. 6375-6383
    • Mariappan, M.1    Radhakrishnan, K.2    Dierks, T.3    Schmidt, B.4    von Figura, K.5
  • 67
    • 38949125405 scopus 로고    scopus 로고
    • Post-translational modifications of adiponectin: mechanisms and functional implications
    • Wang Y., Lam K.S., Yau M.H., Xu A. Post-translational modifications of adiponectin: mechanisms and functional implications. Biochem J 2008, 409:623-633.
    • (2008) Biochem J , vol.409 , pp. 623-633
    • Wang, Y.1    Lam, K.S.2    Yau, M.H.3    Xu, A.4
  • 69
    • 0036198797 scopus 로고    scopus 로고
    • Protein disulfide isomerases exploit synergy between catalytic and specific binding domains
    • Freedman R.B., Klappa P., Ruddock L.W. Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO Rep 2002, 3:136-140.
    • (2002) EMBO Rep , vol.3 , pp. 136-140
    • Freedman, R.B.1    Klappa, P.2    Ruddock, L.W.3
  • 70
    • 0032481380 scopus 로고    scopus 로고
    • The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
    • Klappa P., Ruddock L.W., Darby N.J., Freedman R.B. The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J 1998, 17:927-935.
    • (1998) EMBO J , vol.17 , pp. 927-935
    • Klappa, P.1    Ruddock, L.W.2    Darby, N.J.3    Freedman, R.B.4
  • 71
    • 4444265582 scopus 로고    scopus 로고
    • Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death
    • Haynes C.M., Titus E.A., Cooper A.A. Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death. Mol Cell 2004, 15:767-776.
    • (2004) Mol Cell , vol.15 , pp. 767-776
    • Haynes, C.M.1    Titus, E.A.2    Cooper, A.A.3
  • 73
    • 77954225337 scopus 로고    scopus 로고
    • A small molecule inhibitor of endoplasmic reticulum oxidation 1 (ERO1) with selectively reversible thiol reactivity
    • Blais J.D., Chin K.T., Zito E., Zhang Y., Heldman N., Harding H.P., Fass D., Thorpe C., Ron D. A small molecule inhibitor of endoplasmic reticulum oxidation 1 (ERO1) with selectively reversible thiol reactivity. J Biol Chem 2010, 285:20993-21003.
    • (2010) J Biol Chem , vol.285 , pp. 20993-21003
    • Blais, J.D.1    Chin, K.T.2    Zito, E.3    Zhang, Y.4    Heldman, N.5    Harding, H.P.6    Fass, D.7    Thorpe, C.8    Ron, D.9
  • 74
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1-α-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis
    • Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R., Tabas I. Role of ERO1-α-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J Cell Biol 2009, 186:783-792.
    • (2009) J Cell Biol , vol.186 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3    Harding, H.4    Ron, D.5    Marks, A.R.6    Tabas, I.7
  • 75
    • 68949196897 scopus 로고    scopus 로고
    • Oxidative folding: cellular strategies for dealing with the resultant equimolar production of reactive oxygen species
    • Shimizu Y., Hendershot L.M. Oxidative folding: cellular strategies for dealing with the resultant equimolar production of reactive oxygen species. Antioxid Redox Signal 2009, 11:2317-2331.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2317-2331
    • Shimizu, Y.1    Hendershot, L.M.2
  • 77
    • 34147126077 scopus 로고    scopus 로고
    • Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1
    • Sevier C.S., Qu H., Heldman N., Gross E., Fass D., Kaiser C.A. Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1. Cell 2007, 129:333-344.
    • (2007) Cell , vol.129 , pp. 333-344
    • Sevier, C.S.1    Qu, H.2    Heldman, N.3    Gross, E.4    Fass, D.5    Kaiser, C.A.6
  • 78
    • 56549083161 scopus 로고    scopus 로고
    • A novel disulphide switch mechanism in Ero1α balances ER oxidation in human cells
    • Appenzeller-Herzog C., Riemer J., Christensen B., Sorensen E.S., Ellgaard L. A novel disulphide switch mechanism in Ero1α balances ER oxidation in human cells. EMBO J 2008, 27:2977-2987.
    • (2008) EMBO J , vol.27 , pp. 2977-2987
    • Appenzeller-Herzog, C.1    Riemer, J.2    Christensen, B.3    Sorensen, E.S.4    Ellgaard, L.5
  • 79
    • 77949716997 scopus 로고    scopus 로고
    • ERO1-β, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis
    • Zito E., Chin K.T., Blais J., Harding H.P., Ron D. ERO1-β, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis. J Cell Biol 2010, 188:821-832.
    • (2010) J Cell Biol , vol.188 , pp. 821-832
    • Zito, E.1    Chin, K.T.2    Blais, J.3    Harding, H.P.4    Ron, D.5
  • 80
    • 70350129433 scopus 로고    scopus 로고
    • PERp1 is significantly up-regulated during plasma cell differentiation and contributes to the oxidative folding of immunoglobulin
    • Shimizu Y., Meunier L., Hendershot L.M. pERp1 is significantly up-regulated during plasma cell differentiation and contributes to the oxidative folding of immunoglobulin. Proc Natl Acad Sci USA 2009, 106:17013-17018.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 17013-17018
    • Shimizu, Y.1    Meunier, L.2    Hendershot, L.M.3
  • 82
    • 0034790475 scopus 로고    scopus 로고
    • A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation
    • Sevier C.S., Cuozzo J.W., Vala A., Aslund F., Kaiser C.A. A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat Cell Biol 2001, 3:874-882.
    • (2001) Nat Cell Biol , vol.3 , pp. 874-882
    • Sevier, C.S.1    Cuozzo, J.W.2    Vala, A.3    Aslund, F.4    Kaiser, C.A.5
  • 83
    • 79954426157 scopus 로고    scopus 로고
    • Signaling cell death from the endoplasmic reticulum stress response
    • Shore G.C., Papa F.R., Oakes S.A. Signaling cell death from the endoplasmic reticulum stress response. Curr Opin Cell Biol 2011, 23:143-149.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 143-149
    • Shore, G.C.1    Papa, F.R.2    Oakes, S.A.3
  • 84
    • 79954421129 scopus 로고    scopus 로고
    • Proteostenosis and plasma cell pathophysiology
    • Cenci S., van Anken E., Sitia R. Proteostenosis and plasma cell pathophysiology. Curr Opin Cell Biol 2011, 23:216-222.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 216-222
    • Cenci, S.1    van Anken, E.2    Sitia, R.3
  • 85
    • 79954421252 scopus 로고    scopus 로고
    • Oxidative protein folding by an endoplasmic reticulum localized peroxiredoxin. Mol Cell, in press.
    • Zito E, Melo EP, Yang Y, Wahlander A, Neubert TA, Ron D: Oxidative protein folding by an endoplasmic reticulum localized peroxiredoxin. Mol Cell, in press.
    • Zito, E.1    Melo, E.P.2    Yang, Y.3    Wahlander, A.4    Neubert, T.A.5    Ron, D.6
  • 86
    • 77956313447 scopus 로고    scopus 로고
    • Oxidative protein folding and the quiescin-sulfhydryl oxidase family of flavoproteins
    • Kodali V.K., Thorpe C. Oxidative protein folding and the quiescin-sulfhydryl oxidase family of flavoproteins. Antioxid Redox Signal 2010, 13:1217-1230.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1217-1230
    • Kodali, V.K.1    Thorpe, C.2
  • 88
    • 64549156522 scopus 로고    scopus 로고
    • Efficient peroxide-mediated oxidative refolding of a protein at physiological pH and implications for oxidative folding in the endoplasmic reticulum
    • Karala A.R., Lappi A.K., Saaranen M.J., Ruddock L.W. Efficient peroxide-mediated oxidative refolding of a protein at physiological pH and implications for oxidative folding in the endoplasmic reticulum. Antioxid Redox Signal 2009, 11:963-970.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 963-970
    • Karala, A.R.1    Lappi, A.K.2    Saaranen, M.J.3    Ruddock, L.W.4
  • 89
    • 77955359156 scopus 로고    scopus 로고
    • Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation
    • Tavender T.J., Bulleid N.J. Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation. J Cell Sci 2010.
    • (2010) J Cell Sci
    • Tavender, T.J.1    Bulleid, N.J.2
  • 91
    • 78650270477 scopus 로고    scopus 로고
    • Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum. EMBO J, Nov 5. [Epub ahead of print].
    • Tavender TJ, Springate JF, Bulleid NJ: Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum. EMBO J, 2010 Nov 5. [Epub ahead of print].
    • (2010)
    • Tavender, T.J.1    Springate, J.F.2    Bulleid, N.J.3
  • 92
    • 79954423932 scopus 로고    scopus 로고
    • Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells
    • Finka A., Mattoo R.U., Goloubinoff P. Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells. Cell Stress Chaperones 2010.
    • (2010) Cell Stress Chaperones
    • Finka, A.1    Mattoo, R.U.2    Goloubinoff, P.3
  • 93
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: integrators of cell stress, development and lifespan
    • Akerfelt M., Morimoto R.I., Sistonen L. Heat shock factors: integrators of cell stress, development and lifespan. Nat Rev Mol Cell Biol 2010, 11:545-555.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 545-555
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 94
    • 36249022750 scopus 로고    scopus 로고
    • Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp
    • Okuda-Shimizu Y., Hendershot L.M. Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp. Mol Cell 2007, 28:544-554.
    • (2007) Mol Cell , vol.28 , pp. 544-554
    • Okuda-Shimizu, Y.1    Hendershot, L.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.