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Volumn 19, Issue 3, 2014, Pages 222-240

Protein disulfide isomerase: A promising target for cancer therapy

Author keywords

[No Author keywords available]

Indexed keywords

4,4' ISOPROPYLIDENEDIPHENOL; 5,5' DITHIOBIS(2 NITROBENZOIC ACID); ACROLEIN; ANTIBIOTIC AGENT; ARSENOSOBENZENE; BACITRACIN; BACITRACIN B; BACITRACIN F; BACITRACIN H; BACOTRACIN A; CHAPERONE; CHLOROMERCURIBENZENESULFONIC ACID; CYSTAMINE; ENZYME INHIBITOR; ESTRADIOL; ESTROGEN; ESTRONE; IODOACETAMINDE; LIOTHYRONINE; N ETHYLMALEIMIDE; PROPYNOIC ACID CARBAMOYL METHYL AMIDE; PROTEIN DISULFIDE ISOMERASE; PROTEIN DISULFIDE ISOMERASE INHIBITOR; RIBOSTAMYCIN; RUTOSIDE; THIOL DERIVATIVE; THIOMUSCIMOL; UNCLASSIFIED DRUG; ANTINEOPLASTIC AGENT;

EID: 84896394053     PISSN: 13596446     EISSN: 18785832     Source Type: Journal    
DOI: 10.1016/j.drudis.2013.10.017     Document Type: Review
Times cited : (211)

References (182)
  • 1
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulphide-isomerase family: Unravelling a string of folds
    • DOI 10.1042/0264-6021:3390001
    • D.M. Ferrari, and H.D. Soling The protein disulphide-isomerase family: unravelling a string of folds Biochem. J. 339 Pt 1 1999 1 10 (Pubitemid 29179283)
    • (1999) Biochemical Journal , vol.339 , Issue.1 , pp. 1-10
    • Ferrari, D.M.1    Soling, H.-D.2
  • 2
    • 0142019685 scopus 로고
    • The enzymatic reactivation of reduced ribonuclease
    • P. Venetianer, and F.B. Straub The enzymatic reactivation of reduced ribonuclease Biochim. Biophys. Acta 67 1963 166 168
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 166-168
    • Venetianer, P.1    Straub, F.B.2
  • 3
    • 73649177752 scopus 로고
    • Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver
    • R.F. Goldberger et al. Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver J. Biol. Chem. 238 1963 628 635
    • (1963) J. Biol. Chem. , vol.238 , pp. 628-635
    • Goldberger, R.F.1
  • 4
    • 0016773552 scopus 로고
    • Randomly reoxidised soybean trypsin inhibitor and the possibility of conformational barriers to disulphide isomerization in proteins
    • H.C. Hawkins, and R.B. Freedman Randomly reoxidised soybean trypsin inhibitor and the possibility of conformational barriers to disulphide isomerization in proteins FEBS Lett. 58 1975 7 11
    • (1975) FEBS Lett. , vol.58 , pp. 7-11
    • Hawkins, H.C.1    Freedman, R.B.2
  • 5
    • 77956625219 scopus 로고    scopus 로고
    • A structural overview of the PDI family of proteins
    • G. Kozlov et al. A structural overview of the PDI family of proteins FEBS J. 277 2010 3924 3936
    • (2010) FEBS J. , vol.277 , pp. 3924-3936
    • Kozlov, G.1
  • 6
    • 71549132149 scopus 로고    scopus 로고
    • Protein disulfide isomerase: A critical evaluation of its function in disulfide bond formation
    • F. Hatahet, and L.W. Ruddock Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation Antioxid. Redox Signal. 11 2009 2807 2850
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2807-2850
    • Hatahet, F.1    Ruddock, L.W.2
  • 7
    • 55849088319 scopus 로고    scopus 로고
    • Regulation of MHC class i assembly and peptide binding
    • D.R. Peaper, and P. Cresswell Regulation of MHC class I assembly and peptide binding Annu. Rev. Cell Dev. Biol. 24 2008 343 368
    • (2008) Annu. Rev. Cell Dev. Biol. , vol.24 , pp. 343-368
    • Peaper, D.R.1    Cresswell, P.2
  • 9
    • 0023654667 scopus 로고
    • A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase
    • J. Koivu et al. A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase J. Biol. Chem. 262 1987 6447 6449
    • (1987) J. Biol. Chem. , vol.262 , pp. 6447-6449
    • Koivu, J.1
  • 10
    • 0026052386 scopus 로고
    • Protein disulfide isomerase appears necessary to maintain the catalytically active structure of the microsomal triglyceride transfer protein
    • J.R. Wetterau et al. Protein disulfide isomerase appears necessary to maintain the catalytically active structure of the microsomal triglyceride transfer protein Biochemistry 30 1991 9728 9735
    • (1991) Biochemistry , vol.30 , pp. 9728-9735
    • Wetterau, J.R.1
  • 11
    • 84857530189 scopus 로고    scopus 로고
    • The protein disulfide isomerase family: Key players in health and disease
    • A.M. Benham The protein disulfide isomerase family: key players in health and disease Antioxid. Redox Signal. 16 2012 781 789
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 781-789
    • Benham, A.M.1
  • 15
    • 78649246847 scopus 로고    scopus 로고
    • Inhibitors of protein disulfide isomerase suppress apoptosis induced by misfolded proteins
    • B.G. Hoffstrom et al. Inhibitors of protein disulfide isomerase suppress apoptosis induced by misfolded proteins Nat. Chem. Biol. 6 2010 900 906
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 900-906
    • Hoffstrom, B.G.1
  • 16
    • 0034917294 scopus 로고    scopus 로고
    • Enhanced protein levels of protein thiol/disulphide oxidoreductases in placentae from pre-eclamptic subjects
    • DOI 10.1053/plac.2001.0693
    • E. Shibata et al. Enhanced protein levels of protein thiol/disulphide oxidoreductases in placentae from pre-eclamptic subjects Placenta 22 2001 566 572 (Pubitemid 32700841)
    • (2001) Placenta , vol.22 , Issue.6 , pp. 566-572
    • Shibata, E.1    Ejima, K.2    Nanri, H.3    Toki, N.4    Koyama, C.5    Ikeda, M.6    Kashimura, M.7
  • 18
    • 34347357589 scopus 로고    scopus 로고
    • Proteomic analysis of proteins differentially expressed in preeclamptic trophoblasts
    • L.Z. Sun et al. Proteomic analysis of proteins differentially expressed in preeclamptic trophoblasts Gynecol. Obstet. Invest. 64 2007 17 23
    • (2007) Gynecol. Obstet. Invest. , vol.64 , pp. 17-23
    • Sun, L.Z.1
  • 19
    • 41349119823 scopus 로고    scopus 로고
    • Novel role of protein disulfide isomerase in the regulation of NADPH oxidase activity: Pathophysiological implications in vascular diseases
    • DOI 10.1089/ars.2007.2011
    • F.R. Laurindo et al. Novel role of protein disulfide isomerase in the regulation of NADPH oxidase activity: pathophysiological implications in vascular diseases Antioxid. Redox Signal. 10 2008 1101 1113 (Pubitemid 351451715)
    • (2008) Antioxidants and Redox Signaling , vol.10 , Issue.6 , pp. 1101-1113
    • Laurindo, F.R.M.1    Fernandes, D.C.2    Amanso, A.M.3    Lopes, L.R.4    Santos, C.X.C.5
  • 20
    • 0033593450 scopus 로고    scopus 로고
    • Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase
    • X.M. Jiang et al. Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase J. Biol. Chem. 274 1999 2416 2423
    • (1999) J. Biol. Chem. , vol.274 , pp. 2416-2423
    • Jiang, X.M.1
  • 21
    • 0034495137 scopus 로고    scopus 로고
    • Presence of closely spaced protein thiols on the surface of mammalian cells
    • N. Donoghue et al. Presence of closely spaced protein thiols on the surface of mammalian cells Protein Sci. 9 2000 2436 2445 (Pubitemid 32105726)
    • (2000) Protein Science , vol.9 , Issue.12 , pp. 2436-2445
    • Donoghue, N.1    Yam, P.T.W.2    Jiang, X.-M.3    Hogg, P.J.4
  • 22
    • 0029163450 scopus 로고
    • Secretion, surface localization, turnover, and steady state expression of protein disulfide isomerase in rat hepatocytes
    • K. Terada et al. Secretion, surface localization, turnover, and steady state expression of protein disulfide isomerase in rat hepatocytes J. Biol. Chem. 270 1995 20410 20416
    • (1995) J. Biol. Chem. , vol.270 , pp. 20410-20416
    • Terada, K.1
  • 23
    • 79960601577 scopus 로고    scopus 로고
    • Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry
    • S. Bi et al. Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry Proc. Natl. Acad. Sci. U. S. A. 108 2011 10650 10655
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 10650-10655
    • Bi, S.1
  • 24
    • 77954902619 scopus 로고    scopus 로고
    • Thiol isomerases negatively regulate the cellular shedding activity of ADAM17
    • S.H. Willems et al. Thiol isomerases negatively regulate the cellular shedding activity of ADAM17 Biochem. J. 428 2010 439 450
    • (2010) Biochem. J. , vol.428 , pp. 439-450
    • Willems, S.H.1
  • 25
    • 77956533379 scopus 로고    scopus 로고
    • Extracellular protein disulfide isomerase regulates coagulation on endothelial cells through modulation of phosphatidylserine exposure
    • N.I. Popescu et al. Extracellular protein disulfide isomerase regulates coagulation on endothelial cells through modulation of phosphatidylserine exposure Blood 116 2010 993 1001
    • (2010) Blood , vol.116 , pp. 993-1001
    • Popescu, N.I.1
  • 28
    • 0032985071 scopus 로고    scopus 로고
    • Protein disulphide isomerase mediates platelet aggregation and secretion
    • D.W. Essex, and M. Li Protein disulphide isomerase mediates platelet aggregation and secretion Br. J. Haematol. 104 1999 448 454 (Pubitemid 29119264)
    • (1999) British Journal of Haematology , vol.104 , Issue.3 , pp. 448-454
    • Essex, D.W.1    Li, M.2
  • 29
    • 0035918587 scopus 로고    scopus 로고
    • Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation
    • DOI 10.1021/bi002454e
    • D.W. Essex et al. Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation Biochemistry 40 2001 6070 6075 (Pubitemid 32466310)
    • (2001) Biochemistry , vol.40 , Issue.20 , pp. 6070-6075
    • Essex, D.W.1    Li, M.2    Miller, A.3    Feinman, R.D.4
  • 30
    • 40549084318 scopus 로고    scopus 로고
    • A critical role for extracellular protein disulfide isomerase during thrombus formation in mice
    • DOI 10.1172/JCI34134
    • J. Cho et al. A critical role for extracellular protein disulfide isomerase during thrombus formation in mice J. Clin. Invest. 118 2008 1123 1131 (Pubitemid 351364619)
    • (2008) Journal of Clinical Investigation , vol.118 , Issue.3 , pp. 1123-1131
    • Cho, J.1    Furie, B.C.2    Coughlin, S.R.3    Furie, B.4
  • 31
    • 77958522684 scopus 로고    scopus 로고
    • Effect of protein disulfide isomerase chaperone activity inhibition on tissue factor activity
    • A. Raturi, and W. Ruf Effect of protein disulfide isomerase chaperone activity inhibition on tissue factor activity J. Thromb. Haemost. 8 2010 1863 1865
    • (2010) J. Thromb. Haemost. , vol.8 , pp. 1863-1865
    • Raturi, A.1    Ruf, W.2
  • 32
    • 84883794015 scopus 로고    scopus 로고
    • Protein disulfide isomerase as an antithrombotic target
    • R. Flaumenhaft Protein disulfide isomerase as an antithrombotic target Trends Cardiovasc. Med. 23 2013 264 268
    • (2013) Trends Cardiovasc. Med. , vol.23 , pp. 264-268
    • Flaumenhaft, R.1
  • 34
    • 33847222149 scopus 로고    scopus 로고
    • Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein
    • S. Jain et al. Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein J. Virol. 81 2007 2328 2339
    • (2007) J. Virol. , vol.81 , pp. 2328-2339
    • Jain, S.1
  • 36
    • 81455143967 scopus 로고    scopus 로고
    • Protein disulfide isomerase and host-pathogen interaction
    • B.S. Stolf et al. Protein disulfide isomerase and host-pathogen interaction Sci. World J. 11 2011 1749 1761
    • (2011) Sci. World J. , vol.11 , pp. 1749-1761
    • Stolf, B.S.1
  • 38
    • 0037474328 scopus 로고    scopus 로고
    • Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion
    • DOI 10.1074/jbc.M205467200
    • R. Barbouche et al. Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion J. Biol. Chem. 278 2003 3131 3136 (Pubitemid 36801223)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.5 , pp. 3131-3136
    • Barbouche, R.1    Miquelis, R.2    Jones, I.M.3    Fenouillet, E.4
  • 39
    • 24944540240 scopus 로고    scopus 로고
    • Progress in targeting HIV-1 entry
    • H.J. Ryser, and R. Fluckiger Progress in targeting HIV-1 entry Drug Discov. Today 10 2005 1085 1094
    • (2005) Drug Discov. Today , vol.10 , pp. 1085-1094
    • Ryser, H.J.1    Fluckiger, R.2
  • 40
    • 0035367291 scopus 로고    scopus 로고
    • Distribution of protein disulphide isomerase in rat liver mitochondria
    • DOI 10.1042/0264-6021:3560567
    • M.P. Rigobello et al. Distribution of protein disulphide isomerase in rat liver mitochondria Biochem. J. 356 2001 567 570 (Pubitemid 32536819)
    • (2001) Biochemical Journal , vol.356 , Issue.2 , pp. 567-570
    • Rigobello, M.P.1    Donella-Deana, A.2    Cesaro, L.3    Bindoli, A.4
  • 41
    • 0036836665 scopus 로고    scopus 로고
    • Proteins of the PDI family: Unpredicted non-ER locations and functions
    • C. Turano et al. Proteins of the PDI family: unpredicted non-ER locations and functions J. Cell. Physiol. 193 2002 154 163
    • (2002) J. Cell. Physiol. , vol.193 , pp. 154-163
    • Turano, C.1
  • 43
    • 84862907646 scopus 로고    scopus 로고
    • Human protein disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a′
    • C. Wang et al. Human protein disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a′ J. Biol. Chem. 287 2012 1139 1149
    • (2012) J. Biol. Chem. , vol.287 , pp. 1139-1149
    • Wang, C.1
  • 44
    • 60349123960 scopus 로고    scopus 로고
    • Solution structure of the bb′ domains of human protein disulfide isomerase
    • A.Y. Denisov et al. Solution structure of the bb′ domains of human protein disulfide isomerase FEBS J. 276 2009 1440 1449
    • (2009) FEBS J. , vol.276 , pp. 1440-1449
    • Denisov, A.Y.1
  • 45
    • 53549090995 scopus 로고    scopus 로고
    • Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b′ domain
    • V.D. Nguyen et al. Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b′ domain J. Mol. Biol. 383 2008 1144 1155
    • (2008) J. Mol. Biol. , vol.383 , pp. 1144-1155
    • Nguyen, V.D.1
  • 47
    • 0029973729 scopus 로고    scopus 로고
    • Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy
    • J. Kemmink et al. Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy Biochemistry 35 1996 7684 7691
    • (1996) Biochemistry , vol.35 , pp. 7684-7691
    • Kemmink, J.1
  • 48
    • 84878866786 scopus 로고    scopus 로고
    • Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase
    • C. Wang et al. Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase Antioxid. Redox Signal. 19 2013 36 45
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 36-45
    • Wang, C.1
  • 49
    • 30344444015 scopus 로고    scopus 로고
    • The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites
    • DOI 10.1016/j.cell.2005.10.044, PII S0092867405014121
    • G. Tian et al. The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites Cell 124 2006 61 73 (Pubitemid 43069310)
    • (2006) Cell , vol.124 , Issue.1 , pp. 61-73
    • Tian, G.1    Xiang, S.2    Noiva, R.3    Lennarz, W.J.4    Schindelin, H.5
  • 50
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: Substrate interactions and functional properties
    • DOI 10.1038/sj.embor.7400311
    • L. Ellgaard, and L.W. Ruddock The human protein disulphide isomerase family: substrate interactions and functional properties EMBO Rep. 6 2005 28 32 (Pubitemid 41710070)
    • (2005) EMBO Reports , vol.6 , Issue.1 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 51
    • 34848927255 scopus 로고    scopus 로고
    • Substrate recognition by the protein disulfide isomerases
    • DOI 10.1111/j.1742-4658.2007.06058.x
    • F. Hatahet, and L.W. Ruddock Substrate recognition by the protein disulfide isomerases FEBS J. 274 2007 5223 5234 (Pubitemid 47512369)
    • (2007) FEBS Journal , vol.274 , Issue.20 , pp. 5223-5234
    • Hatahet, F.1    Ruddock, L.W.2
  • 52
    • 0026705344 scopus 로고
    • Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity
    • K. Vuori et al. Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity J. Biol. Chem. 267 1992 7211 7214
    • (1992) J. Biol. Chem. , vol.267 , pp. 7211-7214
    • Vuori, K.1
  • 53
    • 0029918154 scopus 로고    scopus 로고
    • PH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: Studies with a novel simple peptide substrate
    • L.W. Ruddock et al. pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: studies with a novel simple peptide substrate Biochem. J. 315 Pt 3 1996 1001 1005 (Pubitemid 26147634)
    • (1996) Biochemical Journal , vol.315 , Issue.3 , pp. 1001-1005
    • Ruddock, L.W.1    Hirst, T.R.2    Freedman, R.B.3
  • 54
    • 0030446158 scopus 로고    scopus 로고
    • Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase
    • DOI 10.1021/bi9617724
    • T. Kortemme et al. Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase Biochemistry 35 1996 14503 14511 (Pubitemid 26423709)
    • (1996) Biochemistry , vol.35 , Issue.46 , pp. 14503-14511
    • Kortemme, T.1    Darby, N.J.2    Creighton, T.E.3
  • 56
    • 77649275063 scopus 로고    scopus 로고
    • a allows PDI to act as a catalyst of both disulfide bond formation and isomerization
    • a allows PDI to act as a catalyst of both disulfide bond formation and isomerization J. Mol. Biol. 396 2010 883 892
    • (2010) J. Mol. Biol. , vol.396 , pp. 883-892
    • Karala, A.R.1
  • 57
    • 0030898705 scopus 로고    scopus 로고
    • Scanning and escape during protein-disulfide isomerase-assisted protein folding
    • DOI 10.1074/jbc.272.14.8845
    • K.W. Walker, and H.F. Gilbert Scanning and escape during protein-disulfide isomerase-assisted protein folding J. Biol. Chem. 272 1997 8845 8848 (Pubitemid 27154874)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 8845-8848
    • Walker, K.W.1    Gilbert, H.F.2
  • 58
    • 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
    • DOI 10.1093/emboj/17.4.927
    • P. Klappa et al. The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins EMBO J. 17 1998 927 935 (Pubitemid 28077647)
    • (1998) EMBO Journal , vol.17 , Issue.4 , pp. 927-935
    • Klappa, P.1    Ruddock, L.W.2    Darby, N.J.3    Freedman, R.B.4
  • 59
    • 77952680368 scopus 로고    scopus 로고
    • Bacitracin is not a specific inhibitor of protein disulfide isomerase
    • A.R. Karala, and L.W. Ruddock Bacitracin is not a specific inhibitor of protein disulfide isomerase FEBS J. 277 2010 2454 2462
    • (2010) FEBS J. , vol.277 , pp. 2454-2462
    • Karala, A.R.1    Ruddock, L.W.2
  • 60
    • 0029146852 scopus 로고
    • Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site
    • H. Quan et al. Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site J. Biol. Chem. 270 1995 17078 17080
    • (1995) J. Biol. Chem. , vol.270 , pp. 17078-17080
    • Quan, H.1
  • 61
    • 0035815678 scopus 로고    scopus 로고
    • Domains b′ and a′ of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase: The N-terminal domains a and b enhance this function and can be substituted in part by those of ERp57
    • DOI 10.1074/jbc.M010656200
    • A. Pirneskoski et al. Domains b′ and a′ of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57 J. Biol. Chem. 276 2001 11287 11293 (Pubitemid 38089317)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 11287-11293
    • Pirneskoski, A.1    Ruddock, L.W.2    Klappa, P.3    Freedman, R.B.4    Kivirikko, K.I.5    Koivunen, P.6
  • 62
    • 0035890070 scopus 로고    scopus 로고
    • Manipulation of oxidative protein folding and PDI redox state in mammalian cells
    • DOI 10.1093/emboj/20.22.6288
    • A. Mezghrani et al. Manipulation of oxidative protein folding and PDI redox state in mammalian cells EMBO J. 20 2001 6288 6296 (Pubitemid 33078702)
    • (2001) EMBO Journal , vol.20 , Issue.22 , pp. 6288-6296
    • Mezghrani, A.1    Fassio, A.2    Benham, A.3    Simmen, T.4    Braakman, I.5    Sitia, R.6
  • 63
    • 77957806157 scopus 로고    scopus 로고
    • Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated
    • C. Appenzeller-Herzog et al. Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated EMBO J. 29 2010 3318 3329
    • (2010) EMBO J. , vol.29 , pp. 3318-3329
    • Appenzeller-Herzog, C.1
  • 64
    • 58649096169 scopus 로고    scopus 로고
    • Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a′ domains of protein-disulfide isomerase
    • L. Wang et al. Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a′ domains of protein-disulfide isomerase J. Biol. Chem. 284 2009 199 206
    • (2009) J. Biol. Chem. , vol.284 , pp. 199-206
    • Wang, L.1
  • 66
    • 84859480323 scopus 로고    scopus 로고
    • Protein disulfide isomerase in redox cell signaling and homeostasis
    • F.R. Laurindo et al. Protein disulfide isomerase in redox cell signaling and homeostasis Free Radic. Biol. Med. 52 2012 1954 1969
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 1954-1969
    • Laurindo, F.R.1
  • 67
    • 70350218853 scopus 로고    scopus 로고
    • Nitrosative stress-induced s-glutathionylation of protein disulfide isomerase leads to activation of the unfolded protein response
    • D.M. Townsend et al. Nitrosative stress-induced s-glutathionylation of protein disulfide isomerase leads to activation of the unfolded protein response Cancer Res. 69 2009 7626 7634
    • (2009) Cancer Res. , vol.69 , pp. 7626-7634
    • Townsend, D.M.1
  • 68
    • 84862271547 scopus 로고    scopus 로고
    • S-Glutathionylation of protein disulfide isomerase regulates estrogen receptor alpha stability and function
    • Y. Xiong et al. S-Glutathionylation of protein disulfide isomerase regulates estrogen receptor alpha stability and function Int. J. Cell Biol. 2012 2012 273549
    • (2012) Int. J. Cell Biol. , vol.2012 , pp. 273549
    • Xiong, Y.1
  • 69
    • 79251493784 scopus 로고    scopus 로고
    • Nitrosative stress-induced S-glutathionylation of protein disulfide isomerase
    • J.D. Uys et al. Nitrosative stress-induced S-glutathionylation of protein disulfide isomerase Methods Enzymol. 490 2011 321 332
    • (2011) Methods Enzymol. , vol.490 , pp. 321-332
    • Uys, J.D.1
  • 70
    • 84872978155 scopus 로고    scopus 로고
    • Protein disulfide isomerase modification and inhibition contribute to ER stress and apoptosis induced by oxidized low density lipoproteins
    • C. Muller et al. Protein disulfide isomerase modification and inhibition contribute to ER stress and apoptosis induced by oxidized low density lipoproteins Antioxid. Redox Signal. 18 2013 731 742
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 731-742
    • Muller, C.1
  • 71
    • 70449377144 scopus 로고    scopus 로고
    • Reticulon-4A (Nogo-A) redistributes protein disulfide isomerase to protect mice from SOD1-dependent amyotrophic lateral sclerosis
    • Y.S. Yang et al. Reticulon-4A (Nogo-A) redistributes protein disulfide isomerase to protect mice from SOD1-dependent amyotrophic lateral sclerosis J. Neurosci. 29 2009 13850 13859
    • (2009) J. Neurosci. , vol.29 , pp. 13850-13859
    • Yang, Y.S.1
  • 72
    • 84879718279 scopus 로고    scopus 로고
    • Reticulon1-C modulates protein disulphide isomerase function
    • P. Bernardoni et al. Reticulon1-C modulates protein disulphide isomerase function Cell Death Dis. 4 2013 e581
    • (2013) Cell Death Dis. , vol.4 , pp. 581
    • Bernardoni, P.1
  • 73
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • DOI 10.1146/annurev.biochem.73.011303.074134
    • M. Schroder, and R.J. Kaufman The mammalian unfolded protein response Annu. Rev. Biochem. 74 2005 739 789 (Pubitemid 40995523)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 74
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • G.S. Hotamisligil Endoplasmic reticulum stress and the inflammatory basis of metabolic disease Cell 140 2010 900 917
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 75
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • H.P. Harding et al. Perk is essential for translational regulation and cell survival during the unfolded protein response Mol. Cell 5 2000 897 904
    • (2000) Mol. Cell , vol.5 , pp. 897-904
    • Harding, H.P.1
  • 76
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • DOI 10.1016/S0092-8674(01)00611-0
    • H. Yoshida et al. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor Cell 107 2001 881 891 (Pubitemid 34084979)
    • (2001) Cell , vol.107 , Issue.7 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 77
    • 70449577164 scopus 로고    scopus 로고
    • In vitro reconstitution of ER-stress induced ATF6 transport in COPII vesicles
    • A.J. Schindler, and R. Schekman In vitro reconstitution of ER-stress induced ATF6 transport in COPII vesicles Proc. Natl. Acad. Sci. U. S. A. 106 2009 17775 17780
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 17775-17780
    • Schindler, A.J.1    Schekman, R.2
  • 79
    • 0036531922 scopus 로고    scopus 로고
    • Comparative gene expression profile analysis of neurofibromatosis 1-associated and sporadic pilocytic astrocytomas
    • D.H. Gutmann et al. Comparative gene expression profile analysis of neurofibromatosis 1-associated and sporadic pilocytic astrocytomas Cancer Res. 62 2002 2085 2091 (Pubitemid 34408456)
    • (2002) Cancer Research , vol.62 , Issue.7 , pp. 2085-2091
    • Gutmann, D.H.1    Hedrick, N.M.2    Li, J.3    Nagarajan, R.4    Perry, A.5    Watson, M.A.6
  • 80
    • 54549108740 scopus 로고    scopus 로고
    • Comprehensive genomic characterization defines human glioblastoma genes and core pathways
    • Cancer Genome Atlas Research Network
    • Cancer Genome Atlas Research Network Comprehensive genomic characterization defines human glioblastoma genes and core pathways Nature 455 2008 1061 1068
    • (2008) Nature , vol.455 , pp. 1061-1068
  • 82
    • 33645772227 scopus 로고    scopus 로고
    • Neuronal and glioma-derived stem cell factor induces angiogenesis within the brain
    • L. Sun et al. Neuronal and glioma-derived stem cell factor induces angiogenesis within the brain Cancer Cell 9 2006 287 300
    • (2006) Cancer Cell , vol.9 , pp. 287-300
    • Sun, L.1
  • 83
    • 25444448993 scopus 로고    scopus 로고
    • Functional network analysis reveals extended gliomagenesis pathway maps and three novel MYC-interacting genes in human gliomas
    • DOI 10.1158/0008-5472.CAN-05-1204
    • M. Bredel et al. Functional network analysis reveals extended gliomagenesis pathway maps and three novel MYC-interacting genes in human gliomas Cancer Res. 65 2005 8679 8689 (Pubitemid 41377355)
    • (2005) Cancer Research , vol.65 , Issue.19 , pp. 8679-8689
    • Bredel, M.1    Bredel, C.2    Juric, D.3    Harsh, G.R.4    Vogel, H.5    Recht, L.D.6    Sikic, B.I.7
  • 84
    • 16844376909 scopus 로고    scopus 로고
    • Reverse engineering of regulatory networks in human B cells
    • K. Basso et al. Reverse engineering of regulatory networks in human B cells Nat. Genet. 37 2005 382 390
    • (2005) Nat. Genet. , vol.37 , pp. 382-390
    • Basso, K.1
  • 85
    • 66649127621 scopus 로고    scopus 로고
    • Mutations of multiple genes cause deregulation of NF-kappaB in diffuse large B-cell lymphoma
    • M. Compagno et al. Mutations of multiple genes cause deregulation of NF-kappaB in diffuse large B-cell lymphoma Nature 459 2009 717 721
    • (2009) Nature , vol.459 , pp. 717-721
    • Compagno, M.1
  • 87
    • 66749104378 scopus 로고    scopus 로고
    • High-resolution DNA copy number and gene expression analyses distinguish chromophobe renal cell carcinomas and renal oncocytomas
    • M.V. Yusenko et al. High-resolution DNA copy number and gene expression analyses distinguish chromophobe renal cell carcinomas and renal oncocytomas BMC Cancer 9 2009 152
    • (2009) BMC Cancer , vol.9 , pp. 152
    • Yusenko, M.V.1
  • 88
    • 66349100709 scopus 로고    scopus 로고
    • Patterns of gene expression and copy-number alterations in von-hippel lindau disease-associated and sporadic clear cell carcinoma of the kidney
    • R. Beroukhim et al. Patterns of gene expression and copy-number alterations in von-hippel lindau disease-associated and sporadic clear cell carcinoma of the kidney Cancer Res. 69 2009 4674 4681
    • (2009) Cancer Res. , vol.69 , pp. 4674-4681
    • Beroukhim, R.1
  • 90
    • 48549092983 scopus 로고    scopus 로고
    • A gene signature predicting for survival in suboptimally debulked patients with ovarian cancer
    • T. Bonome et al. A gene signature predicting for survival in suboptimally debulked patients with ovarian cancer Cancer Res. 68 2008 5478 5486
    • (2008) Cancer Res. , vol.68 , pp. 5478-5486
    • Bonome, T.1
  • 94
    • 18544365698 scopus 로고    scopus 로고
    • Gene-expression profiles predict survival of patients with lung adenocarcinoma
    • D.G. Beer et al. Gene-expression profiles predict survival of patients with lung adenocarcinoma Nat. Med. 8 2002 816 824
    • (2002) Nat. Med. , vol.8 , pp. 816-824
    • Beer, D.G.1
  • 96
    • 79952326406 scopus 로고    scopus 로고
    • Proteomics-based signature for human benign prostate hyperplasia and prostate adenocarcinoma
    • A.A. Alaiya et al. Proteomics-based signature for human benign prostate hyperplasia and prostate adenocarcinoma Int. J. Oncol. 38 2011 1047 1057
    • (2011) Int. J. Oncol. , vol.38 , pp. 1047-1057
    • Alaiya, A.A.1
  • 97
    • 33644636189 scopus 로고    scopus 로고
    • Expression of fibrinogen E-fragment and fibrin E-fragment is inhibited in the human infiltrating ductal carcinoma of the breast: The two-dimensional electrophoresis and MALDI-TOF-mass spectrometry analyses
    • K. Chahed et al. Expression of fibrinogen E-fragment and fibrin E-fragment is inhibited in the human infiltrating ductal carcinoma of the breast: the two-dimensional electrophoresis and MALDI-TOF-mass spectrometry analyses Int. J. Oncol. 27 2005 1425 1431
    • (2005) Int. J. Oncol. , vol.27 , pp. 1425-1431
    • Chahed, K.1
  • 98
    • 37249045988 scopus 로고    scopus 로고
    • Detection of protein alterations in male breast cancer using two dimensional gel electrophoresis and mass spectrometry: The involvement of several pathways in tumorigenesis
    • DOI 10.1016/j.cca.2007.10.018, PII S0009898107005128
    • K. Chahed et al. Detection of protein alterations in male breast cancer using two dimensional gel electrophoresis and mass spectrometry: the involvement of several pathways in tumorigenesis Clin. Chim. Acta 388 2008 106 114 (Pubitemid 350266579)
    • (2008) Clinica Chimica Acta , vol.388 , Issue.1-2 , pp. 106-114
    • Chahed, K.1    Kabbage, M.2    Hamrita, B.3    Guillier, C.L.4    Trimeche, M.5    Remadi, S.6    Ehret-Sabatier, L.7    Chouchane, L.8
  • 99
    • 7044235835 scopus 로고    scopus 로고
    • Proteome analysis of gastric cancer metastasis by two-dimensional gel electrophoresis and matrix assisted laser desorption/lonization-mass spectrometry for identification of metastasis-related proteins
    • DOI 10.1021/pr049916l
    • J. Chen et al. Proteome analysis of gastric cancer metastasis by two-dimensional gel electrophoresis and matrix assisted laser desorption/ionization-mass spectrometry for identification of metastasis-related proteins J. Proteome Res. 3 2004 1009 1016 (Pubitemid 39425658)
    • (2004) Journal of Proteome Research , vol.3 , Issue.5 , pp. 1009-1016
    • Chen, J.1    Kahne, T.2    Rocken, C.3    Gotze, T.4    Yu, J.5    Sung, J.J.Y.6    Chen, M.7    Hu, P.8    Malfertheiner, P.9    Ebert, M.P.A.10
  • 100
    • 72549105117 scopus 로고    scopus 로고
    • Up-regulated proteins in the fluid bathing the tumour cell microenvironment as potential serological markers for early detection of cancer of the breast
    • P. Gromov et al. Up-regulated proteins in the fluid bathing the tumour cell microenvironment as potential serological markers for early detection of cancer of the breast Mol. Oncol. 4 2010 65 89
    • (2010) Mol. Oncol. , vol.4 , pp. 65-89
    • Gromov, P.1
  • 101
    • 79955849323 scopus 로고    scopus 로고
    • Differential protein expression in primary breast cancer and matched axillary node metastasis
    • P. Thongwatchara et al. Differential protein expression in primary breast cancer and matched axillary node metastasis Oncol. Rep. 26 2011 185 191
    • (2011) Oncol. Rep. , vol.26 , pp. 185-191
    • Thongwatchara, P.1
  • 103
    • 61849145128 scopus 로고    scopus 로고
    • Protein disulfide isomerases are antibody targets during immune-mediated tumor destruction
    • C. Fonseca et al. Protein disulfide isomerases are antibody targets during immune-mediated tumor destruction Blood 113 2009 1681 1688
    • (2009) Blood , vol.113 , pp. 1681-1688
    • Fonseca, C.1
  • 106
    • 0025429099 scopus 로고
    • Altered regulation of protein disulfide isomerase in cells resistant to the growth-inhibitory effects of transforming growth factor beta 1
    • N.J. Sipes et al. Altered regulation of protein disulfide isomerase in cells resistant to the growth-inhibitory effects of transforming growth factor beta 1 Cell Growth Differ. 1 1990 241 246
    • (1990) Cell Growth Differ. , vol.1 , pp. 241-246
    • Sipes, N.J.1
  • 107
    • 48549102186 scopus 로고    scopus 로고
    • Increasing melanoma cell death using inhibitors of protein disulfide isomerases to abrogate survival responses to endoplasmic reticulum stress
    • P.E. Lovat et al. Increasing melanoma cell death using inhibitors of protein disulfide isomerases to abrogate survival responses to endoplasmic reticulum stress Cancer Res. 68 2008 5363 5369
    • (2008) Cancer Res. , vol.68 , pp. 5363-5369
    • Lovat, P.E.1
  • 109
    • 84862777172 scopus 로고    scopus 로고
    • Enhancement of hexokinase II inhibitor-induced apoptosis in hepatocellular carcinoma cells via augmenting ER stress and anti-angiogenesis by protein disulfide isomerase inhibition
    • S.J. Yu et al. Enhancement of hexokinase II inhibitor-induced apoptosis in hepatocellular carcinoma cells via augmenting ER stress and anti-angiogenesis by protein disulfide isomerase inhibition J. Bioenergy Biomembr. 44 2012 101 115
    • (2012) J. Bioenergy Biomembr. , vol.44 , pp. 101-115
    • Yu, S.J.1
  • 110
    • 84867095394 scopus 로고    scopus 로고
    • Discovery of an orally active small-molecule irreversible inhibitor of protein disulfide isomerase for ovarian cancer treatment
    • S. Xu et al. Discovery of an orally active small-molecule irreversible inhibitor of protein disulfide isomerase for ovarian cancer treatment Proc. Natl. Acad. Sci. U. S. A. 109 2012 16348 16353
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 16348-16353
    • Xu, S.1
  • 111
    • 79551585674 scopus 로고    scopus 로고
    • Protein disulfide isomerase knockdown-induced cell death is cell-line-dependent and involves apoptosis in MCF-7 cells
    • T. Hashida et al. Protein disulfide isomerase knockdown-induced cell death is cell-line-dependent and involves apoptosis in MCF-7 cells J. Toxicol. Sci. 36 2011 1 7
    • (2011) J. Toxicol. Sci. , vol.36 , pp. 1-7
    • Hashida, T.1
  • 112
    • 84862783592 scopus 로고    scopus 로고
    • Protein disulfide isomerase-mediated disulfide bonds regulate the gelatinolytic activity and secretion of matrix metalloproteinase-9
    • M.M. Khan et al. Protein disulfide isomerase-mediated disulfide bonds regulate the gelatinolytic activity and secretion of matrix metalloproteinase-9 Exp. Cell Res. 318 2012 904 914
    • (2012) Exp. Cell Res. , vol.318 , pp. 904-914
    • Khan, M.M.1
  • 113
    • 51049124323 scopus 로고    scopus 로고
    • Ritonavir induces endoplasmic reticulum stress and sensitizes sarcoma cells toward bortezomib-induced apoptosis
    • M. Kraus et al. Ritonavir induces endoplasmic reticulum stress and sensitizes sarcoma cells toward bortezomib-induced apoptosis Mol. Cancer Ther. 7 2008 1940 1948
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 1940-1948
    • Kraus, M.1
  • 114
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • D. Hanahan, and R.A. Weinberg Hallmarks of cancer: the next generation Cell 144 2011 646 674
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 115
    • 0036782706 scopus 로고    scopus 로고
    • Transcription factors as targets for cancer therapy
    • DOI 10.1038/nrc906
    • J.E. Darnell Jr. Transcription factors as targets for cancer therapy Nat. Rev. Cancer 2 2002 740 749 (Pubitemid 37328909)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.10 , pp. 740-749
    • Darnell Jr., J.E.1
  • 116
    • 77950002202 scopus 로고    scopus 로고
    • Translational control in cancer
    • D. Silvera et al. Translational control in cancer Nat. Rev. Cancer 10 2010 254 266
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 254-266
    • Silvera, D.1
  • 117
    • 0025861453 scopus 로고
    • Effect of protein and peptide inhibitors on the activity of protein disulfide isomerase
    • N.A. Morjana, and H.F. Gilbert Effect of protein and peptide inhibitors on the activity of protein disulfide isomerase Biochemistry 30 1991 4985 4990
    • (1991) Biochemistry , vol.30 , pp. 4985-4990
    • Morjana, N.A.1    Gilbert, H.F.2
  • 118
    • 79955574624 scopus 로고    scopus 로고
    • Discovery of a small molecule PDI inhibitor that inhibits reduction of HIV-1 envelope glycoprotein gp120
    • M.M. Khan et al. Discovery of a small molecule PDI inhibitor that inhibits reduction of HIV-1 envelope glycoprotein gp120 ACS Chem. Biol. 6 2011 245 251
    • (2011) ACS Chem. Biol. , vol.6 , pp. 245-251
    • Khan, M.M.1
  • 119
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • A. Holmgren Thioredoxin catalyses the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide J. Biol. Chem. 254 1979 9627 9632 (Pubitemid 10248727)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.19 , pp. 9627-9632
    • Holmgren, A.1
  • 120
    • 0031939209 scopus 로고    scopus 로고
    • Protein disulfide isomerase
    • H.F. Gilbert Protein disulfide isomerase Methods Enzymol. 290 1998 26 50
    • (1998) Methods Enzymol. , vol.290 , pp. 26-50
    • Gilbert, H.F.1
  • 121
    • 17044417590 scopus 로고    scopus 로고
    • A high-throughput turbidometric assay for screening inhibitors of protein disulfide isomerase activity
    • A.M. Smith et al. A high-throughput turbidometric assay for screening inhibitors of protein disulfide isomerase activity J. Biomol. Screen. 9 2004 614 620
    • (2004) J. Biomol. Screen. , vol.9 , pp. 614-620
    • Smith, A.M.1
  • 123
    • 0017694426 scopus 로고
    • Purification and characterization of a thiol:protein disulfide oxidoreductase from bovine liver
    • D.F. Carmichael et al. Purification and characterization of a thiol:protein disulfide oxidoreductase from bovine liver J. Biol. Chem. 252 1977 7163 7167 (Pubitemid 8206268)
    • (1977) Journal of Biological Chemistry , vol.252 , Issue.20 , pp. 7163-7167
    • Carmichael, D.F.1    Morin, J.E.2    Dixon, J.E.3
  • 125
    • 27444447668 scopus 로고    scopus 로고
    • A direct, continuous, sensitive assay for protein disulphide-isomerase based on fluorescence self-quenching
    • DOI 10.1042/BJ20050770
    • A. Raturi et al. A direct, continuous, sensitive assay for protein disulphide-isomerase based on fluorescence self-quenching Biochem. J. 391 2005 351 357 (Pubitemid 41532433)
    • (2005) Biochemical Journal , vol.391 , Issue.2 , pp. 351-357
    • Raturi, A.1    Vacratsis, P.O.2    Seslija, D.3    Lee, L.4    Mutus, B.5
  • 126
    • 32644454393 scopus 로고    scopus 로고
    • A fluorescence-based assay for the reductase activity of protein disulfide isomerase
    • DOI 10.1016/j.ab.2005.11.037, PII S000326970500864X
    • R. Tomazzolli et al. A fluorescence-based assay for the reductase activity of protein disulfide isomerase Anal. Biochem. 350 2006 105 112 (Pubitemid 43247631)
    • (2006) Analytical Biochemistry , vol.350 , Issue.1 , pp. 105-112
    • Tomazzolli, R.1    Serra, M.D.2    Bellisola, G.3    Colombatti, M.4    Guella, G.5
  • 127
    • 0026062381 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Dependence of the rate on the composition of the redox buffer
    • M.M. Lyles, and H.F. Gilbert Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer Biochemistry 30 1991 613 619
    • (1991) Biochemistry , vol.30 , pp. 613-619
    • Lyles, M.M.1    Gilbert, H.F.2
  • 128
    • 38549146938 scopus 로고    scopus 로고
    • Identification and enzymatic activities of four protein disulfide isomerase (PDI) isoforms of Leishmania amazonensis
    • B.X. Hong, and L. Soong Identification and enzymatic activities of four protein disulfide isomerase (PDI) isoforms of Leishmania amazonensis Parasitol. Res. 102 2008 437 446
    • (2008) Parasitol. Res. , vol.102 , pp. 437-446
    • Hong, B.X.1    Soong, L.2
  • 129
    • 0027203922 scopus 로고
    • The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity
    • DOI 10.1016/0092-8674(93)90469-7
    • M.L. LaMantia, and W.J. Lennarz The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity Cell 74 1993 899 908 (Pubitemid 23270609)
    • (1993) Cell , vol.74 , Issue.5 , pp. 899-908
    • LaMantia, M.1    Lennarz, W.J.2
  • 130
    • 0017144476 scopus 로고
    • Thiol-protein disulphide oxidoreductases. Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase
    • A.L. Ibbetson, and R.B. Freedman Thiol-protein disulphide oxidoreductases. Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase Biochem. J. 159 1976 377 384
    • (1976) Biochem. J. , vol.159 , pp. 377-384
    • Ibbetson, A.L.1    Freedman, R.B.2
  • 131
    • 0021152329 scopus 로고
    • Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerase
    • D.A. Hillson et al. Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase Methods Enzymol. 107 1984 281 294
    • (1984) Methods Enzymol. , vol.107 , pp. 281-294
    • Hillson, D.A.1
  • 132
    • 0021659707 scopus 로고
    • Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor
    • DOI 10.1016/0022-2836(84)90077-9
    • T.E. Creighton, and D.P. Goldenberg Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor J. Mol. Biol. 179 1984 497 526 (Pubitemid 16223357)
    • (1984) Journal of Molecular Biology , vol.179 , Issue.3 , pp. 497-526
    • Creighton, T.E.1    Goldenberg, D.P.2
  • 133
    • 35448949114 scopus 로고    scopus 로고
    • Protein disulfide isomerases from C. Elegans are equally efficient at thiol-disulfide exchange in simple peptide-based systems but show differences in reactivity towards protein substrates
    • A.R. Karala et al. Protein disulfide isomerases from C. elegans are equally efficient at thiol-disulfide exchange in simple peptide-based systems but show differences in reactivity towards protein substrates Antioxid. Redox Signal. 9 2007 1815 1823
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 1815-1823
    • Karala, A.R.1
  • 134
    • 0029058524 scopus 로고
    • Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese
    • J.L. Song, and C.C. Wang Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese Eur. J. Biochem. 231 1995 312 316
    • (1995) Eur. J. Biochem. , vol.231 , pp. 312-316
    • Song, J.L.1    Wang, C.C.2
  • 135
    • 0028131648 scopus 로고
    • Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds
    • H. Cai et al. Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds J. Biol. Chem. 269 1994 24550 24552 (Pubitemid 24311703)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.40 , pp. 24550-24552
    • Cai, H.1    Wang, C.-C.2    Tsou, C.-L.3
  • 137
    • 0035808319 scopus 로고    scopus 로고
    • Hormone binding by protein disulfide isomerase, a high capacity hormone reservoir of the endoplasmic reticulum
    • DOI 10.1074/jbc.M007670200
    • T.P. Primm, and H.F. Gilbert Hormone binding by protein disulfide isomerase, a high capacity hormone reservoir of the endoplasmic reticulum J. Biol. Chem. 276 2001 281 286 (Pubitemid 32050318)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.1 , pp. 281-286
    • Primm, T.P.1    Gilbert, H.F.2
  • 139
    • 79960800956 scopus 로고    scopus 로고
    • Acid-denatured Green Fluorescent Protein (GFP) as model substrate to study the chaperone activity of protein disulfide isomerase
    • R.E. Mares et al. Acid-denatured Green Fluorescent Protein (GFP) as model substrate to study the chaperone activity of protein disulfide isomerase Int. J. Mol. Sci. 12 2011 4625 4636
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 4625-4636
    • Mares, R.E.1
  • 140
    • 79955409571 scopus 로고    scopus 로고
    • Discovery and preclinical evaluation of a novel class of cytotoxic propynoic acid carbamoyl methyl amides (PACMAs)
    • R. Yamada et al. Discovery and preclinical evaluation of a novel class of cytotoxic propynoic acid carbamoyl methyl amides (PACMAs) J. Med. Chem. 54 2011 2902 2914
    • (2011) J. Med. Chem. , vol.54 , pp. 2902-2914
    • Yamada, R.1
  • 141
    • 84873176247 scopus 로고    scopus 로고
    • Synthesis of radiolabeled protein disulfide isomerase (PDI) inhibitors as new potential PET agents for imaging of the enzyme PDI in neurological disorders and cancer
    • M. Gao et al. Synthesis of radiolabeled protein disulfide isomerase (PDI) inhibitors as new potential PET agents for imaging of the enzyme PDI in neurological disorders and cancer Appl. Radiat. Isot. 74 2013 61 69
    • (2013) Appl. Radiat. Isot. , vol.74 , pp. 61-69
    • Gao, M.1
  • 142
    • 84874024997 scopus 로고    scopus 로고
    • 1,3,5-Triazine as a modular scaffold for covalent inhibitors with streamlined target identification
    • R. Banerjee et al. 1,3,5-Triazine as a modular scaffold for covalent inhibitors with streamlined target identification J. Am. Chem. Soc. 135 2013 2497 2500
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 2497-2500
    • Banerjee, R.1
  • 143
    • 0021997899 scopus 로고
    • Evidence for the involvement of vicinal sulfhydryl groups in insulin-activated hexose transport by 3T3-L1 adipocytes
    • S.C. Frost, and M.D. Lane Evidence for the involvement of vicinal sulfhydryl groups in insulin-activated hexose transport by 3T3-L1 adipocytes J. Biol. Chem. 260 1985 2646 2652 (Pubitemid 15139315)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.5 , pp. 2646-2652
    • Frost, S.C.1    Lane, M.D.2
  • 144
    • 0028365452 scopus 로고
    • Purification of vicinal dithiol-containing proteins by arsenical-based affinity chromatography
    • E. Kalef, and C. Gitler Purification of vicinal dithiol-containing proteins by arsenical-based affinity chromatography Methods Enzymol. 233 1994 395 403
    • (1994) Methods Enzymol. , vol.233 , pp. 395-403
    • Kalef, E.1    Gitler, C.2
  • 145
    • 0037015005 scopus 로고    scopus 로고
    • Evidence for a role for protein tyrosine phosphatase in the control of ion release from the guard cell vacuole in stomatal closure
    • E.A. MacRobbie Evidence for a role for protein tyrosine phosphatase in the control of ion release from the guard cell vacuole in stomatal closure Proc. Natl. Acad. Sci. U. S. A. 99 2002 11963 11968
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 11963-11968
    • Macrobbie, E.A.1
  • 146
    • 0038779198 scopus 로고    scopus 로고
    • Thiol-modifying phenylarsine oxide inhibits guanine nucleotide binding of Rho but not of Rac GTPases
    • DOI 10.1124/mol.63.6.1349
    • R. Gerhard et al. Thiol-modifying phenylarsine oxide inhibits guanine nucleotide binding of Rho but not of Rac GTPases Mol. Pharmacol. 63 2003 1349 1355 (Pubitemid 36627230)
    • (2003) Molecular Pharmacology , vol.63 , Issue.6 , pp. 1349-1355
    • Gerhard, R.1    John, H.2    Aktories, K.3    Just, I.4
  • 147
    • 0028257964 scopus 로고
    • Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction
    • H.J. Ryser et al. Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction Proc. Natl. Acad. Sci. U. S. A. 91 1994 4559 4563
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 4559-4563
    • Ryser, H.J.1
  • 148
    • 0026050289 scopus 로고
    • Cell surface sulfhydryls are required for the cytotoxicity of diphtheria toxin but not of ricin in Chinese hamster ovary cells
    • H.J. Ryser et al. Cell surface sulfhydryls are required for the cytotoxicity of diphtheria toxin but not of ricin in Chinese hamster ovary cells J. Biol. Chem. 266 1991 18439 18442 (Pubitemid 21908102)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.28 , pp. 18439-18442
    • Ryser, H.J.-P.1    Mandel, R.2    Ghani, F.3
  • 149
    • 0025010857 scopus 로고
    • Cleavage of disulfide bonds in endocytosed macromolecules. A processing not associated with lysosomes or endosomes
    • E.P. Feener et al. Cleavage of disulfide bonds in endocytosed macromolecules. A processing not associated with lysosomes or endosomes J. Biol. Chem. 265 1990 18780 18785
    • (1990) J. Biol. Chem. , vol.265 , pp. 18780-18785
    • Feener, E.P.1
  • 150
    • 4344676781 scopus 로고    scopus 로고
    • Inactivation of protein disulfide isomerase by alkylators including alpha,beta-unsaturated aldehydes at low physiological pHs
    • X.W. Liu, and D.E. Sok Inactivation of protein disulfide isomerase by alkylators including alpha,beta-unsaturated aldehydes at low physiological pHs Biol. Chem. 385 2004 633 637
    • (2004) Biol. Chem. , vol.385 , pp. 633-637
    • Liu, X.W.1    Sok, D.E.2
  • 151
    • 33750002010 scopus 로고    scopus 로고
    • Redox Regulation Facilitates Optimal Peptide Selection by MHC Class I during Antigen Processing
    • DOI 10.1016/j.cell.2006.08.041, PII S0092867406012190
    • B. Park et al. Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing Cell 127 2006 369 382 (Pubitemid 44572373)
    • (2006) Cell , vol.127 , Issue.2 , pp. 369-382
    • Park, B.1    Lee, S.2    Kim, E.3    Cho, K.4    Riddell, S.R.5    Cho, S.6    Ahn, K.7
  • 152
    • 84861808529 scopus 로고    scopus 로고
    • Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents
    • R. Jasuja et al. Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents J. Clin. Invest. 122 2012 2104 2113
    • (2012) J. Clin. Invest. , vol.122 , pp. 2104-2113
    • Jasuja, R.1
  • 153
    • 0019421249 scopus 로고
    • Bacitracin: An inhibitor of the insulin degrading activity of glutathione-insulin transhydrogenase
    • DOI 10.1016/0006-291X(81)90858-5
    • R.A. Roth Bacitracin: an inhibitor of the insulin degrading activity of glutathione-insulin transhydrogenase Biochem. Biophys. Res. Commun. 98 1981 431 438 (Pubitemid 11159482)
    • (1981) Biochemical and Biophysical Research Communications , vol.98 , Issue.2 , pp. 431-438
    • Roth, R.A.1
  • 155
    • 79958122391 scopus 로고    scopus 로고
    • Bacitracin inhibits the reductive activity of protein disulfide isomerase by disulfide bond formation with free cysteines in the substrate-binding domain
    • N. Dickerhof et al. Bacitracin inhibits the reductive activity of protein disulfide isomerase by disulfide bond formation with free cysteines in the substrate-binding domain FEBS J. 278 2011 2034 2043
    • (2011) FEBS J. , vol.278 , pp. 2034-2043
    • Dickerhof, N.1
  • 156
    • 0034773112 scopus 로고    scopus 로고
    • Bacitracin inhibits fibronectin matrix assembly by mesangial cells in high glucose
    • DOI 10.1046/j.1523-1755.2001.00991.x
    • B.S. Weston et al. Bacitracin inhibits fibronectin matrix assembly by mesangial cells in high glucose Kidney Int. 60 2001 1756 1764 (Pubitemid 32999980)
    • (2001) Kidney International , vol.60 , Issue.5 , pp. 1756-1764
    • Weston, B.S.1    Wahab, N.A.2    Roberts, T.3    Mason, R.M.4
  • 157
    • 1642564464 scopus 로고    scopus 로고
    • Mechanism of bacitracin permeation enhancement through the skin and cellular membranes from an ethosomal carrier
    • DOI 10.1016/j.jconrel.2003.10.014
    • B. Godin, and E. Touitou Mechanism of bacitracin permeation enhancement through the skin and cellular membranes from an ethosomal carrier J. Control. Release 94 2004 365 379 (Pubitemid 38117147)
    • (2004) Journal of Controlled Release , vol.94 , Issue.2-3 , pp. 365-379
    • Godin, B.1    Touitou, E.2
  • 158
    • 40649086615 scopus 로고    scopus 로고
    • Validation of putative genomic biomarkers of nephrotoxicity in rats
    • E.J. Wang et al. Validation of putative genomic biomarkers of nephrotoxicity in rats Toxicology 246 2008 91 100
    • (2008) Toxicology , vol.246 , pp. 91-100
    • Wang, E.J.1
  • 159
    • 0023238983 scopus 로고
    • Interaction of antibiotics with functional sites in 16S ribosomal RNA
    • DOI 10.1038/327389a0
    • D. Moazed, and H.F. Noller Interaction of antibiotics with functional sites in 16S ribosomal RNA Nature 327 1987 389 394 (Pubitemid 17075811)
    • (1987) Nature , vol.327 , Issue.6121 , pp. 389-394
    • Moazed, D.1    Noller, H.F.2
  • 160
    • 0036304251 scopus 로고    scopus 로고
    • Aminoglycoside antibiotics bind to protein disulfide isomerase and inhibit its chaperone activity
    • T. Horibe et al. Aminoglycoside antibiotics bind to protein disulfide isomerase and inhibit its chaperone activity J. Antibiot. 55 2002 528 530 (Pubitemid 34746678)
    • (2002) Journal of Antibiotics , vol.55 , Issue.5 , pp. 528-530
    • Horibe, T.1    Nagai, H.2    Matsui, H.3    Hagiwara, Y.4    Kikuchi, M.5
  • 162
    • 80455131183 scopus 로고    scopus 로고
    • Characterization of the estradiol-binding site structure of human protein disulfide isomerase (PDI)
    • X.M. Fu et al. Characterization of the estradiol-binding site structure of human protein disulfide isomerase (PDI) PLoS ONE 6 2011 e27185
    • (2011) PLoS ONE , vol.6 , pp. 27185
    • Fu, X.M.1
  • 163
    • 33646798398 scopus 로고    scopus 로고
    • Bisphenol A binds to protein disulfide isomerase and inhibits its enzymatic and hormone-binding activities
    • DOI 10.1210/en.2005-1235
    • T. Hiroi et al. Bisphenol A binds to protein disulfide isomerase and inhibits its enzymatic and hormone-binding activities Endocrinology 147 2006 2773 2780 (Pubitemid 43764614)
    • (2006) Endocrinology , vol.147 , Issue.6 , pp. 2773-2780
    • Hiroi, T.1    Okada, K.2    Imaoka, S.3    Osada, M.4    Funae, Y.5
  • 164
    • 0026043928 scopus 로고
    • Cellular binding proteins of thyroid hormones
    • K. Ichikawa, and K. Hashizume Cellular binding proteins of thyroid hormones Life Sci. 49 1991 1513 1522
    • (1991) Life Sci. , vol.49 , pp. 1513-1522
    • Ichikawa, K.1    Hashizume, K.2
  • 166
    • 0020518888 scopus 로고
    • Structural similarities in the plasma membrane 3,3',5-triiodo-L-thyronine receptors from human, rat and mouse cultured cells. Analysis of affinity labeling
    • S.Y. Cheng Structural similarities in the plasma membrane 3,3′,5-triiodo-L-thyronine receptors from human, rat and mouse cultured cells. Analysis by affinity labeling Endocrinology 113 1983 1155 1157 (Pubitemid 13051963)
    • (1983) Endocrinology , vol.113 , Issue.3 , pp. 1155-1157
    • Cheng, S.Y.1
  • 167
    • 0023653293 scopus 로고
    • Sequence of membrane-associated thyroid hormone binding protein from bovine liver: Its identity with protein disulphide isomerase
    • K. Yamauchi et al. Sequence of membrane-associated thyroid hormone binding protein from bovine liver: its identity with protein disulphide isomerase Biochem. Biophys. Res. Commun. 146 1987 1485 1492
    • (1987) Biochem. Biophys. Res. Commun. , vol.146 , pp. 1485-1492
    • Yamauchi, K.1
  • 168
    • 0029808166 scopus 로고    scopus 로고
    • Reexamination of hormone-binding properties of protein disulfide-isomerase
    • R. Guthapfel et al. Reexamination of hormone-binding properties of protein disulfide-isomerase Eur. J. Biochem. 242 1996 315 319 (Pubitemid 26414237)
    • (1996) European Journal of Biochemistry , vol.242 , Issue.2 , pp. 315-319
    • Guthapfel, R.1    Gueguen, P.2    Quemeneur, E.3
  • 169
    • 79960980803 scopus 로고    scopus 로고
    • Bisphenol A: An endocrine disruptor with widespread exposure and multiple effects
    • B.S. Rubin Bisphenol A: an endocrine disruptor with widespread exposure and multiple effects J. Steroid Biochem. Mol. Biol. 127 2011 27 34
    • (2011) J. Steroid Biochem. Mol. Biol. , vol.127 , pp. 27-34
    • Rubin, B.S.1
  • 170
    • 40949108026 scopus 로고    scopus 로고
    • Direct evidence revealing structural elements essential for the high binding ability of bisphenol A to human estrogen-related receptor-gamma
    • H. Okada et al. Direct evidence revealing structural elements essential for the high binding ability of bisphenol A to human estrogen-related receptor-gamma Environ. Health Perspect. 116 2008 32 38
    • (2008) Environ. Health Perspect. , vol.116 , pp. 32-38
    • Okada, H.1
  • 172
    • 80052103006 scopus 로고    scopus 로고
    • Chemical stress on protein disulfide isomerases and inhibition of their functions
    • S. Imaoka Chemical stress on protein disulfide isomerases and inhibition of their functions Int. Rev. Cell Mol. Biol. 290 2011 121 166
    • (2011) Int. Rev. Cell Mol. Biol. , vol.290 , pp. 121-166
    • Imaoka, S.1
  • 173
    • 84855253249 scopus 로고    scopus 로고
    • The binding site of bisphenol A to protein disulphide isomerase
    • S. Hashimoto et al. The binding site of bisphenol A to protein disulphide isomerase J. Biochem. 151 2012 35 45
    • (2012) J. Biochem. , vol.151 , pp. 35-45
    • Hashimoto, S.1
  • 174
    • 0034655128 scopus 로고    scopus 로고
    • Sulfhydryl regulation of L-selectin shedding: Phenylarsine oxide promotes activation-independent L-selectin shedding from leukocytes
    • T.A. Bennett et al. Sulfhydryl regulation of L-selectin shedding: phenylarsine oxide promotes activation-independent L-selectin shedding from leukocytes J. Immunol. 164 2000 4120 4129 (Pubitemid 30215068)
    • (2000) Journal of Immunology , vol.164 , Issue.8 , pp. 4120-4129
    • Bennett, T.A.1    Edwards, B.S.2    Sklar, L.A.3    Rogelj, S.4
  • 175
    • 79953100968 scopus 로고    scopus 로고
    • Antiviral propierties of 5,5′-dithiobis-2-nitrobenzoic acid and bacitracin against T-tropic human immunodeficiency virus type 1
    • H.H. Lara et al. Antiviral propierties of 5,5′-dithiobis-2- nitrobenzoic acid and bacitracin against T-tropic human immunodeficiency virus type 1 Virol. J. 8 2011 137
    • (2011) Virol. J. , vol.8 , pp. 137
    • Lara, H.H.1
  • 177
    • 84861413246 scopus 로고    scopus 로고
    • Opposing effects of bacitracin on human papillomavirus type 16 infection: Enhancement of binding and entry and inhibition of endosomal penetration
    • S.K. Campos et al. Opposing effects of bacitracin on human papillomavirus type 16 infection: enhancement of binding and entry and inhibition of endosomal penetration J. Virol. 86 2012 4169 4181
    • (2012) J. Virol. , vol.86 , pp. 4169-4181
    • Campos, S.K.1
  • 179
    • 34047258016 scopus 로고    scopus 로고
    • 1 2,3-epoxide reduction
    • DOI 10.1074/jbc.M608954200
    • N. Wajih et al. Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum. A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction J. Biol. Chem. 282 2007 2626 2635 (Pubitemid 47076752)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.4 , pp. 2626-2635
    • Wajih, N.1    Hutson, S.M.2    Wallin, R.3
  • 180
    • 1942471909 scopus 로고    scopus 로고
    • Protein disulfide isomerase suppresses the transcriptional activity of NF-κB
    • DOI 10.1016/j.bbrc.2004.04.002, PII S0006291X04007053
    • T. Higuchi et al. Protein disulfide isomerase suppresses the transcriptional activity of NF-kappaB Biochem. Biophys. Res. Commun. 318 2004 46 52 (Pubitemid 38526243)
    • (2004) Biochemical and Biophysical Research Communications , vol.318 , Issue.1 , pp. 46-52
    • Higuchi, T.1    Watanabe, Y.2    Waga, I.3
  • 181
    • 0030471654 scopus 로고    scopus 로고
    • Cell surface protein disulfide-isomerase is involved in the shedding of human thyrotropin receptor ectodomain
    • DOI 10.1021/bi961359w
    • J. Couet et al. Cell surface protein disulfide-isomerase is involved in the shedding of human thyrotropin receptor ectodomain Biochemistry 35 1996 14800 14805 (Pubitemid 26423813)
    • (1996) Biochemistry , vol.35 , Issue.47 , pp. 14800-14805
    • Couet, J.1    De Bernard, S.2    Loosfelt, H.3    Saunier, B.4    Milgrom, E.5    Misrahi, M.6
  • 182
    • 67349253073 scopus 로고    scopus 로고
    • Experimental stroke protection induced by 4-hydroxybenzyl alcohol is cancelled by bacitracin
    • E. Descamps et al. Experimental stroke protection induced by 4-hydroxybenzyl alcohol is cancelled by bacitracin Neurosci. Res. 64 2009 137 142
    • (2009) Neurosci. Res. , vol.64 , pp. 137-142
    • Descamps, E.1


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