메뉴 건너뛰기




Volumn 328, Issue , 2013, Pages 1-34

Assisting oxidative protein folding: How do protein disulphide-isomerases couple conformational and chemical processes in protein folding?

Author keywords

Endoplasmic reticulum; Enzyme mechanism; Mobility; Oxidative folding; Protein conformation

Indexed keywords

PROTEIN DISULFIDE ISOMERASE;

EID: 84874506387     PISSN: 03401022     EISSN: None     Source Type: Book Series    
DOI: 10.1007/128-2011-171     Document Type: Article
Times cited : (20)

References (136)
  • 1
    • 33746265142 scopus 로고    scopus 로고
    • GroEL-mediated protein folding: Making the impossible, possible
    • Lin Z, Rye HS (2006) GroEL-mediated protein folding: making the impossible, possible. Crit Rev Biochem Mol Biol 41:211-239
    • (2006) Crit Rev Biochem Mol Biol , vol.41 , pp. 211-239
    • Lin, Z.1    Rye, H.S.2
  • 2
    • 45649083920 scopus 로고    scopus 로고
    • Concerted release of substrate domains from GroEL by ATP is demonstrated with FRET
    • Papo N, Kipnis Y, Haran G et al (2008) Concerted release of substrate domains from GroEL by ATP is demonstrated with FRET. J Mol Biol 380:717-725
    • (2008) J Mol Biol , vol.380 , pp. 717-725
    • Papo, N.1    Kipnis, Y.2    Haran, G.3
  • 3
    • 58749116660 scopus 로고    scopus 로고
    • Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin
    • Altschuler GM, Willison KR (2008) Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin. J R Soc Interface 5:1391-1408
    • (2008) J R Soc Interface , vol.5 , pp. 1391-1408
    • Altschuler, G.M.1    Willison, K.R.2
  • 5
    • 23744457478 scopus 로고    scopus 로고
    • Versatility of the endoplasmic reticulum protein folding factory
    • van Anken E, Braakman I (2005) Versatility of the endoplasmic reticulum protein folding factory. Crit Rev Biochem Mol Biol 40:191-228
    • (2005) Crit Rev Biochem Mol Biol , vol.40 , pp. 191-228
    • Van Anken, E.1    Braakman, I.2
  • 6
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: Protein folding, quality control, degradation, and related human diseases
    • Hebert DN, Molinari M (2007) In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol Rev 87:1377-1408
    • (2007) Physiol Rev , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 7
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: Substrate interactions and functional properties
    • Ellgaard L, Ruddock LW (2005) The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep 6:28-32
    • (2005) EMBO Rep , vol.6 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 8
    • 41549159471 scopus 로고    scopus 로고
    • The human PDI family: Versatility packed into a single fold
    • Appenzeller-Herzog C, Ellgaard L (2008) The human PDI family: versatility packed into a single fold. Biochim Biophys Acta 1783:535-548
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 535-548
    • Appenzeller-Herzog, C.1    Ellgaard, L.2
  • 9
    • 0028964420 scopus 로고
    • The formation of protein disulphide bonds
    • Freedman RB (1995) The formation of protein disulphide bonds. Curr Opin Struct Biol 5:85-91
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 85-91
    • Freedman, R.B.1
  • 10
    • 41449093101 scopus 로고    scopus 로고
    • Disulfide bond isomerization in prokaryotes
    • Gleiter S, Bardwell JC (2008) Disulfide bond isomerization in prokaryotes. Biochim Biophys Acta 1783:530-534
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 530-534
    • Gleiter, S.1    Bardwell, J.C.2
  • 12
    • 66749163678 scopus 로고    scopus 로고
    • Disulfide formation in the ER and mitochondria: Two solutions to a common process
    • Riemer J, Bulleid N, Herrmann JM (2009) Disulfide formation in the ER and mitochondria: two solutions to a common process. Science 324:1284-1287
    • (2009) Science , vol.324 , pp. 1284-1287
    • Riemer, J.1    Bulleid, N.2    Herrmann, J.M.3
  • 13
  • 16
    • 33646350007 scopus 로고    scopus 로고
    • Folding of small disulfide-rich proteins: Clarifying the puzzle
    • Arolas JL, Aviles FX, Chang JY et al (2006) Folding of small disulfide-rich proteins: clarifying the puzzle. Trends Biochem Sci 31:292-301
    • (2006) Trends Biochem Sci , vol.31 , pp. 292-301
    • Arolas, J.L.1    Aviles, F.X.2    Chang, J.Y.3
  • 17
    • 14044266878 scopus 로고    scopus 로고
    • Evidence for the underlying cause of diversity of the disulfide folding pathway
    • Chang JY (2004) Evidence for the underlying cause of diversity of the disulfide folding pathway. Biochemistry 43:4522-4529
    • (2004) Biochemistry , vol.43 , pp. 4522-4529
    • Chang, J.Y.1
  • 18
    • 0026088557 scopus 로고
    • The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor
    • Darby NJ, van Mierlo CP, Creighton TE (1991) The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor. FEBS Lett 279:61-64
    • (1991) FEBS Lett , vol.279 , pp. 61-64
    • Darby, N.J.1    Van Mierlo, C.P.2    Creighton, T.E.3
  • 19
    • 0026736195 scopus 로고
    • The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor
    • van Mierlo CP, Darby NJ, Creighton TE (1992) The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci USA 89:6775-6779
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6775-6779
    • Van Mierlo, C.P.1    Darby, N.J.2    Creighton, T.E.3
  • 20
    • 0027298344 scopus 로고
    • Structural characterization of the disulfide folding intermediates of bovine alpha-lactalbumin
    • Ewbank JJ, Creighton TE (1993) Structural characterization of the disulfide folding intermediates of bovine alpha-lactalbumin. Biochemistry 32:3694-3707
    • (1993) Biochemistry , vol.32 , pp. 3694-3707
    • Ewbank, J.J.1    Creighton, T.E.2
  • 21
    • 0027953901 scopus 로고
    • Structural characterization of a three-disulfide intermediate of ribonuclease A involved in both the folding and unfolding pathways
    • Talluri S, Rothwarf DM, Scheraga HA (1994) Structural characterization of a three-disulfide intermediate of ribonuclease A involved in both the folding and unfolding pathways. Biochemistry 33:10437-10449
    • (1994) Biochemistry , vol.33 , pp. 10437-10449
    • Talluri, S.1    Rothwarf, D.M.2    Scheraga, H.A.3
  • 22
    • 0032765075 scopus 로고    scopus 로고
    • Characterisation of the dominant oxidative folding intermediate of hen lysozyme
    • Berg B, Chung EW, Robinson CV et al
    • van den Berg B, Chung EW, Robinson CV et al (1999) Characterisation of the dominant oxidative folding intermediate of hen lysozyme. J Mol Biol 290:781-796
    • (1999) J Mol Biol , vol.290 , pp. 781-796
  • 23
    • 0025292406 scopus 로고
    • Structural effects induced by removal of a disulfide-bridge: The X-ray structure of the C30A/C51A mutant of basic pancreatic trypsin inhibitor at 1.6 A
    • Eigenbrot C, Randal M, Kossiakoff AA (1990) Structural effects induced by removal of a disulfide-bridge: the X-ray structure of the C30A/C51A mutant of basic pancreatic trypsin inhibitor at 1.6 A. Protein Eng 3:591-598
    • (1990) Protein Eng , vol.3 , pp. 591-598
    • Eigenbrot, C.1    Randal, M.2    Kossiakoff, A.A.3
  • 24
    • 0027414479 scopus 로고
    • Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1 H and 15 N resonance assignments and determination of backbone dynamics from 15 N relaxation measurements
    • van Mierlo CP, Darby NJ, Keeler J et al (1993) Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1 H and 15 N resonance assignments and determination of backbone dynamics from 15 N relaxation measurements. J Mol Biol 229:1125-1146
    • (1993) J Mol Biol , vol.229 , pp. 1125-1146
    • Van Mierlo, C.P.1    Darby, N.J.2    Keeler, J.3
  • 25
    • 0030708903 scopus 로고    scopus 로고
    • Structural characterization of an analog of the major rate-determining disulfide folding intermediate of bovine pancreatic ribonuclease A
    • Laity JH, Lester CC, Shimotakahara S et al (1997) Structural characterization of an analog of the major rate-determining disulfide folding intermediate of bovine pancreatic ribonuclease A. Biochemistry 36:12683-12699
    • (1997) Biochemistry , vol.36 , pp. 12683-12699
    • Laity, J.H.1    Lester, C.C.2    Shimotakahara, S.3
  • 26
    • 0034107224 scopus 로고    scopus 로고
    • Early intermediates in the PDI-assisted folding of ribonuclease A
    • Vinci F, Ruoppolo M, Pucci P et al (2000) Early intermediates in the PDI-assisted folding of ribonuclease A. Protein Sci 9:525-535
    • (2000) Protein Sci , vol.9 , pp. 525-535
    • Vinci, F.1    Ruoppolo, M.2    Pucci, P.3
  • 27
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: Predominance of native intermediates
    • Weissman JS, Kim PS (1991) Reexamination of the folding of BPTI: predominance of native intermediates. Science 253:1386-1393
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 28
    • 0028818785 scopus 로고
    • A kinetic explanation for the rearrangement pathway of BPTI folding
    • Weissman JS, Kim PS (1995) A kinetic explanation for the rearrangement pathway of BPTI folding. Nat Struct Biol 2:1123-1130
    • (1995) Nat Struct Biol , vol.2 , pp. 1123-1130
    • Weissman, J.S.1    Kim, P.S.2
  • 29
    • 0026628991 scopus 로고
    • Native and non-native intermediates in the BPTI folding pathway
    • Goldenberg DP (1992) Native and non-native intermediates in the BPTI folding pathway. Trends Biochem Sci 17:257-261
    • (1992) Trends Biochem Sci , vol.17 , pp. 257-261
    • Goldenberg, D.P.1
  • 30
    • 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 AR, Lappi AK, Saaranen MJ et al (2009) Efficient peroxide-mediated oxidative refolding of a protein at physiological pH and implications for oxidative folding in the endoplasmic reticulum. Antioxid Redox Signal 11:963-970
    • (2009) Antioxid Redox Signal , vol.11 , pp. 963-970
    • Karala, A.R.1    Lappi, A.K.2    Saaranen, M.J.3
  • 31
    • 0028303047 scopus 로고
    • Controlling the speed of hirudin folding
    • Chang JY (1994) Controlling the speed of hirudin folding. Biochem J 300(Pt 3):643-650
    • (1994) Biochem J , vol.300 , Issue.PART 3 , pp. 643-650
    • Chang, J.Y.1
  • 32
    • 0033462152 scopus 로고    scopus 로고
    • Comparison of the kinetics of S-S bond, secondary structure, and active site formation during refolding of reduced denatured hen egg white lysozyme
    • Roux P, Ruoppolo M, Chaffotte AF et al (1999) Comparison of the kinetics of S-S bond, secondary structure, and active site formation during refolding of reduced denatured hen egg white lysozyme. Protein Sci 8:2751-2760
    • (1999) Protein Sci , vol.8 , pp. 2751-2760
    • Roux, P.1    Ruoppolo, M.2    Chaffotte, A.F.3
  • 33
    • 0029861578 scopus 로고    scopus 로고
    • Glutathione-dependent pathways of refolding of RNase T1 by oxidation and disulfide isomerization: Catalysis by protein disulfide isomerase
    • Ruoppolo M, Freedman RB, Pucci P et al (1996) Glutathione-dependent pathways of refolding of RNase T1 by oxidation and disulfide isomerization: catalysis by protein disulfide isomerase. Biochemistry 35:13636-13646
    • (1996) Biochemistry , vol.35 , pp. 13636-13646
    • Ruoppolo, M.1    Freedman, R.B.2    Pucci, P.3
  • 34
    • 0029155302 scopus 로고
    • Refolding by disulfide isomerization: The mixed disulfide between ribonuclease T1 and glutathione as a model refolding substrate
    • Ruoppolo M, Freedman RB (1995) Refolding by disulfide isomerization: the mixed disulfide between ribonuclease T1 and glutathione as a model refolding substrate. Biochemistry 34:9380-9388
    • (1995) Biochemistry , vol.34 , pp. 9380-9388
    • Ruoppolo, M.1    Freedman, R.B.2
  • 35
    • 38349086453 scopus 로고    scopus 로고
    • Balancing conformational and oxidative kinetic traps during the folding of bovine pancreatic trypsin inhibitor (BPTI) with glutathione and glutathione disulfide
    • Kibria FM, Lees WJ (2008) Balancing conformational and oxidative kinetic traps during the folding of bovine pancreatic trypsin inhibitor (BPTI) with glutathione and glutathione disulfide. J Am Chem Soc 130:796-797
    • (2008) J Am Chem Soc , vol.130 , pp. 796-797
    • Kibria, F.M.1    Lees, W.J.2
  • 36
    • 73649177752 scopus 로고
    • Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver
    • Goldberger RF, Epstein CJ, Anfinsen CB (1963) Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. J Biol Chem 238:628-635
    • (1963) J Biol Chem , vol.238 , pp. 628-635
    • Goldberger, R.F.1    Epstein, C.J.2    Anfinsen, C.B.3
  • 37
    • 0142019685 scopus 로고
    • The enzymic reactivation of reduced ribonuclease
    • Venetianer P, Straub FB (1963) The enzymic reactivation of reduced ribonuclease. Biochim Biophys Acta 67:166-168
    • (1963) Biochim Biophys Acta , vol.67 , pp. 166-168
    • Venetianer, P.1    Straub, F.B.2
  • 39
    • 0000870776 scopus 로고
    • Native disulphide bond formation in protein biosynthesis evidence for the role of protein disulphide isomerase
    • Freedman RB (1984) Native disulphide bond formation in protein biosynthesis: evidence for the role of protein disulphide isomerase. Trends Biochem Sci 9:438-441
    • (1984) Trends Biochem Sci , vol.9 , pp. 438-441
    • Freedman, R.B.1
  • 40
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: Building bridges in protein folding
    • Freedman RB, Hirst TR, Tuite MF (1994) Protein disulphide isomerase: building bridges in protein folding. Trends Biochem Sci 19:331-336
    • (1994) Trends Biochem Sci , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 41
    • 0019317631 scopus 로고
    • Catalysis by protein-disulphide isomerase of the unfolding and refolding of proteins with disulphide bonds
    • Creighton TE, Hillson DA, Freedman RB (1980) Catalysis by protein-disulphide isomerase of the unfolding and refolding of proteins with disulphide bonds. J Mol Biol 142:43-62
    • (1980) J Mol Biol , vol.142 , pp. 43-62
    • Creighton, T.E.1    Hillson, D.A.2    Freedman, R.B.3
  • 42
    • 0027171355 scopus 로고
    • On the biosynthesis of bovine pancreatic trypsin inhibitor (BPTI). Structure, processing, folding and disulphide bond formation of the precursor in vitro and in microsomes
    • Creighton TE, Bagley CJ, Cooper L et al (1993) On the biosynthesis of bovine pancreatic trypsin inhibitor (BPTI). Structure, processing, folding and disulphide bond formation of the precursor in vitro and in microsomes. J Mol Biol 232:1176-1196
    • (1993) J Mol Biol , vol.232 , pp. 1176-1196
    • Creighton, T.E.1    Bagley, C.J.2    Cooper, L.3
  • 43
    • 0028225291 scopus 로고
    • Dissecting the mechanism of protein disulfide isomerase: Catalysis of disulfide bond formation in a model peptide
    • Darby NJ, Freedman RB, Creighton TE (1994) Dissecting the mechanism of protein disulfide isomerase: catalysis of disulfide bond formation in a model peptide. Biochemistry 33:7937-7947
    • (1994) Biochemistry , vol.33 , pp. 7937-7947
    • Darby, N.J.1    Freedman, R.B.2    Creighton, T.E.3
  • 44
    • 0027270735 scopus 로고
    • Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase
    • Weissman JS, Kim PS (1993) Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. Nature 365:185-188
    • (1993) Nature , vol.365 , pp. 185-188
    • Weissman, J.S.1    Kim, P.S.2
  • 45
    • 0034697982 scopus 로고    scopus 로고
    • Catalysis of the oxidative folding of bovine pancreatic ribonuclease A by protein disulfide isomerase
    • Shin HC, Scheraga HA (2000) Catalysis of the oxidative folding of bovine pancreatic ribonuclease A by protein disulfide isomerase. J Mol Biol 300:995-1003
    • (2000) J Mol Biol , vol.300 , pp. 995-1003
    • Shin, H.C.1    Scheraga, H.A.2
  • 46
    • 0037134845 scopus 로고    scopus 로고
    • Effect of protein disulfide isomerase on the ratedetermining steps of the folding of bovine pancreatic ribonuclease A
    • Shin HC, Song MC, Scheraga HA (2002) Effect of protein disulfide isomerase on the ratedetermining steps of the folding of bovine pancreatic ribonuclease A. FEBS Lett 521:77-80
    • (2002) FEBS Lett , vol.521 , pp. 77-80
    • Shin, H.C.1    Song, M.C.2    Scheraga, H.A.3
  • 47
    • 0033199237 scopus 로고    scopus 로고
    • The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase
    • van den Berg B, Chung EW, Robinson CV et al (1999) The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase. EMBO J 18:4794-4803
    • (1999) EMBO J , vol.18 , pp. 4794-4803
    • Van Den Berg, B.1    Chung, E.W.2    Robinson, C.V.3
  • 48
    • 0031776171 scopus 로고    scopus 로고
    • A single dipeptide sequence modulates the redox properties of a whole enzyme family
    • Huber-Wunderlich M, Glockshuber R (1998) A single dipeptide sequence modulates the redox properties of a whole enzyme family. Fold Des 3:161-171
    • (1998) Fold des , vol.3 , pp. 161-171
    • Huber-Wunderlich, M.1    Glockshuber, R.2
  • 49
    • 0027293791 scopus 로고
    • Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin
    • Lundstrom J, Holmgren A (1993) Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin. Biochemistry 32:6649-6655
    • (1993) Biochemistry , vol.32 , pp. 6649-6655
    • Lundstrom, J.1    Holmgren, A.2
  • 50
    • 71549132149 scopus 로고    scopus 로고
    • Protein disulfide isomerase: A critical evaluation of its function in disulfide bond formation
    • Hatahet F, Ruddock LW (2009) Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxid Redox Signal 11:2807-2850
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2807-2850
    • Hatahet, F.1    Ruddock, L.W.2
  • 51
    • 0025914427 scopus 로고
    • Mimicking the active site of protein disulfideisomerase by substitution of proline 34 in Escherichia coli thioredoxin
    • Krause G, Lundstrom J, Barea JL et al (1991) Mimicking the active site of protein disulfideisomerase by substitution of proline 34 in Escherichia coli thioredoxin. J Biol Chem 266:9494-9500
    • (1991) J Biol Chem , vol.266 , pp. 9494-9500
    • Krause, G.1    Lundstrom, J.2    Barea, J.L.3
  • 52
    • 0026793715 scopus 로고
    • A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease
    • Lundstrom J, Krause G, Holmgren A (1992) A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease. J Biol Chem 267:9047-9052
    • (1992) J Biol Chem , vol.267 , pp. 9047-9052
    • Lundstrom, J.1    Krause, G.2    Holmgren, A.3
  • 53
    • 0028222390 scopus 로고
    • Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin
    • Zapun A, Creighton TE (1994) Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin. Biochemistry 33:5202-5211
    • (1994) Biochemistry , vol.33 , pp. 5202-5211
    • Zapun, A.1    Creighton, T.E.2
  • 54
    • 0034714289 scopus 로고    scopus 로고
    • Disulfide bonds are generated by quinone reduction
    • Bader MW, Xie T, Yu CA et al (2000) Disulfide bonds are generated by quinone reduction. J Biol Chem 275:26082-26088
    • (2000) J Biol Chem , vol.275 , pp. 26082-26088
    • Bader, M.W.1    Xie, T.2    Yu, C.A.3
  • 55
    • 0028953741 scopus 로고
    • Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase
    • Darby NJ, Creighton TE (1995) Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase. Biochemistry 34:3576-3587
    • (1995) Biochemistry , vol.34 , pp. 3576-3587
    • Darby, N.J.1    Creighton, T.E.2
  • 56
    • 0031736826 scopus 로고    scopus 로고
    • Expression of active human tissue-type plasminogen activator in Escherichia coli
    • Qiu J, Swartz JR, Georgiou G (1998) Expression of active human tissue-type plasminogen activator in Escherichia coli. Appl Environ Microbiol 64:4891-4896
    • (1998) Appl Environ Microbiol , vol.64 , pp. 4891-4896
    • Qiu, J.1    Swartz, J.R.2    Georgiou, G.3
  • 58
    • 15744375548 scopus 로고    scopus 로고
    • The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC
    • Berkmen M, Boyd D, Beckwith J (2005) The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC. J Biol Chem 280:11387-11394
    • (2005) J Biol Chem , vol.280 , pp. 11387-11394
    • Berkmen, M.1    Boyd, D.2    Beckwith, J.3
  • 59
    • 35748965031 scopus 로고    scopus 로고
    • The oxidase DsbA folds a protein with a nonconsecutive disulfide
    • Messens J, Collet JF, Van Belle K et al (2007) The oxidase DsbA folds a protein with a nonconsecutive disulfide. J Biol Chem 282:31302-31307
    • (2007) J Biol Chem , vol.282 , pp. 31302-31307
    • Messens, J.1    Collet, J.F.2    Van Belle, K.3
  • 60
    • 0028949156 scopus 로고
    • Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
    • Zapun A,Missiakas D, Raina S et al (1995) Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 34:5075-5089
    • (1995) Biochemistry , vol.34 , pp. 5075-5089
    • Zapun Amissiakas, D.1    Raina, S.2
  • 61
    • 0030875033 scopus 로고    scopus 로고
    • Interactions between protein disulphide isomerase and peptides
    • Klappa P, Hawkins HC, Freedman RB (1997) Interactions between protein disulphide isomerase and peptides. Eur J Biochem 248:37-42
    • (1997) Eur J Biochem , vol.248 , pp. 37-42
    • Klappa, P.1    Hawkins, H.C.2    Freedman, R.B.3
  • 62
    • 0032523820 scopus 로고    scopus 로고
    • A pancreas-specific glycosylated protein disulphide-isomerase binds to misfolded proteins and peptides with an interaction inhibited by oestrogens
    • Klappa P, Stromer T, Zimmermann R et al (1998) A pancreas-specific glycosylated protein disulphide-isomerase binds to misfolded proteins and peptides with an interaction inhibited by oestrogens. Eur J Biochem 254:63-69
    • (1998) Eur J Biochem , vol.254 , pp. 63-69
    • Klappa, P.1    Stromer, T.2    Zimmermann, R.3
  • 63
    • 0032481380 scopus 로고    scopus 로고
    • The b0 domain provides the principal peptidebinding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
    • Klappa P, Ruddock LW, Darby NJ et al (1998) The b0 domain provides the principal peptidebinding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J 17:927-935
    • (1998) EMBO J , vol.17 , pp. 927-935
    • Klappa, P.1    Ruddock, L.W.2    Darby, N.J.3
  • 64
    • 0034048836 scopus 로고    scopus 로고
    • Specificity in substrate binding by protein folding catalysts: Tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp
    • Ruddock LW, Freedman RB, Klappa P (2000) Specificity in substrate binding by protein folding catalysts: tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp. Protein Sci 9:758-764
    • (2000) Protein Sci , vol.9 , pp. 758-764
    • Ruddock, L.W.1    Freedman, R.B.2    Klappa, P.3
  • 65
    • 0028131648 scopus 로고
    • Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds
    • Cai H, Wang CC, Tsou CL (1994) Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds. J Biol Chem 269:24550-24552
    • (1994) J Biol Chem , vol.269 , pp. 24550-24552
    • Cai, H.1    Wang, C.C.2    Tsou, C.L.3
  • 66
    • 0029058524 scopus 로고
    • Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese
    • Song JL, Wang CC (1995) Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese. Eur J Biochem 231:312-316
    • (1995) Eur J Biochem , vol.231 , pp. 312-316
    • Song, J.L.1    Wang, C.C.2
  • 67
    • 0032540353 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen
    • Wilson R, Lees JF, Bulleid NJ (1998) Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen. J Biol Chem 273:9637-9643
    • (1998) J Biol Chem , vol.273 , pp. 9637-9643
    • Wilson, R.1    Lees, J.F.2    Bulleid, N.J.3
  • 68
    • 0032079359 scopus 로고    scopus 로고
    • Thiol-independent interaction of protein disulphide isomerase with type X collagen during intra-cellular folding and assembly
    • McLaughlin SH, Bulleid NJ (1998) Thiol-independent interaction of protein disulphide isomerase with type X collagen during intra-cellular folding and assembly. Biochem J 331 (Pt 3):793-800
    • (1998) Biochem J , vol.331 , Issue.PART 3 , pp. 793-800
    • McLaughlin, S.H.1    Bulleid, N.J.2
  • 69
    • 0031616949 scopus 로고    scopus 로고
    • Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases
    • Kivirikko KI, Pihlajaniemi T (1998) Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases. Adv Enzymol Relat Areas Mol Biol 72:325-398
    • (1998) Adv Enzymol Relat Areas Mol Biol , vol.72 , pp. 325-398
    • Kivirikko, K.I.1    Pihlajaniemi, T.2
  • 70
    • 0037244002 scopus 로고    scopus 로고
    • Microsomal triglyceride transfer protein and its role in apoB-lipoprotein assembly
    • Hussain MM, Shi J, Dreizen P (2003) Microsomal triglyceride transfer protein and its role in apoB-lipoprotein assembly. J Lipid Res 44:22-32
    • (2003) J Lipid Res , vol.44 , pp. 22-32
    • Hussain, M.M.1    Shi, J.2    Dreizen, P.3
  • 71
    • 8844224950 scopus 로고    scopus 로고
    • Production of human prolyl 4-hydroxylase in Escherichia coli
    • Kersteen EA, Higgin JJ, Raines RT (2004) Production of human prolyl 4-hydroxylase in Escherichia coli. Protein Expr Purif 38:279-291
    • (2004) Protein Expr Purif , vol.38 , pp. 279-291
    • Kersteen, E.A.1    Higgin, J.J.2    Raines, R.T.3
  • 72
    • 0026632893 scopus 로고
    • Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum
    • Zapun A, Creighton TE, Rowling PJ et al (1992) Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum. Proteins 14:10-15
    • (1992) Proteins , vol.14 , pp. 10-15
    • Zapun, A.1    Creighton, T.E.2    Rowling, P.J.3
  • 73
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C, Sinskey AJ, Lodish HF (1992) Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257:1496-1502
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 74
    • 1242294484 scopus 로고    scopus 로고
    • A major fraction of endoplasmic reticulumlocated glutathione is present as mixed disulfides with protein
    • Bass R, Ruddock LW, Klappa P et al (2004) A major fraction of endoplasmic reticulumlocated glutathione is present as mixed disulfides with protein. J Biol Chem 279:5257-5262
    • (2004) J Biol Chem , vol.279 , pp. 5257-5262
    • Bass, R.1    Ruddock, L.W.2    Klappa, P.3
  • 75
    • 39749200944 scopus 로고    scopus 로고
    • Assessment of endoplasmic reticulum glutathione redox status is confounded by extensive ex vivo oxidation
    • Dixon BM, Heath SH, Kim R et al (2008) Assessment of endoplasmic reticulum glutathione redox status is confounded by extensive ex vivo oxidation. Antioxid Redox Signal 10: 963-972
    • (2008) Antioxid Redox Signal , vol.10 , pp. 963-972
    • Dixon, B.M.1    Heath, S.H.2    Kim, R.3
  • 76
    • 41449116766 scopus 로고    scopus 로고
    • Ero1 and redox homeostasis in the endoplasmic reticulum
    • Sevier CS, Kaiser CA (2008) Ero1 and redox homeostasis in the endoplasmic reticulum. Biochim Biophys Acta 1783:549-556
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 549-556
    • Sevier, C.S.1    Kaiser, C.A.2
  • 77
    • 0035890070 scopus 로고    scopus 로고
    • Manipulation of oxidative protein folding and PDI redox state in mammalian cells
    • Mezghrani A, Fassio A, Benham A et al (2001) Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J 20:6288-6296
    • (2001) EMBO J , vol.20 , pp. 6288-6296
    • Mezghrani, A.1    Fassio, A.2    Benham, A.3
  • 78
    • 0034711439 scopus 로고    scopus 로고
    • Biochemical basis of oxidative protein folding in the endoplasmic reticulum
    • Tu BP, Ho-Schleyer SC, Travers KJ et al (2000) Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290:1571-1574
    • (2000) Science , vol.290 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3
  • 79
    • 33644868738 scopus 로고    scopus 로고
    • Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation
    • Kulp MS, Frickel EM, Ellgaard L et al (2006) Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation. J Biol Chem 281:876-884
    • (2006) J Biol Chem , vol.281 , pp. 876-884
    • Kulp, M.S.1    Frickel, E.M.2    Ellgaard, L.3
  • 80
    • 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 a0 domains of protein-disulfide isomerase
    • Wang L, Li SJ, Sidhu A et al (2009) Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a0 domains of protein-disulfide isomerase. J Biol Chem 284:199-206
    • (2009) J Biol Chem , vol.284 , pp. 199-206
    • Wang, L.1    Li, S.J.2    Sidhu, A.3
  • 81
    • 0023720121 scopus 로고
    • Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes
    • Bulleid NJ, Freedman RB (1988) Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes. Nature 335:649-651
    • (1988) Nature , vol.335 , pp. 649-651
    • Bulleid, N.J.1    Freedman, R.B.2
  • 82
    • 0027250528 scopus 로고
    • Post-translational folding of influenza hemagglutinin in isolated endoplasmic reticulum-derived microsomes
    • Marquardt T, Hebert DN, Helenius A (1993) Post-translational folding of influenza hemagglutinin in isolated endoplasmic reticulum-derived microsomes. J Biol Chem 268: 19618-19625
    • (1993) J Biol Chem , vol.268 , pp. 19618-19625
    • Marquardt, T.1    Hebert, D.N.2    Helenius, A.3
  • 83
    • 0026604334 scopus 로고
    • Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum
    • Braakman I, Helenius J, Helenius A (1992) Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. EMBO J 11:1717-1722
    • (1992) EMBO J , vol.11 , pp. 1717-1722
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 84
    • 0037147191 scopus 로고    scopus 로고
    • Coordinated nonvectorial folding in a newly synthesized multidomain protein
    • Jansens A, van Duijn E, Braakman I (2002) Coordinated nonvectorial folding in a newly synthesized multidomain protein. Science 298:2401-2403
    • (2002) Science , vol.298 , pp. 2401-2403
    • Jansens, A.1    Van Duijn, E.2    Braakman, I.3
  • 85
    • 0038725418 scopus 로고    scopus 로고
    • Folding of HIV-1 envelope glycoprotein involves extensive isomerization of disulfide bonds and conformation-dependent leader peptide cleavage
    • Land A, Zonneveld D, Braakman I (2003) Folding of HIV-1 envelope glycoprotein involves extensive isomerization of disulfide bonds and conformation-dependent leader peptide cleavage. FASEB J 17:1058-1067
    • (2003) FASEB J , vol.17 , pp. 1058-1067
    • Land, A.1    Zonneveld, D.2    Braakman, I.3
  • 86
    • 0022387362 scopus 로고
    • Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
    • Edman JC, Ellis L, Blacher RW et al (1985) Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature 317:267-270
    • (1985) Nature , vol.317 , pp. 267-270
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3
  • 87
    • 33746298040 scopus 로고    scopus 로고
    • Protein disulfide isomerase: The structure of oxidative folding
    • Gruber CW, Cemazar M, Heras B et al (2006) Protein disulfide isomerase: the structure of oxidative folding. Trends Biochem Sci 31:455-464
    • (2006) Trends Biochem Sci , vol.31 , pp. 455-464
    • Gruber, C.W.1    Cemazar, M.2    Heras, B.3
  • 88
    • 0032920177 scopus 로고    scopus 로고
    • On the role of the cis-proline residue in the active site of DsbA
    • Charbonnier JB, Belin P, Moutiez M et al (1999) On the role of the cis-proline residue in the active site of DsbA. Protein Sci 8:96-105
    • (1999) Protein Sci , vol.8 , pp. 96-105
    • Charbonnier, J.B.1    Belin, P.2    Moutiez, M.3
  • 89
    • 30344444015 scopus 로고    scopus 로고
    • The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites
    • Tian G, Xiang S, Noiva R et al (2006) The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell 124:61-73
    • (2006) Cell , vol.124 , pp. 61-73
    • Tian, G.1    Xiang, S.2    Noiva, R.3
  • 90
    • 34250206320 scopus 로고    scopus 로고
    • A conserved cis-proline precludes metal binding by the active site thiolates in members of the thioredoxin family of proteins
    • Su D, Berndt C, Fomenko DE et al (2007) A conserved cis-proline precludes metal binding by the active site thiolates in members of the thioredoxin family of proteins. Biochemistry 46:6903-6910
    • (2007) Biochemistry , vol.46 , pp. 6903-6910
    • Su, D.1    Berndt, C.2    De, F.3
  • 91
    • 0032897837 scopus 로고    scopus 로고
    • The structure in solution of the b domain of protein disulfide isomerase
    • Kemmink J, Dijkstra K, Mariani M et al (1999) The structure in solution of the b domain of protein disulfide isomerase. J Biomol NMR 13:357-368
    • (1999) J Biomol NMR , vol.13 , pp. 357-368
    • Kemmink, J.1    Dijkstra, K.2    Mariani, M.3
  • 92
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell JC, McGovern K, Beckwith J (1991) Identification of a protein required for disulfide bond formation in vivo. Cell 67:581-589
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 93
    • 0028360184 scopus 로고
    • Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo
    • Nelson JW, Creighton TE (1994) Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry 33:5974-5983
    • (1994) Biochemistry , vol.33 , pp. 5974-5983
    • Nelson, J.W.1    Creighton, T.E.2
  • 95
    • 0031024788 scopus 로고    scopus 로고
    • Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: Structural and functional characterization of mutants of Asp 26 and Lys 57
    • Dyson HJ, Jeng MF, Tennant LL et al (1997) Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: structural and functional characterization of mutants of Asp 26 and Lys 57. Biochemistry 36:2622-2636
    • (1997) Biochemistry , vol.36 , pp. 2622-2636
    • Dyson, H.J.1    Jeng, M.F.2    Tennant, L.L.3
  • 96
    • 0026511733 scopus 로고
    • Relationship between electrostatics and redox function in human thioredoxin: Characterization of pH titration shifts using twodimensional homo- and heteronuclear NMR
    • Forman-Kay JD, Clore GM, Gronenborn AM (1992) Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using twodimensional homo- and heteronuclear NMR. Biochemistry 31:3442-3452
    • (1992) Biochemistry , vol.31 , pp. 3442-3452
    • Forman-Kay, J.D.1    Clore, G.M.2    Gronenborn, A.M.3
  • 97
    • 0029934516 scopus 로고    scopus 로고
    • The CXXC motif: Imperatives for the formation of native disulfide bonds in the cell
    • Chivers PT, Laboissiere MC, Raines RT (1996) The CXXC motif: imperatives for the formation of native disulfide bonds in the cell. EMBO J 15:2659-2667
    • (1996) EMBO J , vol.15 , pp. 2659-2667
    • Chivers, P.T.1    Laboissiere, M.C.2    Raines, R.T.3
  • 98
    • 77956514975 scopus 로고    scopus 로고
    • The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1alpha
    • Chambers JE, Tavender TJ, Oka OB et al (2010) The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1alpha. J Biol Chem 285:29200-29207
    • (2010) J Biol Chem , vol.285 , pp. 29200-29207
    • Chambers, J.E.1    Tavender, T.J.2    Oka, O.B.3
  • 99
    • 0030934272 scopus 로고    scopus 로고
    • The CXXC motif: A rheostat in the active site
    • Chivers PT, Prehoda KE, Raines RT (1997) The CXXC motif: a rheostat in the active site. Biochemistry 36:4061-4066
    • (1997) Biochemistry , vol.36 , pp. 4061-4066
    • Chivers, P.T.1    Prehoda, K.E.2    Raines, R.T.3
  • 100
    • 65649140478 scopus 로고    scopus 로고
    • Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue
    • Ren G, Stephan D, Xu Z et al (2009) Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue. J Biol Chem 284:10150-10159
    • (2009) J Biol Chem , vol.284 , pp. 10150-10159
    • Ren, G.1    Stephan, D.2    Xu, Z.3
  • 101
    • 0025865875 scopus 로고
    • Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis
    • Krause G, Holmgren A (1991) Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis. J Biol Chem 266:4056-4066
    • (1991) J Biol Chem , vol.266 , pp. 4056-4066
    • Krause, G.1    Holmgren, A.2
  • 102
    • 24644501647 scopus 로고    scopus 로고
    • Catalysis of protein disulfide bond isomerization in a homogeneous substrate
    • Kersteen EA, Barrows SR, Raines RT (2005) Catalysis of protein disulfide bond isomerization in a homogeneous substrate. Biochemistry 44:12168-12178
    • (2005) Biochemistry , vol.44 , pp. 12168-12178
    • Kersteen, E.A.1    Barrows, S.R.2    Raines, R.T.3
  • 103
    • 46449120166 scopus 로고    scopus 로고
    • Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail
    • Wang L, Vavassori S, Li S et al (2008) Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail. EMBO Rep 9:642-647
    • (2008) EMBO Rep , vol.9 , pp. 642-647
    • Wang, L.1    Vavassori, S.2    Li, S.3
  • 104
    • 77649275063 scopus 로고    scopus 로고
    • Modulation of an active-site cysteine pKa allows PDI to act as a catalyst of both disulfide bond formation and isomerization
    • Karala AR, Lappi AK, Ruddock LW (2010) Modulation of an active-site cysteine pKa allows PDI to act as a catalyst of both disulfide bond formation and isomerization. J Mol Biol 396:883-892
    • J Mol Biol , vol.396 , pp. 883-892
    • Karala, A.R.1    Lappi, A.K.2
  • 105
    • 0344255647 scopus 로고    scopus 로고
    • A conserved arginine plays a role in the catalytic cycle of the protein disulphide isomerases
    • Lappi AK, Lensink MF, Alanen HI et al (2004) A conserved arginine plays a role in the catalytic cycle of the protein disulphide isomerases. J Mol Biol 335:283-295
    • (2004) J Mol Biol , vol.335 , pp. 283-295
    • Lappi, A.K.1    Lensink, M.F.2    Alanen, H.I.3
  • 106
    • 0029093531 scopus 로고
    • Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase
    • Darby NJ, Creighton TE (1995) Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase. Biochemistry 34:11725-11735
    • (1995) Biochemistry , vol.34 , pp. 11725-11735
    • Darby, N.J.1    Creighton, T.E.2
  • 107
    • 0032512878 scopus 로고    scopus 로고
    • The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency
    • Darby NJ, Penka E, Vincentelli R (1998) The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency. J Mol Biol 276:239-247
    • (1998) J Mol Biol , vol.276 , pp. 239-247
    • Darby, N.J.1    Penka, E.2    Vincentelli, R.3
  • 108
    • 0037406092 scopus 로고    scopus 로고
    • Mutations in domain a0 of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A
    • Ruoppolo M, Orru S, Talamo F et al (2003) Mutations in domain a0 of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A. Protein Sci 12:939-952
    • (2003) Protein Sci , vol.12 , pp. 939-952
    • Ruoppolo, M.1    Orru, S.2    Talamo, F.3
  • 109
    • 77952680368 scopus 로고    scopus 로고
    • Bacitracin is not a specific inhibitor of protein disulfide isomerase
    • Karala AR, Ruddock LW (2010) Bacitracin is not a specific inhibitor of protein disulfide isomerase. FEBS J 277:2454-2462
    • FEBS J , vol.277 , pp. 2454-2462
    • Karala, A.R.1
  • 110
    • 0036371371 scopus 로고    scopus 로고
    • Model peptide substrates and ligands in analysis of action of mammalian protein disulfide-isomerase
    • Freedman RB, Klappa P, Ruddock LW(2002) Model peptide substrates and ligands in analysis of action of mammalian protein disulfide-isomerase. Methods Enzymol 348:342-354
    • (2002) Methods Enzymol , vol.348 , pp. 342-354
    • Freedman, R.B.1    Klappa, P.2    Ruddock, L.W.3
  • 111
    • 60349123960 scopus 로고    scopus 로고
    • Solution structure of the bb' domains of human protein disulfide isomerase
    • Denisov AY, Maattanen P, Dabrowski C et al (2009) Solution structure of the bb' domains of human protein disulfide isomerase. FEBS J 276:1440-1449
    • (2009) FEBS J , vol.276 , pp. 1440-1449
    • Denisov, A.Y.1    Maattanen, P.2    Dabrowski, C.3
  • 112
    • 70350124054 scopus 로고    scopus 로고
    • Mapping of the ligand binding site on the b' domain of human PDI; Interaction with peptide ligands and the x-linker region
    • Byrne LJ, Sidhu A, Wallis AK et al (2009) Mapping of the ligand binding site on the b' domain of human PDI; interaction with peptide ligands and the x-linker region. Biochem J 423:209-217
    • (2009) Biochem J , vol.423 , pp. 209-217
    • Byrne, L.J.1    Sidhu, A.2    Wallis, A.K.3
  • 113
    • 77955653538 scopus 로고    scopus 로고
    • Domain a0 of protein disulfide isomerase plays key role in inhibiting alpha-synuclein fibril formation
    • doi:10.1007/s12192-009-0157-2
    • Cheng H, Wang L, Wang CC (2009) Domain a0 of protein disulfide isomerase plays key role in inhibiting alpha-synuclein fibril formation. Cell Stress Chaperones 15:415-421. doi:10.1007/s12192-009-0157-2
    • (2009) Cell Stress Chaperones , vol.15 , pp. 415-421
    • Cheng, H.1    Wang, L.2    Wang, C.C.3
  • 114
    • 77449149046 scopus 로고    scopus 로고
    • Redox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface
    • Serve O, Kamiya Y, Maeno A et al (2010) Redox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface. J Mol Biol 396:361-374
    • (2010) J Mol Biol , vol.396 , pp. 361-374
    • Serve, O.1    Kamiya, Y.2    Maeno, A.3
  • 115
    • 73149111990 scopus 로고    scopus 로고
    • The ligand-binding b0 domain of human protein disulphide-isomerase mediates homodimerization
    • Wallis AK, Sidhu A, Byrne LJ et al (2009) The ligand-binding b0 domain of human protein disulphide-isomerase mediates homodimerization. Protein Sci 18:2569-2577
    • (2009) Protein Sci , vol.18 , pp. 2569-2577
    • Wallis, A.K.1    Sidhu, A.2    Byrne, L.J.3
  • 116
    • 57749102824 scopus 로고    scopus 로고
    • The catalytic activity of protein-disulfide isomerase requires a conformationally flexible molecule
    • Tian G, Kober FX, Lewandrowski U et al (2008) The catalytic activity of protein-disulfide isomerase requires a conformationally flexible molecule. J Biol Chem 283:33630-33640
    • (2008) J Biol Chem , vol.283 , pp. 33630-33640
    • Tian, G.1    Kober, F.X.2    Lewandrowski, U.3
  • 117
    • 58149215628 scopus 로고    scopus 로고
    • Insights into MHC class i peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer
    • Dong G, Wearsch PA, Peaper DR et al (2009) Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer. Immunity 30:21-32
    • (2009) Immunity , vol.30 , pp. 21-32
    • Dong, G.1    Wearsch, P.A.2    Peaper, D.R.3
  • 118
    • 33646546083 scopus 로고    scopus 로고
    • Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: A small angle X-ray scattering study in solution
    • Li SJ, Hong XG, Shi YY et al (2006) Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: a small angle X-ray scattering study in solution. J Biol Chem 281:6581-6588
    • (2006) J Biol Chem , vol.281 , pp. 6581-6588
    • Li, S.J.1    Hong, X.G.2    Shi, Y.Y.3
  • 119
    • 0031127294 scopus 로고    scopus 로고
    • The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules
    • Kemmink J, Darby NJ, Dijkstra K et al (1997) The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules. Curr Biol 7:239-245
    • (1997) Curr Biol , vol.7 , pp. 239-245
    • Kemmink, J.1    Darby, N.J.2    Dijkstra, K.3
  • 120
    • 0031954077 scopus 로고    scopus 로고
    • Experimental and theoretical analyses of the domain architecture of mammalian protein disulphide-isomerase
    • Freedman RB, Gane PJ, Hawkins HC et al (1998) Experimental and theoretical analyses of the domain architecture of mammalian protein disulphide-isomerase. Biol Chem 379: 321-328
    • (1998) Biol Chem , vol.379 , pp. 321-328
    • Freedman, R.B.1    Gane, P.J.2    Hawkins, H.C.3
  • 121
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulphide-isomerase family: Unravelling a string of folds
    • Ferrari DM, Soling HD (1999) The protein disulphide-isomerase family: unravelling a string of folds. Biochem J 339(Pt 1):1-10
    • (1999) Biochem J 339(Pt 1 , pp. 1-10
    • Ferrari, D.M.1    Soling, H.D.2
  • 122
    • 0043264811 scopus 로고    scopus 로고
    • Defining the domain boundaries of the human protein disulfide isomerases
    • Alanen HI, Salo KE, Pekkala M et al (2003) Defining the domain boundaries of the human protein disulfide isomerases. Antioxid Redox Signal 5:367-374
    • (2003) Antioxid Redox Signal , vol.5 , pp. 367-374
    • Alanen, H.I.1    Salo, K.E.2    Pekkala, M.3
  • 123
    • 12144288546 scopus 로고    scopus 로고
    • Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase
    • Pirneskoski A, Klappa P, Lobell M et al (2004) Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase. J Biol Chem 279:10374-10381
    • (2004) J Biol Chem , vol.279 , pp. 10374-10381
    • Pirneskoski, A.1    Klappa, P.2    Lobell, M.3
  • 124
    • 77449149046 scopus 로고    scopus 로고
    • Redox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface
    • Serve O, Kamiya Y, Maeno A et al (2009) Redox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface. J Mol Biol 396:361-374
    • (2009) J Mol Biol , vol.396 , pp. 361-374
    • Serve, O.1    Kamiya, Y.2    Maeno, A.3
  • 125
    • 0036198797 scopus 로고    scopus 로고
    • Protein disulfide isomerases exploit synergy between catalytic and specific binding domains
    • Freedman RB, Klappa P, Ruddock LW (2002) Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO Rep 3:136-140
    • (2002) EMBO Rep , vol.3 , pp. 136-140
    • Freedman, R.B.1    Klappa, P.2    Ruddock, L.W.3
  • 126
    • 0035815678 scopus 로고    scopus 로고
    • Domains b0 and a0 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
    • Pirneskoski A, Ruddock LW, Klappa P et al (2001) Domains b0 and a0 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 276:11287-11293
    • (2001) J Biol Chem , vol.276 , pp. 11287-11293
    • Pirneskoski, A.1    Ruddock, L.W.2    Klappa, P.3
  • 127
    • 14044256548 scopus 로고    scopus 로고
    • Three binding sites in protein-disulfide isomerase cooperate in collagen prolyl 4-hydroxylase tetramer assembly
    • Koivunen P, Salo KE, Myllyharju J et al (2005) Three binding sites in protein-disulfide isomerase cooperate in collagen prolyl 4-hydroxylase tetramer assembly. J Biol Chem 280:5227-5235
    • (2005) J Biol Chem , vol.280 , pp. 5227-5235
    • Koivunen, P.1    Salo, K.E.2    Myllyharju, J.3
  • 128
    • 77957773053 scopus 로고    scopus 로고
    • Crystal structures of human Ero1alpha reveal the mechanisms of regulated and targeted oxidation of PDI
    • Inaba K, Masui S, Iida H et al (2010) Crystal structures of human Ero1alpha reveal the mechanisms of regulated and targeted oxidation of PDI. EMBO J 29:3330-3343
    • (2010) EMBO J , vol.29 , pp. 3330-3343
    • Inaba, K.1    Masui, S.2    Iida, H.3
  • 129
    • 77956625219 scopus 로고    scopus 로고
    • A structural overview of the PDI family of proteins
    • Kozlov G, Maattanen P, Thomas DY et al (2010) A structural overview of the PDI family of proteins. FEBS J 19:3924-3936
    • (2010) FEBS J , vol.19 , pp. 3924-3936
    • Kozlov, G.1    Maattanen, P.2    Thomas, D.Y.3
  • 130
    • 53549090995 scopus 로고    scopus 로고
    • Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b0 domain
    • Nguyen VD, Wallis K, Howard MJ et al (2008) Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b0 domain. J Mol Biol 383:1144-1155
    • (2008) J Mol Biol , vol.383 , pp. 1144-1155
    • Nguyen, V.D.1    Wallis, K.2    Howard, M.J.3
  • 131
    • 77956234972 scopus 로고    scopus 로고
    • Plasticity of human protein disulphide isomerase: Evidence for mobility around the x-linker region and its functional significance
    • Wang C, Chen S, Wang X et al (2010) Plasticity of human protein disulphide isomerase: evidence for mobility around the x-linker region and its functional significance. J Biol Chem 35:26788-26797
    • (2010) J Biol Chem , vol.35 , pp. 26788-26797
    • Wang, C.1    Chen, S.2    Wang, X.3
  • 132
    • 0035868331 scopus 로고    scopus 로고
    • The pancreas-specific protein disulphide- isomerase PDIp interacts with a hydroxyaryl group in ligands
    • Klappa P, Freedman RB, Langenbuch M et al (2001) The pancreas-specific protein disulphide- isomerase PDIp interacts with a hydroxyaryl group in ligands. Biochem J 354: 553-559
    • (2001) Biochem J , vol.354 , pp. 553-559
    • Klappa, P.1    Freedman, R.B.2    Langenbuch, M.3
  • 133
    • 65149091065 scopus 로고    scopus 로고
    • Structure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72
    • Kozlov G, Maattanen P, Schrag JD et al (2009) Structure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72. Structure 17:651-659
    • (2009) Structure , vol.17 , pp. 651-659
    • Kozlov, G.1    Maattanen, P.2    Schrag, J.D.3
  • 134
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redoxdependent chaperone to unfold cholera toxin
    • Tsai B, Rodighiero C, Lencer WI et al (2001) Protein disulfide isomerase acts as a redoxdependent chaperone to unfold cholera toxin. Cell 104:937-948
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3
  • 136
    • 77955566504 scopus 로고    scopus 로고
    • Redox-dependent domain rearrangement of protein disulfide isomerase from a thermophilic fungus
    • Nakasako M, Maeno A, Kurimoto E et al (2010) Redox-dependent domain rearrangement of protein disulfide isomerase from a thermophilic fungus. Biochemistry 49:6953-6962
    • (2010) Biochemistry , vol.49 , pp. 6953-6962
    • Nakasako, M.1    Maeno, A.2    Kurimoto, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.