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Volumn 9, Issue 8, 2014, Pages

Compact conformations of human protein disulfide isomerase

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ASPARTIC ACID; GLUTAMINE; LYSINE; PROTEIN DISULFIDE ISOMERASE;

EID: 84922436533     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0103472     Document Type: Article
Times cited : (30)

References (29)
  • 1
    • 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
  • 2
    • 0031034725 scopus 로고    scopus 로고
    • Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2
    • DOI 10.1093/emboj/16.3.651
    • Yao Y, Zhou Y, Wang C (1997) Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2. EMBO J 16: 651-658. (Pubitemid 27067793)
    • (1997) EMBO Journal , vol.16 , Issue.3 , pp. 651-658
    • Yao, Y.1    Zhou, Y.-C.2    Wang, C.-C.3
  • 4
    • 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
  • 5
    • 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
    • Klappa P, Ruddock LW, Darby NJ, Freedman RB (1998) 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: 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
  • 6
    • 0036198797 scopus 로고    scopus 로고
    • Protein disulfide isomerases exploit synergy between catalytic and specific binding domains
    • DOI 10.1093/embo-reports/kvf035
    • Freedman RB, Klappa P, Ruddock LW (2002) Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO Rep 3: 136-140. (Pubitemid 34213490)
    • (2002) EMBO Reports , vol.3 , Issue.2 , pp. 136-140
    • Freedman, R.B.1    Klappa, P.2    Ruddock, L.W.3
  • 7
    • 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
    • Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE (1996) Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Biochemistry 35: 7684-7691.
    • (1996) Biochemistry , vol.35 , pp. 7684-7691
    • Kemmink, J.1    Darby, N.J.2    Dijkstra, K.3    Nilges, M.4    Creighton, T.E.5
  • 9
    • 53549090995 scopus 로고    scopus 로고
    • Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b' domain
    • Nguyen VD, Wallis K, Howard MJ, Haapalainen AM, Salo KE, et al. (2008) Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b' 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    Haapalainen, A.M.4    Salo, K.E.5
  • 10
    • 60349123960 scopus 로고    scopus 로고
    • Solution structure of the bb' domains of human protein disulfide isomerase
    • Denisov AY, Maattanen P, Dabrowski C, Kozlov G, Thomas DY, 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    Kozlov, G.4    Thomas, D.Y.5
  • 11
    • 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
    • Tian G, Xiang S, Noiva R, Lennarz WJ, Schindelin H (2006) The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell 124: 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
  • 12
    • 57749102824 scopus 로고    scopus 로고
    • The catalytic activity of protein-disulfide isomerase requires a conformationally flexible molecule
    • Tian G, Kober FX, Lewandrowski U, Sickmann A, Lennarz WJ, 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    Sickmann, A.4    Lennarz, W.J.5
  • 13
    • 84878866786 scopus 로고    scopus 로고
    • Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase
    • Wang C, Li W, Ren J, Fang J, Ke H, et al. (2013) Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase. Antioxid Redox Signal 19: 36-45.
    • (2013) Antioxid Redox Signal , vol.19 , pp. 36-45
    • Wang, C.1    Li, W.2    Ren, J.3    Fang, J.4    Ke, H.5
  • 14
    • 77956234972 scopus 로고    scopus 로고
    • Plasticity of human protein disulfide isomerase: Evidence for mobility around the X-linker region and its functional significance
    • Wang C, Chen S, Wang X, Wang L, Wallis AK, et al. (2010) Plasticity of human protein disulfide isomerase: evidence for mobility around the X-linker region and its functional significance. J Biol Chem 285: 26788-26797.
    • (2010) J Biol Chem , vol.285 , pp. 26788-26797
    • Wang, C.1    Chen, S.2    Wang, X.3    Wang, L.4    Wallis, A.K.5
  • 15
    • 38949151546 scopus 로고    scopus 로고
    • Molecular simulations of protein dynamics: New windows on mechanisms in biology
    • DOI 10.1038/sj.embor.7401160, PII 7401160
    • Dodson GG, Lane DP, Verma CS (2008) Molecular simulations of protein dynamics: new windows on mechanisms in biology. EMBO Rep 9: 144-150. (Pubitemid 351223451)
    • (2008) EMBO Reports , vol.9 , Issue.2 , pp. 144-150
    • Dodson, G.G.1    Lane, D.P.2    Verma, C.S.3
  • 16
    • 0346882663 scopus 로고    scopus 로고
    • ModLoop: Automated modeling of loops in protein structures
    • DOI 10.1093/bioinformatics/btg362
    • Fiser A, Sali A (2003) Mod Loop: automated modeling of loops in protein structures. Bioinformatics 19: 2500-2501. (Pubitemid 38016660)
    • (2003) Bioinformatics , vol.19 , Issue.18 , pp. 2500-2501
    • Fiser, A.1    Sali, A.2
  • 20
    • 77955653538 scopus 로고    scopus 로고
    • Domain a' of protein disulfide isomerase plays key role in inhibiting alpha-synuclein fibril formation
    • Cheng H, Wang L, Wang CC (2010) Domain a' of protein disulfide isomerase plays key role in inhibiting alpha-synuclein fibril formation. Cell Stress Chaperones 15: 415-421.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 415-421
    • Cheng, H.1    Wang, L.2    Wang, C.C.3
  • 21
    • 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
    • DOI 10.1074/jbc.M508422200
    • Li SJ, Hong XG, Shi YY, Li H, Wang CC (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. (Pubitemid 43847592)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.10 , pp. 6581-6588
    • Li, S.-J.1    Hong, X.-G.2    Shi, Y.-Y.3    Li, H.4    Wang, C.-C.5
  • 22
    • 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 proteindisulfide isomerase
    • Wang L, Li SJ, Sidhu A, Zhu L, Liang Y, 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 a' domains of proteindisulfide 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    Zhu, L.4    Liang, Y.5
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 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, Warwood S, Knight D, 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    Warwood, S.4    Knight, D.5
  • 26
    • 80052698007 scopus 로고    scopus 로고
    • Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway
    • Araki K, Nagata K (2011) Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway. J Biol Chem 286: 32705-32712.
    • (2011) J Biol Chem , vol.286 , pp. 32705-32712
    • Araki, K.1    Nagata, K.2
  • 27
    • 0025819371 scopus 로고
    • Redox properties and crosslinking of the dithiol/disulphide active sites of mammalian protein disulphideisomerase
    • Hawkins HC, de Nardi M, Freedman RB (1991) Redox properties and crosslinking of the dithiol/disulphide active sites of mammalian protein disulphideisomerase. Biochem J 275 (Pt 2): 341-348.
    • (1991) Biochem J , vol.275 , Issue.PART 2 , pp. 341-348
    • Hawkins, H.C.1    De Nardi, M.2    Freedman, R.B.3
  • 28
    • 84862907646 scopus 로고    scopus 로고
    • Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a'
    • Wang C, Yu J, Huo L, Wang L, Feng W, et al. (2012) Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a'. J Biol Chem 287: 1139-1149.
    • (2012) J Biol Chem , vol.287 , pp. 1139-1149
    • Wang, C.1    Yu, J.2    Huo, L.3    Wang, L.4    Feng, W.5
  • 29
    • 84874024456 scopus 로고    scopus 로고
    • Highresolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility
    • Amin NT, Wallis AK, Wells SA, Rowe ML, Williamson RA, et al. (2013) Highresolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility. Biochem J 450: 321-332.
    • (2013) Biochem J , vol.450 , pp. 321-332
    • Amin, N.T.1    Wallis, A.K.2    Wells, S.A.3    Rowe, M.L.4    Williamson, R.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.