메뉴 건너뛰기




Volumn , Issue , 2011, Pages 489-500

Redox-dependent chaperoning, following PDI footsteps

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84895386939     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (7)

References (46)
  • 3
    • 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, 535-48.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 535-548
    • Appenzeller-Herzog, C.1    Ellgaard, L.2
  • 4
    • 55849088319 scopus 로고    scopus 로고
    • Regulation of MHC class I assembly and peptide binding
    • Peaper, D. R. & Cresswell, P. (2008). Regulation of MHC class I assembly and peptide binding. Annu. Rev. Cell Dev. Biol., 24, 343-68.
    • (2008) Annu. Rev. Cell Dev. Biol. , vol.24 , pp. 343-368
    • Peaper, D.R.1    Cresswell, P.2
  • 5
    • 0023654667 scopus 로고
    • A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase
    • Koivu, J., Myllyla, R., Helaakoski, T., Pihlajaniemi, T., Tasanen, K. & Kivirikko, K. I. (1987). A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase. J. Biol. Chem., 262, 6447-9.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6447-6449
    • Koivu, J.1    Myllyla, R.2    Helaakoski, T.3    Pihlajaniemi, T.4    Tasanen, K.5    Kivirikko, K.I.6
  • 6
    • 0027136018 scopus 로고
    • Protein disulfide isomerase is both an enzyme and a chaperone
    • Wang, C. C. & Tsou, C. L. (1993). Protein disulfide isomerase is both an enzyme and a chaperone. FASEB J, 7, 1515-7.
    • (1993) FASEB J , vol.7 , pp. 1515-1517
    • Wang, C.C.1    Tsou, C.L.2
  • 7
    • 0037016671 scopus 로고    scopus 로고
    • Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin
    • Winter, J., Klappa, P., Freedman, R. B., Lilie, H. & Rudolph, R. (2002). Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin. J. Biol. Chem., 277, 310-7.
    • (2002) J. Biol. Chem. , vol.277 , pp. 310-317
    • Winter, J.1    Klappa, P.2    Freedman, R.B.3    Lilie, H.4    Rudolph, R.5
  • 8
    • 0035844206 scopus 로고    scopus 로고
    • Discrimination between native and non-native disulfides by protein-disulfide isomerase
    • Zheng, J. & Gilbert, H. F. (2001). Discrimination between native and non-native disulfides by protein-disulfide isomerase. J. Biol. Chem., 276, 15747-52.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15747-15752
    • Zheng, J.1    Gilbert, H.F.2
  • 9
    • 0029058524 scopus 로고
    • Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese
    • Song, J. L. & Wang, C. C. (1995). Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese. Eur. J. Biochem, 231, 312-6.
    • (1995) Eur. J. Biochem , vol.231 , pp. 312-316
    • Song, J.L.1    Wang, C.C.2
  • 10
    • 0028321726 scopus 로고
    • Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme
    • Puig A. & Gilbert, H. F. (1994). Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J. Biol. Chem., 269, 7764-71.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7764-7771
    • Puig, A.1    Gilbert, H.F.2
  • 11
    • 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
    • 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, 651-8.
    • (1997) EMBO J , vol.16 , pp. 651-658
    • Yao, Y.1    Zhou, Y.2    Wang, C.3
  • 12
    • 0028131648 scopus 로고
    • Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds
    • Cai, H., Wang, C. C. & Tsou, C. L. (1994). Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds. J. Biol. Chem., 269, 24550-2.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24550-24552
    • Cai, H.1    Wang, C.C.2    Tsou, C.L.3
  • 13
    • 0030027968 scopus 로고    scopus 로고
    • Supervising the fold: functional principles of molecular chaperones
    • Buchner, J. (1996). Supervising the fold: functional principles of molecular chaperones. FASEB J, 10, 10-9.
    • (1996) FASEB J , vol.10 , pp. 10-19
    • Buchner, J.1
  • 14
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: from nascent chain to folded protein
    • Hartl, F. U. & Hayer-Hartl, M. (2002). Molecular chaperones in the cytosol: from nascent chain to folded protein. Science, 295, 1852-8.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 15
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai, B., Rodighiero, C., Lencer, W. I. & Rapoport, T. A. (2001). Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell, 104, 937-48.
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 16
    • 0037122001 scopus 로고    scopus 로고
    • Is protein disulfide isomerase a redox-dependent molecular chaperone?
    • Lumb, R. A. & Bulleid, N. J. (2002). Is protein disulfide isomerase a redox-dependent molecular chaperone?. EMBO J, 21, 6763-70.
    • (2002) EMBO J , vol.21 , pp. 6763-6770
    • Lumb, R.A.1    Bulleid, N.J.2
  • 17
    • 0022387362 scopus 로고
    • Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
    • Edman, J. C., Ellis, L., Blacher, R. W., Roth, R. A. & Rutter, W. J. (1985). Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature, 317, 267-70.
    • (1985) Nature , vol.317 , pp. 267-270
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3    Roth, R.A.4    Rutter, W.J.5
  • 18
    • 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, N. J., Dijkstra, K., Nilges, M. & Creighton, T. E. (1996). Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Biochemistry, 35, 7684-91.
    • (1996) Biochemistry , vol.35 , pp. 7684-7691
    • Kemmink, J.1    Darby, N.J.2    Dijkstra, K.3    Nilges, M.4    Creighton, T.E.5
  • 19
    • 0029146852 scopus 로고
    • Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site
    • Quan, H., Fan, G. & Wang, C. C. (1995). Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site. J. Biol. Chem., 270, 17078-80.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17078-17080
    • Quan, H.1    Fan, G.2    Wang, C.C.3
  • 20
    • 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., Lennarz, W. J. & Schindelin, H. (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    Lennarz, W.J.4    Schindelin, H.5
  • 22
    • 60349123960 scopus 로고    scopus 로고
    • Solution structure of the bb' domains of human protein disulfide isomerase
    • Denisov, A. Y., Maattanen, P., Dabrowski, C., Kozlov, G., Thomas, D. Y. & Gehring, K. (2009). Solution structure of the bb' domains of human protein disulfide isomerase. FEBS J, 276, 1440-9.
    • (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    Gehring, K.6
  • 23
    • 0033521682 scopus 로고    scopus 로고
    • The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide
    • Koivunen, P., Pirneskoski, A., Karvonen, P., Ljung, J., Helaakoski, T., Notbohm, H. & Kivirikko, K. I. (1999). The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide. EMBO J, 18, 65-74.
    • (1999) EMBO J , vol.18 , pp. 65-74
    • Koivunen, P.1    Pirneskoski, A.2    Karvonen, P.3    Ljung, J.4    Helaakoski, T.5    Notbohm, H.6    Kivirikko, K.I.7
  • 24
    • 0030836862 scopus 로고    scopus 로고
    • A mutant truncated protein disulfide isomerase with no chaperone activity
    • Dai, Y. & Wang, C. (1997). A mutant truncated protein disulfide isomerase with no chaperone activity. J. Biol. Chem., 272, 27572-6.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27572-27576
    • Dai, Y.1    Wang, C.2
  • 26
    • 0032512878 scopus 로고    scopus 로고
    • The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency
    • Darby, N. J., Penka, E. & Vincentelli, R. (1998). The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency. J. Mol. Biol., 276, 239-47.
    • (1998) J. Mol. Biol. , vol.276 , pp. 239-247
    • Darby, N.J.1    Penka, E.2    Vincentelli, R.3
  • 27
    • 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
    • Wang, L., Li, S. J., Sidhu, A., Zhu, L., Liang, Y., Freedman, R. B. & Wang, C. C. (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 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    Zhu, L.4    Liang, Y.5    Freedman, R.B.6    Wang, C.C.7
  • 28
    • 15744380512 scopus 로고    scopus 로고
    • A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain
    • Wilkinson, B., Xiao, R., Gilbert, H. F. (2005). A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain. J. Biol. Chem., 280, 11483-7.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11483-11487
    • Wilkinson, B.1    Xiao, R.2    Gilbert, H.F.3
  • 29
    • 0029093531 scopus 로고
    • Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase
    • Darby, N. J. & Creighton, T. E. (1995). Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase. Biochemistry, 34, 11725-35.
    • (1995) Biochemistry , vol.34 , pp. 11725-11735
    • Darby, N.J.1    Creighton, T.E.2
  • 30
    • 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, M. S., Frickel, E. M., Ellgaard, L. & Weissman, J. S. (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, 876-84.
    • (2006) J. Biol. Chem. , vol.281 , pp. 876-884
    • Kulp, M.S.1    Frickel, E.M.2    Ellgaard, L.3    Weissman, J.S.4
  • 31
    • 1242294484 scopus 로고    scopus 로고
    • A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein
    • Bass, R., Ruddock, L. W., Klappa, P. & Freedman, R. B. (2004). A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein. J. Biol. Chem., 279, 5257-62.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5257-5262
    • Bass, R.1    Ruddock, L.W.2    Klappa, P.3    Freedman, R.B.4
  • 32
    • 36148967364 scopus 로고    scopus 로고
    • In vivo reduction-oxidation state of protein disulfide isomerase: the two active sites independently occur in the reduced and oxidized forms
    • Appenzeller-Herzog, C. & Ellgaard, L. (2008). In vivo reduction-oxidation state of protein disulfide isomerase: the two active sites independently occur in the reduced and oxidized forms. Antioxid. Redox Signal, 10, 55-64.
    • (2008) Antioxid. Redox Signal , vol.10 , pp. 55-64
    • Appenzeller-Herzog, C.1    Ellgaard, L.2
  • 33
    • 9644279595 scopus 로고    scopus 로고
    • The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum
    • Xiao, R., Wilkinson, B., Solovyov, A., Winther, J. R., Holmgren, A., Lundstrom-Ljung, J. & Gilbert, H. F. (2004). The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum. J. Biol. Chem., 279, 49780-6.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49780-49786
    • Xiao, R.1    Wilkinson, B.2    Solovyov, A.3    Winther, J.R.4    Holmgren, A.5    Lundstrom-Ljung, J.6    Gilbert, H.F.7
  • 34
    • 0034919742 scopus 로고    scopus 로고
    • Disulfide bond formation in refolding of thermophilic fungal protein disulfide isomerase
    • Harada, T., Kurimoto, E., Tokuhiro, K., Asami, O., Sakai, T., Nohara, D. & Kato, K. (2001). Disulfide bond formation in refolding of thermophilic fungal protein disulfide isomerase. J. Biosci. Bioeng, 91, 596-8.
    • (2001) J. Biosci. Bioeng , vol.91 , pp. 596-598
    • Harada, T.1    Kurimoto, E.2    Tokuhiro, K.3    Asami, O.4    Sakai, T.5    Nohara, D.6    Kato, K.7
  • 36
    • 0028080915 scopus 로고
    • Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N-and C-terminal domains
    • Lyles, M. M. & Gilbert, H. F. (1994). Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N-and C-terminal domains. J. Biol. Chem., 269, 30946-52.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30946-30952
    • Lyles, M.M.1    Gilbert, H.F.2
  • 38
    • 0032481380 scopus 로고    scopus 로고
    • The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
    • Klappa, P., Ruddock, L. W., Darby, N. J. & Freedman, R. B. (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, 927-35.
    • (1998) EMBO J , vol.17 , pp. 927-935
    • Klappa, P.1    Ruddock, L.W.2    Darby, N.J.3    Freedman, R.B.4
  • 39
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • Raines, R. T. (1998). Ribonuclease A. Chem. Rev., 98, 1045-66.
    • (1998) Chem. Rev. , vol.98 , pp. 1045-1066
    • Raines, R.T.1
  • 41
    • 0030875033 scopus 로고    scopus 로고
    • Interactions between protein disulphide isomerase and peptides
    • Klappa, P., Hawkins, H. C. & Freedman, R. B. (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
  • 42
    • 78651030061 scopus 로고
    • Fluorescent indicators of adsorption in aqueous solution and on the solid phase
    • Weber, G. & Laurence, D. J. (1954). Fluorescent indicators of adsorption in aqueous solution and on the solid phase. Biochem J, 56, xxxi.
    • (1954) Biochem J , vol.56
    • Weber, G.1    Laurence, D.J.2
  • 43
    • 0031972919 scopus 로고    scopus 로고
    • 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation
    • Matulis, D. & Lovrien, R. (1998). 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys. J, 74, 422-9.
    • (1998) Biophys. J , vol.74 , pp. 422-429
    • Matulis, D.1    Lovrien, R.2
  • 45
    • 57749102824 scopus 로고    scopus 로고
    • The catalytic activity of protein-disulfide isomerase requires a conformationally flexible molecule
    • Tian, G., Kober, F. X., Lewandrowski, U., Sickmann, A., Lennarz, W. J. & Schindelin, H. (2008). The catalytic activity of protein-disulfide isomerase requires a conformationally flexible molecule. J. Biol. Chem., 283, 33630-40.
    • (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    Schindelin, H.6
  • 46
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun, D. I. (1999). Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J, 76, 2879-86.
    • (1999) Biophys. J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.