메뉴 건너뛰기




Volumn 44, Issue 7, 1996, Pages 751-759

Distinct distribution of protein disulfide isomerase family proteins in rat tissues

Author keywords

ERp61; ERp72; Immunofluorescence; Protein disulfide isomerase (PDI); Rat tissues; Tissue distribution

Indexed keywords

PROTEIN DISULFIDE ISOMERASE;

EID: 0029943402     PISSN: 00221554     EISSN: None     Source Type: Journal    
DOI: 10.1177/44.7.8675996     Document Type: Article
Times cited : (20)

References (55)
  • 1
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ, Sambrook J. Protein folding in the cell. Nature 1992;355:33
    • (1992) Nature , vol.355 , pp. 33
    • Gething, M.J.1    Sambrook, J.2
  • 2
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munto S, Pelham HR. A C-terminal signal prevents secretion of luminal ER proteins. Cell 1987;48:899
    • (1987) Cell , vol.48 , pp. 899
    • Munto, S.1    Pelham, H.R.2
  • 3
    • 0022387362 scopus 로고
    • Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
    • Edman JC, Ellis L, Blacher RW, Roth RA, Rutter WJ. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature 1985;317:267
    • (1985) Nature , vol.317 , pp. 267
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3    Roth, R.A.4    Rutter, W.J.5
  • 4
    • 73649177752 scopus 로고
    • Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver
    • Goldberger RF, Epstein CJ, Anfinsen CB. Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. J Biol Chem 1963;238:628
    • (1963) J Biol Chem , vol.238 , pp. 628
    • Goldberger, R.F.1    Epstein, C.J.2    Anfinsen, C.B.3
  • 5
    • 0023720121 scopus 로고
    • Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes
    • Bulleid NJ, Freedman RB. Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes. Nature 1988;335:649
    • (1988) Nature , vol.335 , pp. 649
    • Bulleid, N.J.1    Freedman, R.B.2
  • 6
    • 0027172321 scopus 로고
    • The bonds that tie: Catalyzed disulfide bond formation
    • Bardwell JC, Beckwith J. The bonds that tie: catalyzed disulfide bond formation. Cell 1993;74:769
    • (1993) Cell , vol.74 , pp. 769
    • Bardwell, J.C.1    Beckwith, J.2
  • 7
    • 0027203922 scopus 로고    scopus 로고
    • The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity
    • LaMantia ML, Lennarz WJ. The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell 1997; 74:899
    • (1997) Cell , vol.74 , pp. 899
    • LaMantia, M.L.1    Lennarz, W.J.2
  • 8
    • 0022547428 scopus 로고
    • Structure and assembly of the endoplasmic reticulum: Biosynthesis and intracellular sorting of ERp61, ERp59, and ERp49, three protein components of murine endoplasmic reticulum
    • Lewis MJ, Mazzarella RA, Green M. Structure and assembly of the endoplasmic reticulum: biosynthesis and intracellular sorting of ERp61, ERp59, and ERp49, three protein components of murine endoplasmic reticulum. Arch Biochem Biophys 1986;245-389
    • (1986) Arch Biochem Biophys , pp. 245-389
    • Lewis, M.J.1    Mazzarella, R.A.2    Green, M.3
  • 9
    • 0025830169 scopus 로고
    • Purification and characterization of a new isozyme of thiol:protein-disulfide oxidoreduchtase from rat hepatic microsomes. Relationship of this isozyme to cytosolic phosphatidylinositol-specific phospholipase C form 1A
    • Srivastava SP, Chen NQ, Liu YX, Holtzman JL. Purification and characterization of a new isozyme of thiol:protein-disulfide oxidoreduchtase from rat hepatic microsomes. Relationship of this isozyme to cytosolic phosphatidylinositol-specific phospholipase C form 1A. J Biol Chem 1991;266:20337
    • (1991) J Biol Chem , vol.266 , pp. 20337
    • Srivastava, S.P.1    Chen, N.Q.2    Liu, Y.X.3    Holtzman, J.L.4
  • 10
    • 0027281905 scopus 로고
    • The reported cDNA sequence for phospholipase C alpha encodes protein disulfide isomerase, isozyme Q-2 and not phospholipase-C
    • Srivastava SP, Fuchs JA, Holtzman JL. The reported cDNA sequence for phospholipase C alpha encodes protein disulfide isomerase, isozyme Q-2 and not phospholipase-C. Biochem Biophys Res Commun 1993;193:971
    • (1993) Biochem Biophys Res Commun , vol.193 , pp. 971
    • Srivastava, S.P.1    Fuchs, J.A.2    Holtzman, J.L.3
  • 11
    • 0026651766 scopus 로고
    • Protein degradation by the phosphoinositide-specific phospholipase C-alpha family from rat liver endoplasmic reticulum
    • Urade R, Nasu M, Moriyama T, Wada K, Kito M. Protein degradation by the phosphoinositide-specific phospholipase C-alpha family from rat liver endoplasmic reticulum. J Biol Chem 1992;267:15152
    • (1992) J Biol Chem , vol.267 , pp. 15152
    • Urade, R.1    Nasu, M.2    Moriyama, T.3    Wada, K.4    Kito, M.5
  • 13
    • 0023687758 scopus 로고
    • Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C
    • Bennett CF, Balcarek JM, Varrichio A, Crooke ST. Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C. Nature 1988;334:268
    • (1988) Nature , vol.334 , pp. 268
    • Bennett, C.F.1    Balcarek, J.M.2    Varrichio, A.3    Crooke, S.T.4
  • 14
    • 0021910786 scopus 로고
    • Structure and assembly of the endoplasmic reticulum. The synthesis of three major endoplasmic reticulum proteins during lipopolysaccharide-induced differentiation of murine lymphocytes
    • Lewis MJ, Mazzarella RA, Green M. Structure and assembly of the endoplasmic reticulum. The synthesis of three major endoplasmic reticulum proteins during lipopolysaccharide-induced differentiation of murine lymphocytes. J Biol Chem 1985;260:3050
    • (1985) J Biol Chem , vol.260 , pp. 3050
    • Lewis, M.J.1    Mazzarella, R.A.2    Green, M.3
  • 15
    • 0021821853 scopus 로고
    • Structure and assembly of the endoplasmic reticulum. Biosynthetic sorting of endoplasmic reticulum proteins
    • Lewis MJ, Turco SJ, Green M. Structure and assembly of the endoplasmic reticulum. Biosynthetic sorting of endoplasmic reticulum proteins. J Biol Chem 1985;260:6926
    • (1985) J Biol Chem , vol.260 , pp. 6926
    • Lewis, M.J.1    Turco, S.J.2    Green, M.3
  • 16
    • 0025070112 scopus 로고
    • ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase
    • Mazzarella RA, Srinivasan M, Haugejorden SM, Green M. ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. J Biol Chem 1990;265:1094
    • (1990) J Biol Chem , vol.265 , pp. 1094
    • Mazzarella, R.A.1    Srinivasan, M.2    Haugejorden, S.M.3    Green, M.4
  • 17
    • 0026533996 scopus 로고
    • The gene for a novel protein, a member of the protein disulphide isomerase/form I phosphoinositide-specific phospholipase C family, is amplified in hydroxyurea-resistant cells
    • Chaudhuri MM, Tonin PN, Lewis WH, Srinivasan PR. The gene for a novel protein, a member of the protein disulphide isomerase/form I phosphoinositide-specific phospholipase C family, is amplified in hydroxyurea-resistant cells. Biochem J 1992;281:645
    • (1992) Biochem J , vol.281 , pp. 645
    • Chaudhuri, M.M.1    Tonin, P.N.2    Lewis, W.H.3    Srinivasan, P.R.4
  • 18
    • 0027205018 scopus 로고
    • CaBP2 in a rat homolog of ERp72 with protein disulfide isomerase activity
    • Van PN, Rupp K, Lampen A, Soling HD. CaBP2 in a rat homolog of ERp72 with protein disulfide isomerase activity. Eut J Biochem 1993;213:789
    • (1993) Eut J Biochem , vol.213 , pp. 789
    • Van, P.N.1    Rupp, K.2    Lampen, A.3    Soling, H.D.4
  • 19
    • 0028070754 scopus 로고
    • Effects of CaBP2, the rat analog of ERp72, and of CaBP1 on the refolding of denatured reduced proteins. Comparison with protein disulfide isomerase
    • Rupp K, Birnbach U, Lundstrom J, Van PN, Soling HD. Effects of CaBP2, the rat analog of ERp72, and of CaBP1 on the refolding of denatured reduced proteins. Comparison with protein disulfide isomerase. J Biol Chem 1994;269:2501.
    • (1994) J Biol Chem , vol.269 , pp. 2501
    • Rupp, K.1    Birnbach, U.2    Lundstrom, J.3    Van, P.N.4    Soling, H.D.5
  • 21
    • 0023373787 scopus 로고
    • pH-dependcnt function, purification, and intracellular location of a major collagen-binding glycoprotein
    • Saga S, Nagata K, Chen WT, Yamada KM. pH-dependcnt function, purification, and intracellular location of a major collagen-binding glycoprotein. J Cell Biol 1987;105:517
    • (1987) J Cell Biol , vol.105 , pp. 517
    • Saga, S.1    Nagata, K.2    Chen, W.T.3    Yamada, K.M.4
  • 22
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrissey JH. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal Biochem 1981;117:307
    • (1981) Anal Biochem , vol.117 , pp. 307
    • Morrissey, J.H.1
  • 23
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren A. Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 1979;254:9627
    • (1979) J Biol Chem , vol.254 , pp. 9627
    • Holmgren, A.1
  • 24
    • 0023791651 scopus 로고
    • Enhanced fibronectin receptor expression in Rous sarcoma virus-induced tumors
    • Saga S, Chen WT, Yamada KM. Enhanced fibronectin receptor expression in Rous sarcoma virus-induced tumors. Cancer Res 1988;48:5510
    • (1988) Cancer Res , vol.48 , pp. 5510
    • Saga, S.1    Chen, W.T.2    Yamada, K.M.3
  • 25
    • 0026643696 scopus 로고
    • Distribution of the collagen binding heat-shock protein in chicken tissues
    • Miyaishi O, Sakata K, Matsuyama M, Saga S. Distribution of the collagen binding heat-shock protein in chicken tissues. J Histochern Cytochem 1992;40:1021
    • (1992) J Histochern Cytochem , vol.40 , pp. 1021
    • Miyaishi, O.1    Sakata, K.2    Matsuyama, M.3    Saga, S.4
  • 26
    • 0023083305 scopus 로고
    • Tissue distribution and molecular heterogeneity of bovine thiol:protein-disulphide oxidoreductase (disulphide interchange enzyme)
    • Bjelland S. Tissue distribution and molecular heterogeneity of bovine thiol:protein-disulphide oxidoreductase (disulphide interchange enzyme). Comp Biochem Physiol [B] 1987;87:907
    • (1987) Comp Biochem Physiol [B] , vol.87 , pp. 907
    • Bjelland, S.1
  • 27
    • 0019142467 scopus 로고
    • Protein disulphide-isomerase activity in chick-embryo tissues. Correlation with the biosynthesis of procollagen
    • Brockway BE, Forster SJ, Freedman RB. Protein disulphide-isomerase activity in chick-embryo tissues. Correlation with the biosynthesis of procollagen. Biochem J 1980;191:873
    • (1980) Biochem J , vol.191 , pp. 873
    • Brockway, B.E.1    Forster, S.J.2    Freedman, R.B.3
  • 28
    • 0024337857 scopus 로고
    • Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteins
    • Freedman RB. Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins. Cell 1989;57:1069
    • (1989) Cell , vol.57 , pp. 1069
    • Freedman, R.B.1
  • 29
    • 0026731788 scopus 로고
    • Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum
    • Noiva R, Lennarz WJ. Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum. J Biol Chem 1992;267:3553
    • (1992) J Biol Chem , vol.267 , pp. 3553
    • Noiva, R.1    Lennarz, W.J.2
  • 30
    • 0021939801 scopus 로고
    • Sequence of the 5′-end quarter of the humanthyroglobulin messenger ribonucleic acid and of its deduced aminoacid sequence
    • Malthiery Y, Lissitzky S. Sequence of the 5′-end quarter of the humanthyroglobulin messenger ribonucleic acid and of its deduced aminoacid sequence. Eur J Biochem 1985;147:53
    • (1985) Eur J Biochem , vol.147 , pp. 53
    • Malthiery, Y.1    Lissitzky, S.2
  • 31
    • 0023237474 scopus 로고
    • Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA
    • Malthiery Y, Lissitzky S. Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA. Eur J Biochem 1987;165:491
    • (1987) Eur J Biochem , vol.165 , pp. 491
    • Malthiery, Y.1    Lissitzky, S.2
  • 32
    • 0022355018 scopus 로고
    • Primary structure of bovine thyroglobulin deduced from the sequence of its 8,431-base complementary DNA
    • Mercken L, Simons MJ, Swillens S, Massaer M. Vassart G. Primary structure of bovine thyroglobulin deduced from the sequence of its 8,431-base complementary DNA. Nature 1985;316:647
    • (1985) Nature , vol.316 , pp. 647
    • Mercken, L.1    Simons, M.J.2    Swillens, S.3    Massaer, M.4    Vassart, G.5
  • 33
    • 0027032705 scopus 로고
    • Mucin genes and the proteins they encode: Structure, diversity, and regulation
    • Gum JJ. Mucin genes and the proteins they encode: structure, diversity, and regulation. Am J Respir Cell Mol Biol 1992;7:557
    • (1992) Am J Respir Cell Mol Biol , vol.7 , pp. 557
    • Gum, J.J.1
  • 34
    • 0023332890 scopus 로고
    • The primary structure of human secretogranin I (chromogranin B): Comparison with chromogranin A reveals homologous terminal domains and a large intervening variable region
    • Benedum UM, Lamouroux A, Konecki DS, Rosa P, Hille A, Baeuerle PA, Frank R. Lottspeich F, Mallet J, Huttner WB. The primary structure of human secretogranin I (chromogranin B): comparison with chromogranin A reveals homologous terminal domains and a large intervening variable region. EMBO J 1987;6:1203
    • (1987) EMBO J , vol.6 , pp. 1203
    • Benedum, U.M.1    Lamouroux, A.2    Konecki, D.S.3    Rosa, P.4    Hille, A.5    Baeuerle, P.A.6    Frank, R.7    Lottspeich, F.8    Mallet, J.9    Huttner, W.B.10
  • 35
    • 0023954680 scopus 로고
    • Molecular cloning and the nucleotide sequence of cDNA for embryonic chicken pepsinogen: Phylogenetic relationship with prochymosin
    • Tokyo
    • Hayashi K, Agata K, Mochii M, Yasugi S, Eguchi G, Mizuno T. Molecular cloning and the nucleotide sequence of cDNA for embryonic chicken pepsinogen: phylogenetic relationship with prochymosin. J Biochem (Tokyo) 1988;103:290
    • (1988) J Biochem , vol.103 , pp. 290
    • Hayashi, K.1    Agata, K.2    Mochii, M.3    Yasugi, S.4    Eguchi, G.5    Mizuno, T.6
  • 36
    • 0024494720 scopus 로고
    • Human pepsinogen C (progastricsin). Isolation of cDNA clones, localization to chromosome 6, and sequence homology with pepsinogen A
    • Taggert RT, Cass LG, Mohandas TK, Derby P, Barr PJ, Pals G, Bell GI. Human pepsinogen C (progastricsin). Isolation of cDNA clones, localization to chromosome 6, and sequence homology with pepsinogen A. J Biol Chem 1989;264:375
    • (1989) J Biol Chem , vol.264 , pp. 375
    • Taggert, R.T.1    Cass, L.G.2    Mohandas, T.K.3    Derby, P.4    Barr, P.J.5    Pals, G.6    Bell, G.I.7
  • 37
    • 0015851495 scopus 로고
    • Biosynthesis of immunoglobulin a (IgA) and immunoglobulin M (IgM); requirement for J chain and a disulphide-exchanging enzyme for polymerization
    • Della Corte E, Parkhouse RME. Biosynthesis of immunoglobulin A (IgA) and immunoglobulin M (IgM); requirement for J chain and a disulphide-exchanging enzyme for polymerization. Biochem J 1973; 136:597
    • (1973) Biochem J , vol.136 , pp. 597
    • Della Corte, E.1    Parkhouse, R.M.E.2
  • 38
    • 0019815999 scopus 로고
    • Role of disulfide interchange enzyme in immunoglobulin synthesis
    • Roth RA, Koshland ME. Role of disulfide interchange enzyme in immunoglobulin synthesis. Biochemistry 1981;20:6594
    • (1981) Biochemistry , vol.20 , pp. 6594
    • Roth, R.A.1    Koshland, M.E.2
  • 39
    • 0023653141 scopus 로고
    • In vivo cross-linking of protein disulfide isomerase to immunoglobulins
    • Roth RA, Pierce SB. In vivo cross-linking of protein disulfide isomerase to immunoglobulins. Biochemistry 1987;26:4179
    • (1987) Biochemistry , vol.26 , pp. 4179
    • Roth, R.A.1    Pierce, S.B.2
  • 40
    • 0024587333 scopus 로고
    • Induction of expression of protein disulphide-isomerase during lymphocyte maturation stimulated by bacterial lipopolysaccharide
    • Paver JL, Freedman RB, Parkhouse RM. Induction of expression of protein disulphide-isomerase during lymphocyte maturation stimulated by bacterial lipopolysaccharide. FEBS Lett 1989;242:357
    • (1989) FEBS Lett , vol.242 , pp. 357
    • Paver, J.L.1    Freedman, R.B.2    Parkhouse, R.M.3
  • 41
    • 0023303619 scopus 로고
    • Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
    • Pihlajaniemi T, Helaakoski T, Tisanen K, Myllyla R, Huhtala ML, Koivu J, Kivirikko KI. Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J 1987;6:643
    • (1987) EMBO J , vol.6 , pp. 643
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tisanen, K.3    Myllyla, R.4    Huhtala, M.L.5    Koivu, J.6    Kivirikko, K.I.7
  • 42
    • 0023865390 scopus 로고
    • Thyroid hormone down-regulates p55, a thyroid hormone-binding protein that is homologous to protein disulfide isomerase and the beta-subunit of prolyl-4-hydroxylase
    • Obata T, Kitagawa S, Gong QH, Pastan I, Cheng SY. Thyroid hormone down-regulates p55, a thyroid hormone-binding protein that is homologous to protein disulfide isomerase and the beta-subunit of prolyl-4-hydroxylase. J Biol Chem 1988;263:782
    • (1988) J Biol Chem , vol.263 , pp. 782
    • Obata, T.1    Kitagawa, S.2    Gong, Q.H.3    Pastan, I.4    Cheng, S.Y.5
  • 43
    • 0025329901 scopus 로고
    • Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex
    • Wetterau JR, Combs KA, Spinner SN, Joiner BJ. Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J Biol Chem 1990;265:9801.
    • (1990) J Biol Chem , vol.265 , pp. 9801
    • Wetterau, J.R.1    Combs, K.A.2    Spinner, S.N.3    Joiner, B.J.4
  • 44
    • 0025855390 scopus 로고
    • Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast
    • LaMantia M, Miura T, Tachikawa H, Kaplan HA, Lennarz WJ, Mizunaga T. Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast. Proc Natl Acad Sci USA 1991;88:4453
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4453
    • Lamantia, M.1    Miura, T.2    Tachikawa, H.3    Kaplan, H.A.4    Lennarz, W.J.5    Mizunaga, T.6
  • 45
    • 0027501384 scopus 로고
    • Protein degradation by ERp72 from rat and mouse liver endoplasmic reticulum
    • Urade R, Takenaka Y, Kito M. Protein degradation by ERp72 from rat and mouse liver endoplasmic reticulum. J Biol Chem 1993;268:22004
    • (1993) J Biol Chem , vol.268 , pp. 22004
    • Urade, R.1    Takenaka, Y.2    Kito, M.3
  • 46
    • 0027208576 scopus 로고
    • Carnitine medium/long chain acyltransferase of microsomes seems to be the previously cloned approximately 54 kDa ptotein of unknown function
    • Murthy MS, Pande SV. Carnitine medium/long chain acyltransferase of microsomes seems to be the previously cloned approximately 54 kDa ptotein of unknown function. Mol Cell Biochem 1993;122:133
    • (1993) Mol Cell Biochem , vol.122 , pp. 133
    • Murthy, M.S.1    Pande, S.V.2
  • 47
    • 0028114733 scopus 로고
    • A stress-regulated protein, GRP58, a member of thioredoxin superfamily, is a carnitine palmitoyltransferase isoenzyme
    • Murthy MS, Pande SV. A stress-regulated protein, GRP58, a member of thioredoxin superfamily, is a carnitine palmitoyltransferase isoenzyme. Biochem J 1994;304:31
    • (1994) Biochem J , vol.304 , pp. 31
    • Murthy, M.S.1    Pande, S.V.2
  • 48
    • 0026066361 scopus 로고
    • Peptide binding by protein disulfide isomerase, a resident protein of the endoplasmic reticulum lumen
    • Noiva R, Kimura H, Roos J, Lennarz WJ. Peptide binding by protein disulfide isomerase, a resident protein of the endoplasmic reticulum lumen. J Biol Chem 1991;266:19645
    • (1991) J Biol Chem , vol.266 , pp. 19645
    • Noiva, R.1    Kimura, H.2    Roos, J.3    Lennarz, W.J.4
  • 49
    • 0027220866 scopus 로고
    • Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites
    • Noiva R, Freedman RB, Lennarz WJ. Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites. J Biol Chem 1993;268:19210
    • (1993) J Biol Chem , vol.268 , pp. 19210
    • Noiva, R.1    Freedman, R.B.2    Lennarz, W.J.3
  • 50
    • 0028334004 scopus 로고
    • Protein disulfide isomerase associates with misfolded human lysozyme in vivo
    • Otsu M, Omura F, Yoshimori T, Kikuchi M. Protein disulfide isomerase associates with misfolded human lysozyme in vivo. J Biol Chem 1994;269:6874
    • (1994) J Biol Chem , vol.269 , pp. 6874
    • Otsu, M.1    Omura, F.2    Yoshimori, T.3    Kikuchi, M.4
  • 51
    • 0028321726 scopus 로고
    • Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme
    • Puig A, Gilbert HF. Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J Biol Chem 1994;269:7764
    • (1994) J Biol Chem , vol.269 , pp. 7764
    • Puig, A.1    Gilbert, H.F.2
  • 52
    • 0025630758 scopus 로고
    • The stress response in Chinese hamster ovary cells. Regulation of ERp72 and protein disulfide isomerase expression and secretion
    • Dorner AJ, Wasley LC, Raney P, Haugejorden S. Green M, Kaufman RJ. The stress response in Chinese hamster ovary cells. Regulation of ERp72 and protein disulfide isomerase expression and secretion. J Biol Chem 1990;265:22029
    • (1990) J Biol Chem , vol.265 , pp. 22029
    • Dorner, A.J.1    Wasley, L.C.2    Raney, P.3    Haugejorden, S.4    Green, M.5    Kaufman, R.J.6
  • 53
    • 0026742999 scopus 로고
    • HLADR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells
    • Schaiff WT, Krusha KJ, McCourt DW, Green M, Schwartz BD. HLADR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells. J Exp Med 1992;176:657
    • (1992) J Exp Med , vol.176 , pp. 657
    • Schaiff, W.T.1    Krusha, K.J.2    McCourt, D.W.3    Green, M.4    Schwartz, B.D.5
  • 55
    • 0027514241 scopus 로고
    • Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian ptotein disulfide isomerase family
    • Gunther R, Srinivasan M, Haugejorden S, Green M, Ehbrecht IM, Kuntzel H. Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian ptotein disulfide isomerase family. J Biol Chem 1993;268:7728
    • (1993) J Biol Chem , vol.268 , pp. 7728
    • Gunther, R.1    Srinivasan, M.2    Haugejorden, S.3    Green, M.4    Ehbrecht, I.M.5    Kuntzel, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.