메뉴 건너뛰기




Volumn 256, Issue 1, 1998, Pages 51-59

The transient association of ERp57 with N-glycosylated proteins is regulated by glucose trimming

Author keywords

Endoplasmic reticulum; ERp57 GRP58; Molecular chaperone; N linked glycosylation; Protein disulphide isomerase

Indexed keywords

CHAPERONE; GLUCOSE; ISOMERASE; PROTEIN DISULFIDE ISOMERASE;

EID: 0032529113     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2560051.x     Document Type: Article
Times cited : (35)

References (48)
  • 1
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M. J. & Sambrook, J. (1992) Protein folding in the cell, Nature 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 3
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert, D. N., Foellmer, B. & Helenius, A. (1995) Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum, Cell 81, 425-433.
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 4
    • 0029160540 scopus 로고
    • Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins
    • Peterson, J. R., Ora, A., Van, P. N. & Helenius, A. (1995) Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins, Mol. Biol. Cell 6, 1173-1184.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Van, P.N.3    Helenius, A.4
  • 5
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R. & Kornfeld, S. (1985) Assembly of asparagine-linked oligosaccharides, Annu. Rev. Biochem. 54, 631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 6
    • 0026799435 scopus 로고
    • Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:Glycoprotein glucosyltransferase
    • Trombetta, S. H. & Parodi, A. J. (1992) Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:glycoprotein glucosyltransferase, J. Biol. Chem. 267, 9236-9240.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9236-9240
    • Trombetta, S.H.1    Parodi, A.J.2
  • 7
    • 0029126624 scopus 로고
    • The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
    • Sousa, M. & Parodi, A. J. (1995) The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase, EMBO J. 14, 4196-4203.
    • (1995) EMBO J. , vol.14 , pp. 4196-4203
    • Sousa, M.1    Parodi, A.J.2
  • 8
    • 0030449989 scopus 로고    scopus 로고
    • N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin
    • Rodan, A. R., Simons, J. F., Trombetta, H. S. & Helenius, A. (1996) N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin, EMBO J. 15, 6921-6930.
    • (1996) EMBO J. , vol.15 , pp. 6921-6930
    • Rodan, A.R.1    Simons, J.F.2    Trombetta, H.S.3    Helenius, A.4
  • 9
    • 0030694617 scopus 로고    scopus 로고
    • Calnexin and calreticulin bind to enzymically active tissue-type plasminogen activator during biosynthesis and are not required for folding to the native conformation
    • Allen, S. & Bulleid, N. J. (1997) Calnexin and calreticulin bind to enzymically active tissue-type plasminogen activator during biosynthesis and are not required for folding to the native conformation, Biochem. J. 328, 113-119.
    • (1997) Biochem. J. , vol.328 , pp. 113-119
    • Allen, S.1    Bulleid, N.J.2
  • 10
    • 0030933129 scopus 로고    scopus 로고
    • Conformation-independent binding of monoglucosylated ribonuclease B to calnexin
    • Zapun, A., Petrescu, S. M., Rudd, P. M., Dwek, R. A., Thomas, D. Y. & Bergeron, J. J. M. (1997) Conformation-independent binding of monoglucosylated ribonuclease B to calnexin, Cell 88, 29-38.
    • (1997) Cell , vol.88 , pp. 29-38
    • Zapun, A.1    Petrescu, S.M.2    Rudd, P.M.3    Dwek, R.A.4    Thomas, D.Y.5    Bergeron, J.J.M.6
  • 12
    • 0027959156 scopus 로고
    • Protein disulfide isomerase: Building bridges in protein folding
    • Freedman, R. B., Hirst, T. R. & Tuite, M. F. (1994) Protein disulfide 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
  • 13
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver, J. D., Van der Wal, F. J., Bulleid, N. J. & High, S. (1997) Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins, Science 275, 86-88.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    Van Der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 14
    • 0030960372 scopus 로고    scopus 로고
    • The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins
    • Elliott, J. G., Oliver, J. D. & High, S. (1997) The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins, J. Biol. Chem. 272, 13849-13855.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13849-13855
    • Elliott, J.G.1    Oliver, J.D.2    High, S.3
  • 15
    • 0031062459 scopus 로고    scopus 로고
    • The roles of the thiol:protein disulfide oxidoreductases in membrane and secretory protein synthesis within the lumen of the endoplasmic reticulum
    • Holtzman, J. L. (1997) The roles of the thiol:protein disulfide oxidoreductases in membrane and secretory protein synthesis within the lumen of the endoplasmic reticulum, J. Invest. Med. 45, 28-34.
    • (1997) J. Invest. Med. , vol.45 , pp. 28-34
    • Holtzman, J.L.1
  • 16
    • 0032513212 scopus 로고    scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
    • Zapun, A., Darby, N. J., Tessier, D. C., Michalak, M., Bergeron, J. J. M. & Thomas, D. Y. (1998) Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57, J. Biol. Chem. 273, 6009-6012.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6009-6012
    • Zapun, A.1    Darby, N.J.2    Tessier, D.C.3    Michalak, M.4    Bergeron, J.J.M.5    Thomas, D.Y.6
  • 17
    • 0021767942 scopus 로고
    • A novel in vitro transcription-translation system: Accurate and efficient synthesis of single proteins from cloned DNA sequences
    • Steuber, D., Ibrahimi, I., Cutler, D., Dobberstein, B. & Bujard, H. (1984) A novel in vitro transcription-translation system: accurate and efficient synthesis of single proteins from cloned DNA sequences, EMBO J. 3, 3143-3148.
    • (1984) EMBO J. , vol.3 , pp. 3143-3148
    • Steuber, D.1    Ibrahimi, I.2    Cutler, D.3    Dobberstein, B.4    Bujard, H.5
  • 18
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Walter, P. & Blobel, G. (1983) Preparation of microsomal membranes for cotranslational protein translocation, Methods Enzymol. 96, 84-93.
    • (1983) Methods Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 19
    • 0021010426 scopus 로고
    • Signal recognition particle - A ribonucleoprotein required for cotranslational translocation of proteins, isolation and properties
    • Walter, P. & Blobel, G. (1983) Signal recognition particle - a ribonucleoprotein required for cotranslational translocation of proteins, isolation and properties, Methods Enzymol. 96, 682-691.
    • (1983) Methods Enzymol. , vol.96 , pp. 682-691
    • Walter, P.1    Blobel, G.2
  • 20
    • 0026317971 scopus 로고
    • A novel glycosylation phenotype expressed by Lec23, a Chinese hamster ovary mutant deficient in α-glucosidase I
    • Ray, M. K., Yang, J., Sundaram, S. & Stanley, P. (1991) A novel glycosylation phenotype expressed by Lec23, a Chinese hamster ovary mutant deficient in α-glucosidase I, J. Biol. Chem. 266, 22818-22825.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22818-22825
    • Ray, M.K.1    Yang, J.2    Sundaram, S.3    Stanley, P.4
  • 21
    • 0029024163 scopus 로고
    • The translocation, folding, assembly and redox-dependent degradation of secretory and membrane proteins in semi-permeabilized mammalian cells
    • Wilson, R., Allen, A. J., Oliver, J., Brookman, J. L., High, S. & Bulleid, N. J. (1995) The translocation, folding, assembly and redox-dependent degradation of secretory and membrane proteins in semi-permeabilized mammalian cells, Biochem. J. 307, 679-687.
    • (1995) Biochem. J. , vol.307 , pp. 679-687
    • Wilson, R.1    Allen, A.J.2    Oliver, J.3    Brookman, J.L.4    High, S.5    Bulleid, N.J.6
  • 22
    • 0029941071 scopus 로고    scopus 로고
    • The glut 1 glucose transporter interacts with calnexin and calreticulin
    • Oliver, J. D., Hresko, R. C., Mueckler, M. & High, S. (1996) The glut 1 glucose transporter interacts with calnexin and calreticulin, J. Biol. Chem. 271, 13691-13696.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13691-13696
    • Oliver, J.D.1    Hresko, R.C.2    Mueckler, M.3    High, S.4
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0026439921 scopus 로고
    • Morphological analysis of protein transport from the ER to Golgi membranes in digitonin-permeabilized cells: Role of the P5H containing compartment
    • Plutner, H., Davidson, H. W., Saraste, J. & Balch, W. E. (1992) Morphological analysis of protein transport from the ER to Golgi membranes in digitonin-permeabilized cells: role of the P5H containing compartment, J. Cell Biol. 119, 1097-1116.
    • (1992) J. Cell Biol. , vol.119 , pp. 1097-1116
    • Plutner, H.1    Davidson, H.W.2    Saraste, J.3    Balch, W.E.4
  • 25
    • 0028883409 scopus 로고
    • Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines
    • Ora, A. & Helenius, A. (1995) Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines, J. Biol. Chem. 270, 26060-26062.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26060-26062
    • Ora, A.1    Helenius, A.2
  • 26
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou, W. J., Cameron, P. H., Thomas, D. Y. & Bergeron, J. J. (1993) Association of folding intermediates of glycoproteins with calnexin during protein maturation, Nature 364, 771-776.
    • (1993) Nature , vol.364 , pp. 771-776
    • Ou, W.J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.4
  • 27
    • 0022110644 scopus 로고
    • Signal recognition particle (SRP) does not mediate a translational arrest of nascent secretory proteins in mammalian cell-free systems
    • Meyer, D. I. (1985) Signal recognition particle (SRP) does not mediate a translational arrest of nascent secretory proteins in mammalian cell-free systems, EMBO J. 4, 2031-2033.
    • (1985) EMBO J. , vol.4 , pp. 2031-2033
    • Meyer, D.I.1
  • 28
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert, D. N., Foellmer, B. & Helenius, A. (1996) Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes, EMBO J. 15, 2961-2968.
    • (1996) EMBO J. , vol.15 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 29
    • 0018222064 scopus 로고
    • Enhancement of the synthesis of specific cellular polypeptides in a temperature-sensitive Chinese hamster cell line (K12) defective for entry into S phase
    • Melero, J. A. & Fincham, V. (1978) Enhancement of the synthesis of specific cellular polypeptides in a temperature-sensitive Chinese hamster cell line (K12) defective for entry into S phase, J. Cell Physiol. 95, 295-306.
    • (1978) J. Cell Physiol. , vol.95 , pp. 295-306
    • Melero, J.A.1    Fincham, V.2
  • 30
    • 0019833479 scopus 로고
    • The accumulation of three specific proteins related to glucose-regulated proteins in a temperature-sensitive hamster mutant cell line K12
    • Lee, A. S. (1981) The accumulation of three specific proteins related to glucose-regulated proteins in a temperature-sensitive hamster mutant cell line K12, J. Cell Physiol. 106, 119-125.
    • (1981) J. Cell Physiol. , vol.106 , pp. 119-125
    • Lee, A.S.1
  • 31
    • 0023133224 scopus 로고
    • Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells
    • Lee, A. S. (1987) Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells, Trends Biochem. Sci. 12, 20-23.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 20-23
    • Lee, A.S.1
  • 32
    • 0022547428 scopus 로고
    • Structure and assembly of the endoplasmic reticulum: Biosynthesis and intracellular sorting of ERp61, ERp59, and RRp49, three protein components of murine endoplasmic reticulum
    • Lewis, M. J., Mazzarella, R. A. & Green, M. (1986) Structure and assembly of the endoplasmic reticulum: biosynthesis and intracellular sorting of ERp61, ERp59, and RRp49, three protein components of murine endoplasmic reticulum, Arch. Biochem. Biophys. 245, 389-403.
    • (1986) Arch. Biochem. Biophys. , vol.245 , pp. 389-403
    • Lewis, M.J.1    Mazzarella, R.A.2    Green, M.3
  • 33
    • 0028223563 scopus 로고
    • Erp61 is GRP58, a stress-inducible luminal endoplasmic reticulum protein, hut is devoid of phosphatidylinositide-specific phospholipase C activity
    • Mazzarella, R. A., Marcus, N., Haugejorden, S. M., Balcarek, J. M., Baldassare, J. J., Roy, B., Li, L. J., Lee, A. S. & Green, M. (1994) Erp61 is GRP58, a stress-inducible luminal endoplasmic reticulum protein, hut is devoid of phosphatidylinositide-specific phospholipase C activity, Arch. Biochem. Biophys. 308, 454-460.
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 454-460
    • Mazzarella, R.A.1    Marcus, N.2    Haugejorden, S.M.3    Balcarek, J.M.4    Baldassare, J.J.5    Roy, B.6    Li, L.J.7    Lee, A.S.8    Green, M.9
  • 34
    • 0025233474 scopus 로고
    • HIP-70: A protein induced by estrogen in the brain and LH-RH in the pituitary
    • Mobbs, C. V., Fink, G. & Pfaff, D. W. (1990) HIP-70: a protein induced by estrogen in the brain and LH-RH in the pituitary, Science 247, 1477-1479.
    • (1990) Science , vol.247 , pp. 1477-1479
    • Mobbs, C.V.1    Fink, G.2    Pfaff, D.W.3
  • 35
    • 0025830169 scopus 로고
    • Purification and characterization of a new isozyme of thiol:protein-disulfide oxidoreductase from rat hepatic microsomes. Relationship of this isozyme to cytosolic phosphatidylinositol-specific phospholipase C form 1A
    • Srivastava, S. P., Chen, N. Q., Liu, Y. X. & Holtzman, J. L. (1991) Purification and characterization of a new isozyme of thiol:protein-disulfide oxidoreductase from rat hepatic microsomes. Relationship of this isozyme to cytosolic phosphatidylinositol-specific phospholipase C form 1A, J. Biol. Chem. 266, 20337-20344.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20337-20344
    • Srivastava, S.P.1    Chen, N.Q.2    Liu, Y.X.3    Holtzman, J.L.4
  • 36
    • 0026651766 scopus 로고
    • Protein degradation by the phosphoinositide-specific phospholipase Cα family from rat liver endoplasmic reticulum
    • Urade, R., Nasu, M., Moriyama, T., Wada, K. & Kito, M. (1992) Protein degradation by the phosphoinositide-specific phospholipase Cα family from rat liver endoplasmic reticulum, J. Biol. Chem. 267, 15152-15159.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15152-15159
    • Urade, R.1    Nasu, M.2    Moriyama, T.3    Wada, K.4    Kito, M.5
  • 38
    • 0028786868 scopus 로고
    • cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: Characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferase
    • Bourdi, M., Demady, D., Martin, J. L., Jabbour, S. K., Martin, B. M., George, J. W. & Pohl, L. R. (1995) cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferase, Arch. Biochem. Biophys. 323, 397-403.
    • (1995) Arch. Biochem. Biophys. , vol.323 , pp. 397-403
    • Bourdi, M.1    Demady, D.2    Martin, J.L.3    Jabbour, S.K.4    Martin, B.M.5    George, J.W.6    Pohl, L.R.7
  • 39
    • 0023687758 scopus 로고
    • Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C
    • Bennett, C. F., Balcarek, J. M., Varrichio, A. & Crooke, S. T. (1988) Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C, Nature 334, 268-270.
    • (1988) Nature , vol.334 , pp. 268-270
    • Bennett, C.F.1    Balcarek, J.M.2    Varrichio, A.3    Crooke, S.T.4
  • 40
    • 0027281905 scopus 로고
    • The reported cDNA sequence for phospholipase Ca encodes protein disulfide isomerase, isozyme Q-2 and not phospholipase-C
    • Srivastava, S. P., Fuchs, J. A. & Holtzman, J. L. (1993) The reported cDNA sequence for phospholipase Ca encodes protein disulfide isomerase, isozyme Q-2 and not phospholipase-C, Biochem. Biophys. Res. Commun. 193, 971-978.
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 971-978
    • Srivastava, S.P.1    Fuchs, J.A.2    Holtzman, J.L.3
  • 41
    • 0028114733 scopus 로고
    • A stress-regulated protein, GRP58, a member of thioredoxin superfamily, is a carnitine palmitoyltransferase isoenzyme
    • Murthy, M. S. & Pande, S. V. (1994) A stress-regulated protein, GRP58, a member of thioredoxin superfamily, is a carnitine palmitoyltransferase isoenzyme, Biochem. J. 304, 31-34.
    • (1994) Biochem. J. , vol.304 , pp. 31-34
    • Murthy, M.S.1    Pande, S.V.2
  • 42
    • 0028823248 scopus 로고
    • Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase: Identification of its secretory form and inducible expression by the oncogenic transformation
    • Hirano, N., Shibasaki, F, Sakai, R., Tanaka, T., Nishida, J., Yazaki, Y., Takenawa, T. & Hirai, H. (1995) Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase: identification of its secretory form and inducible expression by the oncogenic transformation, Eur. J. Biochem. 234, 336-342.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 336-342
    • Hirano, N.1    Shibasaki, F.2    Sakai, R.3    Tanaka, T.4    Nishida, J.5    Yazaki, Y.6    Takenawa, T.7    Hirai, H.8
  • 43
    • 15844379984 scopus 로고    scopus 로고
    • Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin
    • Cannon, K. S., Hebert, D. N. & Helenius, A. (1996) Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin, J. Biol. Chem. 271, 14280-14284.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14280-14284
    • Cannon, K.S.1    Hebert, D.N.2    Helenius, A.3
  • 44
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius, A. (1994) How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum, Mol. Biol. Cell 5, 253-265.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 45
    • 0029085091 scopus 로고
    • Protein disulphide isomerase and a lumenal cyclophilin-type peptidyl prolyl cis-trans isomerase are in transient contact with secretory proteins during late stages of translocation
    • Klappa, P., Freedman, R. B. & Zimmermann, R. (1995) Protein disulphide isomerase and a lumenal cyclophilin-type peptidyl prolyl cis-trans isomerase are in transient contact with secretory proteins during late stages of translocation, Eur. J. Biochem. 232, 755-764.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 755-764
    • Klappa, P.1    Freedman, R.B.2    Zimmermann, R.3
  • 46
    • 0027203922 scopus 로고
    • The essential function of yeast protein disulfide-isomerase does not reside in its isomerase activity
    • LaMantia, M. L. & Lennarz, W. J. (1993) The essential function of yeast protein disulfide-isomerase does not reside in its isomerase activity, Cell 74, 899-908.
    • (1993) Cell , vol.74 , pp. 899-908
    • LaMantia, M.L.1    Lennarz, W.J.2
  • 47
    • 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, 7764-7771.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7764-7771
    • Puig, A.1    Gilbert, H.F.2
  • 48
    • 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 A(2)
    • Yao, Y., Zhou, Y. C. & Wang, C. C. (1997) Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A(2), EMBO J. 16, 651-658.
    • (1997) EMBO J. , vol.16 , pp. 651-658
    • Yao, Y.1    Zhou, Y.C.2    Wang, C.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.