메뉴 건너뛰기




Volumn 49, Issue 324, 1998, Pages 1091-1103

Effects of N-glycosylation on the folding and structure of plant proteins

Author keywords

Calnexin; Calreticulin; Endoplasmic reticulum; Glucose trimming; Glycoprotein stability

Indexed keywords


EID: 0031867912     PISSN: 00220957     EISSN: None     Source Type: Journal    
DOI: 10.1093/jxb/49.324.1091     Document Type: Article
Times cited : (51)

References (112)
  • 1
    • 0028946717 scopus 로고
    • Intracellular folding of tissue-type plasminogen activator. Effects of disulphide bond formation on N-linked glycosylation and secretion
    • Allen S, Naim HY, Bulleid NJ. 1995. Intracellular folding of tissue-type plasminogen activator. Effects of disulphide bond formation on N-linked glycosylation and secretion. Journal of Biological Chemistry 270, 4797-804.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 4797-4804
    • Allen, S.1    Naim, H.Y.2    Bulleid, N.J.3
  • 3
    • 0021234236 scopus 로고
    • Co-translational excision of α-glucose and α-mannose in nascent vesicular stomatitis virus G protein
    • Atkinson PH, Lee, JT. 1984. Co-translational excision of α-glucose and α-mannose in nascent vesicular stomatitis virus G protein. Journal of Cell Biology 98, 2245-9.
    • (1984) Journal of Cell Biology , vol.98 , pp. 2245-2249
    • Atkinson, P.H.1    Lee, J.T.2
  • 4
    • 2642612976 scopus 로고
    • The role of glycosylation in storage-protein synthesis in developing pea seeds
    • Badenoch-Jones J, Spencer D, Higgins TJV, Millerd A. 1981. The role of glycosylation in storage-protein synthesis in developing pea seeds. Planta 153, 201-9.
    • (1981) Planta , vol.153 , pp. 201-209
    • Badenoch-Jones, J.1    Spencer, D.2    Higgins, T.J.V.3    Millerd, A.4
  • 5
    • 0028810104 scopus 로고
    • Unique expression of major histocompatibility complex class I proteins in the absence of glucose trimming and calnexin association
    • Balow JP, Weissman JD, Kearse KP. 1995. Unique expression of major histocompatibility complex class I proteins in the absence of glucose trimming and calnexin association. Journal of Biological Chemistry 270, 29025-9.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 29025-29029
    • Balow, J.P.1    Weissman, J.D.2    Kearse, K.P.3
  • 7
    • 0002913516 scopus 로고
    • Glycosylation is not needed for the intracellular transport of phytohemagglutinin in developing Phaseolus vulgaris cotyledons and for the maintenance of its biological activities
    • Bollini R, Ceriotti A, Daminati MG, Vitale A. 1985. Glycosylation is not needed for the intracellular transport of phytohemagglutinin in developing Phaseolus vulgaris cotyledons and for the maintenance of its biological activities. Physiologia Plantarum 65, 15-22.
    • (1985) Physiologia Plantarum , vol.65 , pp. 15-22
    • Bollini, R.1    Ceriotti, A.2    Daminati, M.G.3    Vitale, A.4
  • 8
    • 0008881217 scopus 로고    scopus 로고
    • Coordinate induction of three ER-lumenal stress proteins in maize endosperm mutants
    • Boston RS, Gillikin JW, Wrobel RL. 1996. Coordinate induction of three ER-lumenal stress proteins in maize endosperm mutants. Journal of Cellular Biochemistry 19A, 143.
    • (1996) Journal of Cellular Biochemistry , vol.19 A , pp. 143
    • Boston, R.S.1    Gillikin, J.W.2    Wrobel, R.L.3
  • 10
  • 11
    • 0020993866 scopus 로고
    • Ricin and Ricinus communis agglutinin subunits are all derived from a single-size polypeptide precursor
    • Butterworth AG, Lord JM. 1983. Ricin and Ricinus communis agglutinin subunits are all derived from a single-size polypeptide precursor. European Journal of Biochemistry 1983, 57-65.
    • (1983) European Journal of Biochemistry , vol.1983 , pp. 57-65
    • Butterworth, A.G.1    Lord, J.M.2
  • 12
    • 0029986845 scopus 로고    scopus 로고
    • IgM polymerization inhibits the Golgi-mediated processing of the μ-chain carboxy-terminal glycans
    • Cals M-M, Guenzi S, Carelli S, Simmen T, Sparvoli A, Sitia R. 1996. IgM polymerization inhibits the Golgi-mediated processing of the μ-chain carboxy-terminal glycans. Molecular Immunology 33, 15-24.
    • (1996) Molecular Immunology , vol.33 , pp. 15-24
    • Cals, M.-M.1    Guenzi, S.2    Carelli, S.3    Simmen, T.4    Sparvoli, A.5    Sitia, R.6
  • 13
    • 0028450064 scopus 로고
    • Identification and characterization of cDNA clones encoding plant calreticulin
    • Chen F, Hayes PM, Mulrooney DM, Pan A. 1994. Identification and characterization of cDNA clones encoding plant calreticulin. The Plant Cell 6, 835-43.
    • (1994) The Plant Cell , vol.6 , pp. 835-843
    • Chen, F.1    Hayes, P.M.2    Mulrooney, D.M.3    Pan, A.4
  • 14
    • 0000305251 scopus 로고
    • Tunicamycin-inhibited carrot somatic embryogenesis can be restored by secreted cationic peroxidase isoenzymes
    • Cordewener J, Booij H, van der Zandt H, van Engelen F, van Kammen A, de Vries S. 1991. Tunicamycin-inhibited carrot somatic embryogenesis can be restored by secreted cationic peroxidase isoenzymes. Planta 184, 478-86.
    • (1991) Planta , vol.184 , pp. 478-486
    • Cordewener, J.1    Booij, H.2    Van der Zandt, H.3    Van Engelen, F.4    Van Kammen, A.5    De Vries, S.6
  • 15
    • 0031214672 scopus 로고    scopus 로고
    • Cloning and characterization of the calreticulin gene from Ricinus communis L
    • Coughlan SJ, Hastings C, Winfrey Jr R. 1997. Cloning and characterization of the calreticulin gene from Ricinus communis L. Plant Molecular Biology 34, 897-911.
    • (1997) Plant Molecular Biology , vol.34 , pp. 897-911
    • Coughlan, S.J.1    Hastings, C.2    Winfrey Jr., R.3
  • 16
    • 0026893762 scopus 로고
    • Bean homologues of the mammalian glucose-regulated proteins: Induction by tunicamycin and interaction with newly-synthesized seed storage proteins in the endoplasmic reticulum
    • D'Amico L, Valsasina B, Daminati MG, Fabbrini MS, Nitti G, Bollini R, Ceriotti A, Vitale A. 1992. Bean homologues of the mammalian glucose-regulated proteins: induction by tunicamycin and interaction with newly-synthesized seed storage proteins in the endoplasmic reticulum. The Plant Journal 2, 443-55.
    • (1992) The Plant Journal , vol.2 , pp. 443-455
    • D'Amico, L.1    Valsasina, B.2    Daminati, M.G.3    Fabbrini, M.S.4    Nitti, G.5    Bollini, R.6    Ceriotti, A.7    Vitale, A.8
  • 20
    • 0030130430 scopus 로고    scopus 로고
    • Isolation of a full-length cDNA encoding calreticulin from a PCR library of in vitro zygotes of maize
    • Dresselhaus T, Hagel C, Lorz H, Kranz E. 1996. Isolation of a full-length cDNA encoding calreticulin from a PCR library of in vitro zygotes of maize. Plant Molecular Biology 31, 23-24.
    • (1996) Plant Molecular Biology , vol.31 , pp. 23-24
    • Dresselhaus, T.1    Hagel, C.2    Lorz, H.3    Kranz, E.4
  • 21
    • 0001866453 scopus 로고
    • The role of high mannose and complex asparagine-linked glycans in the secretion and stability of glycoproteins
    • Driouich A, Gonnet P, Makkie M, Laine A-C, Faye L. 1989. The role of high mannose and complex asparagine-linked glycans in the secretion and stability of glycoproteins. Planta 180, 96-104.
    • (1989) Planta , vol.180 , pp. 96-104
    • Driouich, A.1    Gonnet, P.2    Makkie, M.3    Laine, A.-C.4    Faye, L.5
  • 22
    • 0029005022 scopus 로고
    • The saccharide chain of lupin seed conglutin γ is not responsible for the protection of the native protein from degradation by trypsin, but facilitates the refolding of the acid-treated protein to the resistant conformation
    • Duranti M, Gius C, Sessa F, Vecchio G. 1995. The saccharide chain of lupin seed conglutin γ is not responsible for the protection of the native protein from degradation by trypsin, but facilitates the refolding of the acid-treated protein to the resistant conformation. European Journal of Biochemistry 230, 886-91.
    • (1995) European Journal of Biochemistry , vol.230 , pp. 886-891
    • Duranti, M.1    Gius, C.2    Sessa, F.3    Vecchio, G.4
  • 23
    • 0028232944 scopus 로고
    • Heat-induced synthesis and tunicamycin-sensitive secretion of the putative storage glycoprotein conglutin γ from mature lupin seeds
    • Duranti M, Scarafoni A, Gius C, Negri A, Faoro F. 1994. Heat-induced synthesis and tunicamycin-sensitive secretion of the putative storage glycoprotein conglutin γ from mature lupin seeds. European Journal of Biochemistry 222, 387-93.
    • (1994) European Journal of Biochemistry , vol.222 , pp. 387-393
    • Duranti, M.1    Scarafoni, A.2    Gius, C.3    Negri, A.4    Faoro, F.5
  • 24
    • 0026244932 scopus 로고
    • The role of N-linked oligosaccharides in glycoprotein function
    • Elbein AD. 1991. The role of N-linked oligosaccharides in glycoprotein function. Trends in Biotechnology 9, 346-52.
    • (1991) Trends in Biotechnology , vol.9 , pp. 346-352
    • Elbein, A.D.1
  • 25
    • 85038532445 scopus 로고    scopus 로고
    • Identification of newly-synthesized precursors of lectin-related proteins in the endoplasmic reticulum of developing lima bean seeds
    • Carnovale E, ed. COST Action 98, 6th Workshop, Rome, Italy: European Commission (in press)
    • Faoro F, Sparvoli F, Ceriotti A, Bollini R. 1997. Identification of newly-synthesized precursors of lectin-related proteins in the endoplasmic reticulum of developing lima bean seeds. In: Carnovale E, ed. In vitro and in vivo models for the evaluation of nutritional quality of legumes. COST Action 98, 6th Workshop, Rome, Italy: European Commission (in press).
    • (1997) In Vitro and in Vivo Models for the Evaluation of Nutritional Quality of Legumes
    • Faoro, F.1    Sparvoli, F.2    Ceriotti, A.3    Bollini, R.4
  • 26
    • 0001142403 scopus 로고
    • Transport and processing of the glycosylated precursor of concanavalin A in jack-bean
    • Faye L, Chrispeels MJ. 1987. Transport and processing of the glycosylated precursor of concanavalin A in jack-bean. Planta 170, 217-24.
    • (1987) Planta , vol.170 , pp. 217-224
    • Faye, L.1    Chrispeels, M.J.2
  • 27
    • 0000724871 scopus 로고
    • Apparent inhibition of β-fructosidase secretion by tunicamycin may be explained by breakdown of the unglycosylated protein during secretion
    • Faye L, Chrispeels MJ. 1989. Apparent inhibition of β-fructosidase secretion by tunicamycin may be explained by breakdown of the unglycosylated protein during secretion. Plant Physiology 89, 845-51.
    • (1989) Plant Physiology , vol.89 , pp. 845-851
    • Faye, L.1    Chrispeels, M.J.2
  • 28
    • 84989674553 scopus 로고
    • Structure, biosynthesis, and function of asparagine-linked glycans on plant glycoproteins
    • Faye L, Johnson KD, Sturm A, Chrispeels MJ. 1989. Structure, biosynthesis, and function of asparagine-linked glycans on plant glycoproteins. Physiologia Plantarum 75, 309-14.
    • (1989) Physiologia Plantarum , vol.75 , pp. 309-314
    • Faye, L.1    Johnson, K.D.2    Sturm, A.3    Chrispeels, M.J.4
  • 29
    • 0029040839 scopus 로고
    • The asparagine-linked oligosaccharides of the human chorionic gonadotropin β subunit facilitate correct disulphide bond pairing
    • Feng W, Matzuk MM, Mountjoy K, Bedows E, Ruddon RW, Boime I. 1995. The asparagine-linked oligosaccharides of the human chorionic gonadotropin β subunit facilitate correct disulphide bond pairing. Journal of Biological Chemistry 270, 11851-9.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 11851-11859
    • Feng, W.1    Matzuk, M.M.2    Mountjoy, K.3    Bedows, E.4    Ruddon, R.W.5    Boime, I.6
  • 30
    • 0030020169 scopus 로고    scopus 로고
    • A new stress protein: Synthesis of Schizosaccharomyces pombe UDP-Glc:glycoprotein glucosyl-transferase mRNA is induced by stress conditions but the enzyme is not essential for cell viability
    • Fernández F, Jannatipour M, Hellman U, Rokeach LA, Parodi AJ. 1996. A new stress protein: synthesis of Schizosaccharomyces pombe UDP-Glc:glycoprotein glucosyl-transferase mRNA is induced by stress conditions but the enzyme is not essential for cell viability. EMBO Journal 15, 705-13.
    • (1996) EMBO Journal , vol.15 , pp. 705-713
    • Fernández, F.1    Jannatipour, M.2    Hellman, U.3    Rokeach, L.A.4    Parodi, A.J.5
  • 31
    • 0028150802 scopus 로고
    • Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae
    • Fernández FS, Trombetta SE, Hellman U, Parodi AJ. 1994. Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae. Journal of Biological Chemistry 269, 30701-6.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 30701-30706
    • Fernández, F.S.1    Trombetta, S.E.2    Hellman, U.3    Parodi, A.J.4
  • 33
    • 0015501858 scopus 로고
    • Phytohemagglutinin of the lima bean (Phaseolus lunatus). Isolation, characterization, and interaction with type A blood-group substance
    • Galbraith W, Goldstein U. 1972. Phytohemagglutinin of the lima bean (Phaseolus lunatus). Isolation, characterization, and interaction with type A blood-group substance. Biochemistry 11, 3976-84.
    • (1972) Biochemistry , vol.11 , pp. 3976-3984
    • Galbraith, W.1    Goldstein, U.2
  • 34
    • 0018786653 scopus 로고
    • The nonglycosylated glycoprotein of vesicular stomatitis virus is temperature sensitive and undergoes intracellular aggregation at elevated temperatures
    • Gibson R, Schlesinger S, Kornfeld S. 1979. The nonglycosylated glycoprotein of vesicular stomatitis virus is temperature sensitive and undergoes intracellular aggregation at elevated temperatures. Journal of Biological Chemistry 254, 3600-7.
    • (1979) Journal of Biological Chemistry , vol.254 , pp. 3600-3607
    • Gibson, R.1    Schlesinger, S.2    Kornfeld, S.3
  • 36
    • 0023645327 scopus 로고
    • The mechanism of folding of pancreatic ribonucleases is independent of the presence of covalently linked carbohydrate
    • Graft R, Lang K, Yogi H, Schmid F. 1987. The mechanism of folding of pancreatic ribonucleases is independent of the presence of covalently linked carbohydrate. Journal of Biological Chemistry 262, 10624-9.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 10624-10629
    • Graft, R.1    Lang, K.2    Yogi, H.3    Schmid, F.4
  • 39
    • 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. Molecular Biology of the Cell 5, 253-65.
    • (1994) Molecular Biology of the Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 41
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Herbert DN, Foellmer B, Helenius A. 1995. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81, 425-33.
    • (1995) Cell , vol.81 , pp. 425-433
    • Herbert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 42
    • 0023100185 scopus 로고
    • Synthesis of mitogenic phytohemagglutinin-L in Escherichia coli
    • Hoffman LM, Dorialdson D. 1987. Synthesis of mitogenic phytohemagglutinin-L in Escherichia coli. Bio/technology 5, 157-60.
    • (1987) Bio/technology , vol.5 , pp. 157-160
    • Hoffman, L.M.1    Dorialdson, D.2
  • 43
    • 0029953675 scopus 로고    scopus 로고
    • Competition between folding and glycosylation in the endoplasmic reticulum
    • Holst B, Brunn AW, Kielland-Brandt MC, Winther JR. 1996. Competition between folding and glycosylation in the endoplasmic reticulum, EMBO Journal 15, 3538-46.
    • (1996) EMBO Journal , vol.15 , pp. 3538-3546
    • Holst, B.1    Brunn, A.W.2    Kielland-Brandt, M.C.3    Winther, J.R.4
  • 44
    • 0027415665 scopus 로고
    • Primary structure and characterization of an Arabidopsis thaliana calnexin-like protein
    • Huang L, Franklin AE, Huffman NE. 1993. Primary structure and characterization of an Arabidopsis thaliana calnexin-like protein. Journal of Biological Chemistry 268, 6560-6.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 6560-6566
    • Huang, L.1    Franklin, A.E.2    Huffman, N.E.3
  • 47
    • 0028921010 scopus 로고
    • The Schizosaccharomyces pombe homologue of the chaperone calnexin is essential for viability
    • Jannatipour M, Rokeach LA. 1995. The Schizosaccharomyces pombe homologue of the chaperone calnexin is essential for viability. Journal of Biological Chemistry 270, 4845-3.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 4845-4853
    • Jannatipour, M.1    Rokeach, L.A.2
  • 48
    • 0028340162 scopus 로고
    • The sequence of a second member of the lima bean lectin gene family and the expression and characterization of recombinant lectin in Escherichia coli
    • Jordan ET, Goldstein U. 1994. The sequence of a second member of the lima bean lectin gene family and the expression and characterization of recombinant lectin in Escherichia coli. Journal of Biological Chemistry 269, 7674-81.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 7674-7681
    • Jordan, E.T.1    Goldstein, U.2
  • 49
    • 0028676107 scopus 로고
    • Carbohydrate moiety of the Petunia inflata S-3 protein is not required for self-incompatibility interactions between pollen and pistil
    • Karunanandaa B, Huang S, Kao T. 1994. Carbohydrate moiety of the Petunia inflata S-3 protein is not required for self-incompatibility interactions between pollen and pistil. The Plant Cell 6, 1933-40.
    • (1994) The Plant Cell , vol.6 , pp. 1933-1940
    • Karunanandaa, B.1    Huang, S.2    Kao, T.3
  • 50
    • 0025130561 scopus 로고
    • Purification to homogeneity and properties of glucosidase II from mung bean seedlings and suspension-cultured soybean cells
    • Kaushal GP, Pastuszak I, Hatanaka K, Elbein AD. 1990. Purification to homogeneity and properties of glucosidase II from mung bean seedlings and suspension-cultured soybean cells. Journal of Biological Chemistry 265, 16271-9.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 16271-16279
    • Kaushal, G.P.1    Pastuszak, I.2    Hatanaka, K.3    Elbein, A.D.4
  • 51
    • 0027230418 scopus 로고
    • Biosynthesis of glucosidase II in suspension-cultured soybean cells
    • Kaushal GP, Zeng Y, Elbein AD. 1993. Biosynthesis of glucosidase II in suspension-cultured soybean cells. Journal of Biological Chemistry 268, 14536-42.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 14536-14542
    • Kaushal, G.P.1    Zeng, Y.2    Elbein, A.D.3
  • 52
    • 0026716017 scopus 로고
    • Oligosaccharyl-transferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kd protein
    • Kelleher D, Kreibich G, Gilmore R. 1992. Oligosaccharyl-transferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kd protein. Cell 69, 55-65.
    • (1992) Cell , vol.69 , pp. 55-65
    • Kelleher, D.1    Kreibich, G.2    Gilmore, R.3
  • 53
    • 0027507503 scopus 로고
    • Kinetics of folding and association of differently glycosylated variants of invertase from Saccharomyces cerevisiae
    • Kern G, Kern D, Jaenicke R, Seckler R. 1993. Kinetics of folding and association of differently glycosylated variants of invertase from Saccharomyces cerevisiae. Protein Scence 2, 1862-8.
    • (1993) Protein Scence , vol.2 , pp. 1862-1868
    • Kern, G.1    Kern, D.2    Jaenicke, R.3    Seckler, R.4
  • 54
    • 0030250175 scopus 로고    scopus 로고
    • Isolation and responses to stress of a gene that encodes a luminal binding protein in Arabidopsis thaliana
    • Koizumi N. 1996. Isolation and responses to stress of a gene that encodes a luminal binding protein in Arabidopsis thaliana. Plant Cell Physiology 37, 862-5.
    • (1996) Plant Cell Physiology , vol.37 , pp. 862-865
    • Koizumi, N.1
  • 57
    • 0028832726 scopus 로고
    • Cloning of two cDNAs encoding calnexin-like and calreticulin-like proteins from maize (Zea mays) leaves: Identification of potential Calcium-binding domains
    • Kwiatkowski BA, Zielinska-Kwiatkowska AG, Migdalski A, Kleczkowski LA, Wasilewska LD. 1995. Cloning of two cDNAs encoding calnexin-like and calreticulin-like proteins from maize (Zea mays) leaves: identification of potential Calcium-binding domains. Gene 165, 219-22.
    • (1995) Gene , vol.165 , pp. 219-222
    • Kwiatkowski, B.A.1    Zielinska-Kwiatkowska, A.G.2    Migdalski, A.3    Kleczkowski, L.A.4    Wasilewska, L.D.5
  • 58
    • 0001847507 scopus 로고
    • Partial characterization of the amylase inhibitor of black beans (Phaseolus vulgaris), variety Rico 23
    • Lajolo F, Finardi Filho F. 1985. Partial characterization of the amylase inhibitor of black beans (Phaseolus vulgaris), variety Rico 23. Journal of Agricultural Food Chemistry 33, 132-8.
    • (1985) Journal of Agricultural Food Chemistry , vol.33 , pp. 132-138
    • Lajolo, F.1    Finardi Filho, F.2
  • 59
  • 60
    • 0027519943 scopus 로고
    • Protein glycosylation. Structural and functional aspects
    • Lis H, Sharon N. 1993. Protein glycosylation. Structural and functional aspects. European Journal of Biochemistry 218, 1-27.
    • (1993) European Journal of Biochemistry , vol.218 , pp. 1-27
    • Lis, H.1    Sharon, N.2
  • 61
    • 0021925967 scopus 로고
    • Precursors of ricin and Ricinus communis agglutinin. Glycosylation and processing during synthesis and intracellular transport
    • Lord JM. 1985. Precursors of ricin and Ricinus communis agglutinin. Glycosylation and processing during synthesis and intracellular transport. European Journal of Biochemistry 146, 411-16.
    • (1985) European Journal of Biochemistry , vol.146 , pp. 411-416
    • Lord, J.M.1
  • 62
    • 0030900410 scopus 로고    scopus 로고
    • The rate of phaseolin assembly is controlled by the glucosylation state of its N-linked oligosaccharide chains
    • Lupattelli F, Pedrazzini E, Bollini R, Vitale A, Ceriotti A. 1997. The rate of phaseolin assembly is controlled by the glucosylation state of its N-linked oligosaccharide chains. The Plant Cell 9, 597-609.
    • (1997) The Plant Cell , vol.9 , pp. 597-609
    • Lupattelli, F.1    Pedrazzini, E.2    Bollini, R.3    Vitale, A.4    Ceriotti, A.5
  • 63
    • 0030933219 scopus 로고    scopus 로고
    • Disulphide bond formation is a determinant of glycosylation site usage in the hemagglutinin-neuramidase glycoprotein in" Newcastle-Disease virus
    • McGinne LW, Morrison TG. 1997. Disulphide bond formation is a determinant of glycosylation site usage in the hemagglutinin-neuramidase glycoprotein in" Newcastle-Disease virus. Journal of Virology 71, 3083-9.
    • (1997) Journal of Virology , vol.71 , pp. 3083-3089
    • McGinne, L.W.1    Morrison, T.G.2
  • 64
    • 0025339572 scopus 로고
    • The yeast KRE5 gene encodes a probable endoplasmic reticulum protein reqjuired for (1-6)-β-D-glucan synthesis and normal cell growth
    • Meaden P, Hill K, Wagner J, Slipetz D, Sommer SS, Bussey H. 1990, The yeast KRE5 gene encodes a probable endoplasmic reticulum protein reqjuired for (1-6)-]β-D-glucan synthesis and normal cell growth. Molecular and Cellular Biology 10, 3013-19.
    • (1990) Molecular and Cellular Biology , vol.10 , pp. 3013-3019
    • Meaden, P.1    Hill, K.2    Wagner, J.3    Slipetz, D.4    Sommer, S.S.5    Bussey, H.6
  • 66
    • 0026563682 scopus 로고
    • Non-glycosylated recombinant pro-concanavalin A is active without polypeptide cleavage
    • Min W, Dunn AJ, Jones DH. 1992. Non-glycosylated recombinant pro-concanavalin A is active without polypeptide cleavage. EMBO Journal 11, 1303-7.
    • (1992) EMBO Journal , vol.11 , pp. 1303-1307
    • Min, W.1    Dunn, A.J.2    Jones, D.H.3
  • 67
    • 0027469640 scopus 로고
    • Direct demonstration of the essential role of the intramolecular high-mannose oligosaccharide chains in the folding and assembly of soybean (Glycine max) lectin polypeptides
    • Nagai K, Yamaguchi H. 1993. Direct demonstration of the essential role of the intramolecular high-mannose oligosaccharide chains in the folding and assembly of soybean (Glycine max) lectin polypeptides. Journal of Biochemistry 113, 123-5.
    • (1993) Journal of Biochemistry , vol.113 , pp. 123-125
    • Nagai, K.1    Yamaguchi, H.2
  • 70
    • 0031131643 scopus 로고    scopus 로고
    • Abundant accumulation of the calcium-binding molecular chaperone calreticulin in specific floral tissues of Arabidopsis thaliana
    • Nelson DE, Glaunsinger B, Bohnert HJ. 1997, Abundant accumulation of the calcium-binding molecular chaperone calreticulin in specific floral tissues of Arabidopsis thaliana. Plant Physiology 114, 29-37.
    • (1997) Plant Physiology , vol.114 , pp. 29-37
    • Nelson, D.E.1    Glaunsinger, B.2    Bohnert, H.J.3
  • 71
    • 0030267033 scopus 로고    scopus 로고
    • Modulation of protein structure and function by asparagine-linked glycosylation
    • O'Connor S, Imperiali B. 1996. Modulation of protein structure and function by asparagine-linked glycosylation. Chemical Biology 3, 803-12.
    • (1996) Chemical Biology , vol.3 , pp. 803-812
    • O'Connor, S.1    Imperiali, B.2
  • 73
    • 0024296803 scopus 로고
    • Post-translational changes in tertiary and quaternary structure of the insulin. proreceptor
    • Olson TS, Bamberger MJ, Lane MD. 1988. Post-translational changes in tertiary and quaternary structure of the insulin. proreceptor. Journal of Biological Chemistry 263, 7342-51.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 7342-7351
    • Olson, T.S.1    Bamberger, M.J.2    Lane, M.D.3
  • 74
    • 0028987945 scopus 로고
    • Drosophila UDP-glucose:glycoprotein glucosyltransferase: Sequence and characterization of an enzyme that distinguishes between denatured and native proteins
    • Parker CG, Fessier LI, Nelson RE, Fessier JH. 1995. Drosophila UDP-glucose:glycoprotein glucosyltransferase: sequence and characterization of an enzyme that distinguishes between denatured and native proteins. EMBO Journal 14, 1294-303.
    • (1995) EMBO Journal , vol.14 , pp. 1294-1303
    • Parker, C.G.1    Fessier, L.I.2    Nelson, R.E.3    Fessier, J.H.4
  • 75
    • 0029006125 scopus 로고
    • + in Schizosaccharomyces pombe, is an essential gene which can be complemented by its soluble ER domain
    • + in Schizosaccharomyces pombe, is an essential gene which can be complemented by its soluble ER domain. EMBO Journal 14, 3064-72.
    • (1995) EMBO Journal , vol.14 , pp. 3064-3072
    • Parlati, F.1    Dignard, D.2    Bergeron, J.J.M.3    Thomas, D.Y.4
  • 79
    • 0029160540 scopus 로고
    • Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins
    • Peterson JR, Ora A, Van PN, Helenius A. 1995. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Molecular Biology of the Cell 6, 1173-84.
    • (1995) Molecular Biology of the Cell , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Van, P.N.3    Helenius, A.4
  • 80
    • 77956983260 scopus 로고
    • Effect of tunicamycin on peroxidase release by cultured peanut suspension cells
    • Ravi K, Hu C, Reddi PS, van Huistee RB. 1986. Effect of tunicamycin on peroxidase release by cultured peanut suspension cells Journal of Experimental Botany 37, 1708-15.
    • (1986) Journal of Experimental Botany , vol.37 , pp. 1708-1715
    • Ravi, K.1    Hu, C.2    Reddi, P.S.3    Van Huistee, R.B.4
  • 81
    • 0023940624 scopus 로고
    • Post-translational protein modification in the endoplasmic reticulum. Demonstration of fatty acylase and deoxymannojirimycin-sensitive α-mannosidase activities
    • Rizzolo L, Kornfeld R. 1988. Post-translational protein modification in the endoplasmic reticulum. Demonstration of fatty acylase and deoxymannojirimycin-sensitive α-mannosidase activities. Journal of Biological Chemistry 263, 9520-25.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 9520-9525
    • Rizzolo, L.1    Kornfeld, R.2
  • 82
    • 0027238117 scopus 로고
    • Role of conserved glycosylation sites in maturation and-transport of influenza A virus hemagglutinin
    • Roberts PC, Garten W, Klenk H-D. 1993, Role of conserved glycosylation sites in maturation and-transport of influenza A virus hemagglutinin. Journal of Virology 67, 3048-60.
    • (1993) Journal of Virology , vol.67 , pp. 3048-3060
    • Roberts, P.C.1    Garten, W.2    Klenk, H.-D.3
  • 83
    • 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 AR, Simons JF, Trombetta ES, Helenius A. 1996. N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin. EMBO Journal 15, 6921-30.
    • (1996) EMBO Journal , vol.15 , pp. 6921-6930
    • Rodan, A.R.1    Simons, J.F.2    Trombetta, E.S.3    Helenius, A.4
  • 84
    • 0025939115 scopus 로고
    • Structure of ricin B-chain at 2.5 Å resolution
    • Rutenber E, Robertus JD. 1991. Structure of ricin B-chain at 2.5 Å resolution. Proteins 10, 260-9.
    • (1991) Proteins , vol.10 , pp. 260-269
    • Rutenber, E.1    Robertus, J.D.2
  • 85
    • 84989741624 scopus 로고
    • The α-amylase inhibitor of bean seed: Two-step proteolytic maturation in the protein storage vacuoles of the developing cotyledon
    • Santino A, Daminati MG, Vitale A, Bollini R. 1992. The α-amylase inhibitor of bean seed: two-step proteolytic maturation in the protein storage vacuoles of the developing cotyledon. Physiotogia Plantarum 85, 425-32.
    • (1992) Physiotogia Plantarum , vol.85 , pp. 425-432
    • Santino, A.1    Daminati, M.G.2    Vitale, A.3    Bollini, R.4
  • 86
    • 0026337737 scopus 로고
    • Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose
    • Shaanan B, Lis H, Sharon N. 1991. Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose. Science 254, 862-6.
    • (1991) Science , vol.254 , pp. 862-866
    • Shaanan, B.1    Lis, H.2    Sharon, N.3
  • 87
    • 0026600774 scopus 로고
    • The glycoprotein precursor of concanavalin A is converted to an active lectin by deglycosylation
    • Sheldon PS, Bowles DJ. 1992. The glycoprotein precursor of concanavalin A is converted to an active lectin by deglycosylation. EMBO Journal 11, 1297-301.
    • (1992) EMBO Journal , vol.11 , pp. 1297-1301
    • Sheldon, P.S.1    Bowles, D.J.2
  • 88
    • 0029991763 scopus 로고    scopus 로고
    • Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase
    • Silberstein S, Gilmore R. 1996. Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase. FASEB Journal 10, 849-58.
    • (1996) FASEB Journal , vol.10 , pp. 849-858
    • Silberstein, S.1    Gilmore, R.2
  • 89
    • 0025405807 scopus 로고
    • Expression of mutant patatin protein in transgenic tobacco plants: Role of glycans and intracellular location
    • Sonnewald U, von Schaewen A, Willmitzer L. 1990. Expression of mutant patatin protein in transgenic tobacco plants: role of glycans and intracellular location. The Plant Cell 2, 345-55.
    • (1990) The Plant Cell , vol.2 , pp. 345-355
    • Sonnewald, U.1    Von Schaewen, A.2    Willmitzer, L.3
  • 90
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
    • Sousa M, Ferrero-Garcia MA, Parodi AJ. 1992. Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry 31, 97-105.
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.1    Ferrero-Garcia, M.A.2    Parodi, A.J.3
  • 91
    • 0029126624 scopus 로고
    • The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
    • Sousa M, Parodi A. 1995. The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO Journal 14, 4196-203.
    • (1995) EMBO Journal , vol.14 , pp. 4196-4203
    • Sousa, M.1    Parodi, A.2
  • 92
    • 85038528505 scopus 로고    scopus 로고
    • Possible role(s) of glycosylation in the biological properties of lectins and related proteins
    • Bardocz S and Pusztai A, eds. COST Action 98, 7th Workshop, Lake Balaton, Hungary: European Commission, (in press)
    • Sparvoli F, Daminati M, Cantoni R, Bollini R. 1997. Possible role(s) of glycosylation in the biological properties of lectins and related proteins. In: Bardocz S and Pusztai A, eds. Biomedical and therapeutical applications of dietary lectins. COST Action 98, 7th Workshop, Lake Balaton, Hungary: European Commission, (in press).
    • (1997) Biomedical and Therapeutical Applications of Dietary Lectins
    • Sparvoli, F.1    Daminati, M.2    Cantoni, R.3    Bollini, R.4
  • 93
    • 0030060231 scopus 로고    scopus 로고
    • In vivo endoproteolytically cleaved phaseolin is stable and accumulates in developing Phaseolus lunatus L. seeds
    • Sparvoli F, Daminati MG, Lioi L, Bollini R. 1996. In vivo endoproteolytically cleaved phaseolin is stable and accumulates in developing Phaseolus lunatus L. seeds. Biochimica et Biophysica Acta 1292, 15-22.
    • (1996) Biochimica et Biophysica Acta , vol.1292 , pp. 15-22
    • Sparvoli, F.1    Daminati, M.G.2    Lioi, L.3    Bollini, R.4
  • 95
    • 10544244921 scopus 로고
    • N-glycosylation of plant proteins
    • Montreuil J, Schachter H, Vliegenthart JFG, eds. Amsterdam: Elsevier Science
    • Sturm A. 1995. N-glycosylation of plant proteins. In: Montreuil J, Schachter H, Vliegenthart JFG, eds. Glycoproteins, Amsterdam: Elsevier Science, 521-41.
    • (1995) Glycoproteins , pp. 521-541
    • Sturm, A.1
  • 96
    • 0024598083 scopus 로고
    • Selective retention of monoglucosylated high mannose oligosaccharides by a class of mutant vesicular stomatitis virus G proteins
    • Suh P, Bergmann JE, Gabel CA. 1989. Selective retention of monoglucosylated high mannose oligosaccharides by a class of mutant vesicular stomatitis virus G proteins. Journal of Cell Biology 108, 811-19.
    • (1989) Journal of Cell Biology , vol.108 , pp. 811-819
    • Suh, P.1    Bergmann, J.E.2    Gabel, C.A.3
  • 98
    • 0031045007 scopus 로고    scopus 로고
    • Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum
    • Tatu U, Helenius A. 1997. Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. Journal of Cell Biology 136, 555-65.
    • (1997) Journal of Cell Biology , vol.136 , pp. 555-565
    • Tatu, U.1    Helenius, A.2
  • 99
    • 0026799435 scopus 로고
    • Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:glycoprotein glucosyltransferase
    • Trombetta SE, Parodi AJ. 1992. Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:glycoprotein glucosyltransferase. Journal of Biological Chemistry 267, 9236-40.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 9236-9240
    • Trombetta, S.E.1    Parodi, A.J.2
  • 100
    • 0030030740 scopus 로고    scopus 로고
    • Stabilization of lysozyme by introducing N-glycosylation signal sequence
    • Ueda T, Iwashita H, Hashimoto Y, Imoto T. 1996. Stabilization of lysozyme by introducing N-glycosylation signal sequence. Journal of Biochemistry 119, 157-61.
    • (1996) Journal of Biochemistry , vol.119 , pp. 157-161
    • Ueda, T.1    Iwashita, H.2    Hashimoto, Y.3    Imoto, T.4
  • 101
    • 0027318961 scopus 로고
    • Biological role of oligosaccharides: All of the theories are correct
    • Varki A. 1993. Biological role of oligosaccharides: all of the theories are correct. Glycobiology 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 102
    • 0029167492 scopus 로고
    • The binding protein associates with monomeric phaseolin
    • Vitale A, Bielli A, Ceriotti A. 1995. The binding protein associates with monomeric phaseolin. Plant Physiology 107, 1411-18.
    • (1995) Plant Physiology , vol.107 , pp. 1411-1418
    • Vitale, A.1    Bielli, A.2    Ceriotti, A.3
  • 103
    • 85051589413 scopus 로고
    • Legume storage proteins
    • Kigel J, Galili G, eds. New York: Marcel Dekker, Inc.
    • Vitale A, Bollini R. 1995. Legume storage proteins. In: Kigel J, Galili G, eds. Seed development and germination. New York: Marcel Dekker, Inc., 73-102.
    • (1995) Seed Development and Germination , pp. 73-102
    • Vitale, A.1    Bollini, R.2
  • 104
    • 0001143106 scopus 로고
    • The role of the endoplasmic reticulum in protein synthesis, modification and intracellular transport
    • Vitale A, Ceriotti A, Denecke J. 1993. The role of the endoplasmic reticulum in protein synthesis, modification and intracellular transport. Journal of Experimental Botany 44, 1417-44.
    • (1993) Journal of Experimental Botany , vol.44 , pp. 1417-1444
    • Vitale, A.1    Ceriotti, A.2    Denecke, J.3
  • 105
    • 0024301301 scopus 로고
    • In vitro mutated phytohemagglutinin genes expressed in tobacco seeds: Role of glycans in protein targeting and stability
    • Voelker TA, Herman EM, Chrispeels MJ. 1989. In vitro mutated phytohemagglutinin genes expressed in tobacco seeds: role of glycans in protein targeting and stability. The Plant Cell 1, 95-104.
    • (1989) The Plant Cell , vol.1 , pp. 95-104
    • Voelker, T.A.1    Herman, E.M.2    Chrispeels, M.J.3
  • 107
    • 0029904281 scopus 로고    scopus 로고
    • Influence of the carbohydrate moiety on the stability of glycoproteins
    • Wang C, Eufemi M, Turano C, Giartosio A. 1996. Influence of the carbohydrate moiety on the stability of glycoproteins. Biochemistry 35, 7299-307.
    • (1996) Biochemistry , vol.35 , pp. 7299-7307
    • Wang, C.1    Eufemi, M.2    Turano, C.3    Giartosio, A.4
  • 108
    • 0025405663 scopus 로고
    • Role of propeptide glycan in post-translational processing and transport of barley lectin to vacuoles in transgenic tobacco
    • Wilkins TA, Bednarek SY, Raikhel NV. 1990. Role of propeptide glycan in post-translational processing and transport of barley lectin to vacuoles in transgenic tobacco. The Plant Cell 2, 301-13.
    • (1990) The Plant Cell , vol.2 , pp. 301-313
    • Wilkins, T.A.1    Bednarek, S.Y.2    Raikhel, N.V.3
  • 109
    • 0025782587 scopus 로고
    • The conformational effects of N-glycosylation on the tailpiece of serum IgM
    • Wormald MR, Dwek RA. 1991. The conformational effects of N-glycosylation on the tailpiece of serum IgM. European Journal of Biochemistry 198, 131-9.
    • (1991) European Journal of Biochemistry , vol.198 , pp. 131-139
    • Wormald, M.R.1    Dwek, R.A.2
  • 111
    • 0030933129 scopus 로고    scopus 로고
    • Conformation-independent binding of monoglucosylated ribonuclease B to calnexin
    • Zapun A, Petrecu S, Rudd P, Dweck RA, Thomas DY, Bergeron JJM. 1997. Conformation-independent binding of monoglucosylated ribonuclease B to calnexin. Cell 88, 29-38.
    • (1997) Cell , vol.88 , pp. 29-38
    • Zapun, A.1    Petrecu, S.2    Rudd, P.3    Dweck, R.A.4    Thomas, D.Y.5    Bergeron, J.J.M.6
  • 112
    • 0030941217 scopus 로고    scopus 로고
    • Restoration of lectin activity to a non-glycosylated ricin B-chain mutant by the introduction of a novel N-glycosylation site
    • Zhan J, de Sousa M, Chaddock JA, Roberts LM, Lord JM. 1997. Restoration of lectin activity to a non-glycosylated ricin B-chain mutant by the introduction of a novel N-glycosylation site. FEES Letters 407, 271-4.
    • (1997) FEES Letters , vol.407 , pp. 271-274
    • Zhan, J.1    De Sousa, M.2    Chaddock, J.A.3    Roberts, L.M.4    Lord, J.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.