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Volumn 3, Issue 10, 1998, Pages 396-399

Calreticulin and calnexin in plants

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EID: 0031680678     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1360-1385(98)01312-0     Document Type: Review
Times cited : (60)

References (46)
  • 1
    • 0030019434 scopus 로고    scopus 로고
    • Soluble endoplasmic reticulum resident proteins and their function in protein synthesis and transport
    • Denecke J. Soluble endoplasmic reticulum resident proteins and their function in protein synthesis and transport. Plant Physiol. Biochem. 34:1996;197-205.
    • (1996) Plant Physiol. Biochem. , vol.34 , pp. 197-205
    • Denecke, J.1
  • 2
    • 0030897340 scopus 로고    scopus 로고
    • Calreticulin
    • Krause K.H., Michalak M. Calreticulin. Cell. 88:1997;439-443.
    • (1997) Cell , vol.88 , pp. 439-443
    • Krause, K.H.1    Michalak, M.2
  • 3
    • 0000531516 scopus 로고
    • Analysis of sorting signals responsible for the accumulation of soluble reticuloplasmins in the plant endoplasmic reticulum
    • Denecke J.et al. Analysis of sorting signals responsible for the accumulation of soluble reticuloplasmins in the plant endoplasmic reticulum. J. Exp. Bot. 44:1993;213-221.
    • (1993) J. Exp. Bot. , vol.44 , pp. 213-221
    • Denecke, J.1
  • 4
    • 0027218614 scopus 로고
    • Purification of calreticulin-like protein(s) from spinach leaves
    • Menegazzi P.et al. Purification of calreticulin-like protein(s) from spinach leaves. Biochem. Biophys. Res. Commun. 190:1993;1130-1135.
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 1130-1135
    • Menegazzi, P.1
  • 5
    • 0029278937 scopus 로고
    • The tobacco homolog of mammalian calreticulin is present in protein complexes in vivo
    • Denecke J.et al. The tobacco homolog of mammalian calreticulin is present in protein complexes in vivo. Plant Cell. 7:1995;391-406.
    • (1995) Plant Cell , vol.7 , pp. 391-406
    • Denecke, J.1
  • 6
    • 0028450064 scopus 로고
    • Identification and characterization of cDNA clones encoding plant calreticulinin barley
    • Chen F.et al. Identification and characterization of cDNA clones encoding plant calreticulinin barley. Plant Cell. 6:1994;835-843.
    • (1994) Plant Cell , vol.6 , pp. 835-843
    • Chen, F.1
  • 7
    • 0028859890 scopus 로고
    • Purification and sequencing and functions of calreticulin from maize
    • Napier R.M.et al. Purification and sequencing and functions of calreticulin from maize. J. Exp. Bot. 46:1995;1603-1613.
    • (1995) J. Exp. Bot. , vol.46 , pp. 1603-1613
    • Napier, R.M.1
  • 8
    • 0030130430 scopus 로고    scopus 로고
    • Isolation of full-length cDNA encoding calreticulin from a PCR library of in vitro zygotes of maize
    • Dresselhaus T.et al. Isolation of full-length cDNA encoding calreticulin from a PCR library of in vitro zygotes of maize. Plant Mol. Biol. 31:1996;23-34.
    • (1996) Plant Mol. Biol. , vol.31 , pp. 23-34
    • Dresselhaus, T.1
  • 10
    • 0031907904 scopus 로고    scopus 로고
    • Gingko biloba expresses calreticulin, the major calcium-binding reticuloplasmin in eukaryotic cells
    • Nardi M.C.et al. Gingko biloba expresses calreticulin, the major calcium-binding reticuloplasmin in eukaryotic cells. Bot. Acta. 111:1998;66-70.
    • (1998) Bot. Acta , vol.111 , pp. 66-70
    • Nardi, M.C.1
  • 11
    • 0032077441 scopus 로고    scopus 로고
    • Functional conservation of calreticulin in Euglena gracilis
    • Navazio L.et al. Functional conservation of calreticulin in Euglena gracilis. J. Eukaryot. Microbiol. 45:1998;307-313.
    • (1998) J. Eukaryot. Microbiol. , vol.45 , pp. 307-313
    • Navazio, L.1
  • 12
    • 0025937289 scopus 로고
    • SSRα and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane
    • Wada I.et al. SSRα and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. J. Biol. Chem. 266:1991;19599-19610.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19599-19610
    • Wada, I.1
  • 13
    • 0027415665 scopus 로고
    • Primary structure and characterization of an Arabidopsis thaliana calnexin-like protein
    • Huang L., Franklin A.E., Hoffman N.E. Primary structure and characterization of an Arabidopsis thaliana calnexin-like protein. J. Biol. Chem. 268:1993;6560-6566.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6560-6566
    • Huang, L.1    Franklin, A.E.2    Hoffman, N.E.3
  • 14
    • 0026757547 scopus 로고
    • Calreticulin
    • Michalak M.et al. Calreticulin. Biochem. J. 285:1992;681-692.
    • (1992) Biochem. J. , vol.285 , pp. 681-692
    • Michalak, M.1
  • 15
    • 0344451953 scopus 로고    scopus 로고
    • 2+ influx
    • 2+ influx. J. Biol. Chem. 267:1996;2557-2562.
    • (1996) J. Biol. Chem. , vol.267 , pp. 2557-2562
    • Mery, L.1
  • 16
    • 0030978516 scopus 로고    scopus 로고
    • Calreticulin is essential for integrin-mediated calcium signalling and cell adhesion
    • Coppolino M.G.et al. Calreticulin is essential for integrin-mediated calcium signalling and cell adhesion. Nature. 386:1997;843-847.
    • (1997) Nature , vol.386 , pp. 843-847
    • Coppolino, M.G.1
  • 17
    • 0027955571 scopus 로고
    • Modulation of gene-expression by calreticulin binding to the glucocorticoid receptor
    • Burns K.et al. Modulation of gene-expression by calreticulin binding to the glucocorticoid receptor. Nature. 367:1994;476-480.
    • (1994) Nature , vol.367 , pp. 476-480
    • Burns, K.1
  • 18
    • 0027976780 scopus 로고
    • Inhibition of nuclear hormone-receptor activity by calreticulin
    • Dedhar S.et al. Inhibition of nuclear hormone-receptor activity by calreticulin. Nature. 367:1994;480-483.
    • (1994) Nature , vol.367 , pp. 480-483
    • Dedhar, S.1
  • 19
    • 0029828912 scopus 로고    scopus 로고
    • Endoplasmic reticulum form of calreticulin modulates glucocorticoid-sensitive gene expression
    • Michalak M.et al. Endoplasmic reticulum form of calreticulin modulates glucocorticoid-sensitive gene expression. J. Biol. Chem. 271:1996;29436-29445.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29436-29445
    • Michalak, M.1
  • 20
    • 0030229971 scopus 로고    scopus 로고
    • Protein degradation: Go outside and see the proteasome
    • Lord M.J. Protein degradation: Go outside and see the proteasome. Curr. Biol. 6:1996;1067-1069.
    • (1996) Curr. Biol. , vol.6 , pp. 1067-1069
    • Lord, M.J.1
  • 21
    • 0029751274 scopus 로고    scopus 로고
    • Primary structure of the N-linked carbohydrate chains from spinach leaves
    • Navazio L.et al. Primary structure of the N-linked carbohydrate chains from spinach leaves. Glycoconjugate J. 13:1996;977-983.
    • (1996) Glycoconjugate J. , vol.13 , pp. 977-983
    • Navazio, L.1
  • 22
    • 0001116042 scopus 로고    scopus 로고
    • Identification and localization of calreticulin in plant cells
    • Opas M.et al. Identification and localization of calreticulin in plant cells. Protoplasma. 191:1996;164-171.
    • (1996) Protoplasma , vol.191 , pp. 164-171
    • Opas, M.1
  • 23
    • 0031131643 scopus 로고    scopus 로고
    • Abundant accumulation of the calcium binding molecular chaperone calreticulin in specific floral tissues of Arabidopsis thaliana
    • Nelson D.E., Glaunsinger B., Bohnert H.J. Abundant accumulation of the calcium binding molecular chaperone calreticulin in specific floral tissues of Arabidopsis thaliana. Plant Physiol. 114:1997;29-37.
    • (1997) Plant Physiol. , vol.114 , pp. 29-37
    • Nelson, D.E.1    Glaunsinger, B.2    Bohnert, H.J.3
  • 24
    • 0030834284 scopus 로고    scopus 로고
    • Identification of calreticulin-like protein as one of the phosphoproteins modulated in response to oligogalacturonides in tobacco cells
    • Droillard M.J.et al. Identification of calreticulin-like protein as one of the phosphoproteins modulated in response to oligogalacturonides in tobacco cells. Planta. 202:1997;341-348.
    • (1997) Planta , vol.202 , pp. 341-348
    • Droillard, M.J.1
  • 25
    • 0029989731 scopus 로고    scopus 로고
    • Plant calreticulin is specifically and efficiently phosphorylated by protein kinase CK2
    • Baldan B.et al. Plant calreticulin is specifically and efficiently phosphorylated by protein kinase CK2. Biochem. Biophys. Res. Commun. 221:1996;498-502.
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 498-502
    • Baldan, B.1
  • 26
    • 0028964421 scopus 로고
    • Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
    • Nauseef W.M., McCormick S.J., Clark R.A. Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J. Biol. Chem. 270:1995;4741-4747.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4741-4747
    • Nauseef, W.M.1    McCormick, S.J.2    Clark, R.A.3
  • 27
    • 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. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J. 15:1996;2961-2968.
    • (1996) EMBO J. , vol.15 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 28
    • 0030053103 scopus 로고    scopus 로고
    • Calreticulin interacts with newly synthesised human immunodeficiency virus type I envelope glycoprotein, suggesting a chaperone function similar to that of calnexin
    • Otteken A., Moss B. Calreticulin interacts with newly synthesised human immunodeficiency virus type I envelope glycoprotein, suggesting a chaperone function similar to that of calnexin. J. Biol. Chem. 271:1996;97-103.
    • (1996) J. Biol. Chem. , vol.271 , pp. 97-103
    • Otteken, A.1    Moss, B.2
  • 29
    • 0028147528 scopus 로고
    • Retention of unassembled components of integral membrane proteins by calnexin
    • Rajagopalan S., Xu Y., Brenner M.B. Retention of unassembled components of integral membrane proteins by calnexin. Science. 263:1994;387-389.
    • (1994) Science , vol.263 , pp. 387-389
    • Rajagopalan, S.1    Xu, Y.2    Brenner, M.B.3
  • 30
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert D.N., Foellmer B., Helenius A. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell. 81:1995;425-433.
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 31
    • 0345314884 scopus 로고    scopus 로고
    • In vitro characterization of the lectin properties of purified recombinant calnexin and calreticulin
    • Vassilakos A.et al. In vitro characterization of the lectin properties of purified recombinant calnexin and calreticulin. FASEB J. 10:1996;688.
    • (1996) FASEB J. , vol.10 , pp. 688
    • Vassilakos, A.1
  • 32
    • 0031045007 scopus 로고    scopus 로고
    • Interactions between newly synthesised glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum
    • Tatu U., Helenius A. Interactions between newly synthesised glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J. Cell Biol. 136:1997;555-565.
    • (1997) J. Cell Biol. , vol.136 , pp. 555-565
    • Tatu, U.1    Helenius, A.2
  • 33
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality-control
    • Hammond C., Braakman I., Helenius A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality-control. Proc. Natl. Acad. Sci. U. S. A. 91:1994;913-917.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 34
    • 0029126624 scopus 로고
    • The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
    • Sousa M., Parodi A.J. The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J. 14:1995;4196-4203.
    • (1995) EMBO J. , vol.14 , pp. 4196-4203
    • Sousa, M.1    Parodi, A.J.2
  • 35
    • 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.et al. N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin. EMBO J. 15:1996;6921-6930.
    • (1996) EMBO J. , vol.15 , pp. 6921-6930
    • Rodan, A.R.1
  • 36
    • 15844386822 scopus 로고    scopus 로고
    • Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi
    • Spiro R.G.et al. Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi. J. Biol. Chem. 271:1996;11588-11594.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11588-11594
    • Spiro, R.G.1
  • 37
    • 0030900410 scopus 로고    scopus 로고
    • The rate of phaseolin assembly is controlled by the glucosylation state of its N-linked oligosaccharide chains
    • Lupattelli F.et al. The rate of phaseolin assembly is controlled by the glucosylation state of its N-linked oligosaccharide chains. Plant Cell. 9:1997;597-609.
    • (1997) Plant Cell , vol.9 , pp. 597-609
    • Lupattelli, F.1
  • 38
    • 0031774263 scopus 로고    scopus 로고
    • BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress
    • Crofts A.J.et al. BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress. Plant Cell. 10:1998;813-823.
    • (1998) Plant Cell , vol.10 , pp. 813-823
    • Crofts, A.J.1
  • 39
    • 0029134004 scopus 로고
    • Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms
    • Wada I.et al. Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms. J. Biol. Chem. 270:1995;20298-20304.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20298-20304
    • Wada, I.1
  • 40
    • 0031832284 scopus 로고    scopus 로고
    • +-ATPase from oat seedlings
    • +-ATPase from oat seedlings. Plant Cell. 10:1998;119-130.
    • (1998) Plant Cell , vol.10 , pp. 119-130
    • Li, X.H.1
  • 41
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond C., Helenius A. Quality control in the secretory pathway. Curr. Opin. Cell Biol. 7:1995;523-529.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 42
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase Erp57 with nascent glycoproteins
    • Oliver J.D.et al. Interaction of the thiol-dependent reductase Erp57 with nascent glycoproteins. Science. 275:1997;86-88.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1
  • 43
    • 0032513212 scopus 로고    scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with Erp57
    • Zapun A.et al. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with Erp57. J. Biol. Chem. 273:1998;6009-6012.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6009-6012
    • Zapun, A.1
  • 44
    • 0032522392 scopus 로고    scopus 로고
    • ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly
    • Lindquist J.A.et al. ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. EMBO J. 17:1998;2186-2195.
    • (1998) EMBO J. , vol.17 , pp. 2186-2195
    • Lindquist, J.A.1
  • 45
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • Booth C., Koch G.L.E. Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell. 59:1989;729-737.
    • (1989) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, G.L.E.2
  • 46
    • 0008881217 scopus 로고
    • Coordinate induction of three ER-lumenal stress proteins in maize endosperm mutants
    • Boston R.S., Gillikin J.W., Wrobel R.L. Coordinate induction of three ER-lumenal stress proteins in maize endosperm mutants. J. Cell. Biochem. 19A:1995;143.
    • (1995) J. Cell. Biochem. , vol.19 , pp. 143
    • Boston, R.S.1    Gillikin, J.W.2    Wrobel, R.L.3


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