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Volumn 20, Issue 6, 1996, Pages 413-422

Protein retention in the endoplasmic reticulum of insect cells is not compromised by baculovirus infection

Author keywords

Endoplasmic reticulum; Immunolocalization; Insect cells; Maize auxin binding protein; Protein targeting; Spodoptera frugiperda

Indexed keywords

MUTANT PROTEIN; PROTEIN; SIGNAL PEPTIDE; VEGETABLE PROTEIN;

EID: 0030174957     PISSN: 10656995     EISSN: None     Source Type: Journal    
DOI: 10.1006/cbir.1996.0052     Document Type: Article
Times cited : (12)

References (26)
  • 1
    • 0029548582 scopus 로고    scopus 로고
    • Efficient membrane targeting of the chick nicotinic acetylcholine receptor α-subunit in stable insect cell lines
    • ATKINSON AE, HENDERSON J, KING LA, 1996. Efficient membrane targeting of the chick nicotinic acetylcholine receptor α-subunit in stable insect cell lines. Cytotechnology 19: 37-42.
    • (1996) Cytotechnology , vol.19 , pp. 37-42
    • Atkinson, A.E.1    Henderson, J.2    King, L.A.3
  • 2
    • 0029137222 scopus 로고
    • Tracking auxin receptors using functional approaches
    • BARBIER-BRYGOO H, 1995. Tracking auxin receptors using functional approaches. Crit Rev Plant Sci 14: 1-26.
    • (1995) Crit Rev Plant Sci , vol.14 , pp. 1-26
    • Barbier-Brygoo, H.1
  • 3
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • BOOTH C, KOCH GLE, 1989. Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell 59: 729-737.
    • (1989) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, G.L.E.2
  • 4
    • 0028675536 scopus 로고
    • Effects of co-expressing chaperone BiP on functional antibody-production in the baculovirus system
    • HSU TA, EIDEN JJ, BOURGAREL P, MEO T, BETENBAUGH MJ, 1994. Effects of co-expressing chaperone BiP on functional antibody-production in the baculovirus system. Protein Express Purific 5: 595-603.
    • (1994) Protein Express Purific , vol.5 , pp. 595-603
    • Hsu, T.A.1    Eiden, J.J.2    Bourgarel, P.3    Meo, T.4    Betenbaugh, M.J.5
  • 5
    • 0024669783 scopus 로고
    • Auxin-binding protein located in the endoplasmic reticulum of maize shoots: Molecular cloning and complete primary structure
    • INOHARA N, SHIMOMURA S, FUKUI T, FUTAI M, 1989. Auxin-binding protein located in the endoplasmic reticulum of maize shoots: molecular cloning and complete primary structure. Proc Natl Acad Sci USA 86: 3564-3568.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3564-3568
    • Inohara, N.1    Shimomura, S.2    Fukui, T.3    Futai, M.4
  • 7
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • LAEMMLI UK, 1970. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 8
    • 0028486254 scopus 로고
    • Authentic processing and targeting of active maize auxin-binding protein in the baculovirus expression system
    • MACDONALD H, HENDERSON J, NAPIER RM, VENIS MA, HAWES C, LAZARUS CM, 1994. Authentic processing and targeting of active maize auxin-binding protein in the baculovirus expression system. Plant Physiol 105: 1049-1057.
    • (1994) Plant Physiol , vol.105 , pp. 1049-1057
    • Macdonald, H.1    Henderson, J.2    Napier, R.M.3    Venis, M.A.4    Hawes, C.5    Lazarus, C.M.6
  • 9
    • 0011193787 scopus 로고
    • Preparation and characterization of monoclonal and polyclonal antibodies to maize auxin-binding protein
    • NAPIER RM, VENIS MA, BOLTON MA, RICHARDSON LJ, BUTCHER GW, 1988. Preparation and characterization of monoclonal and polyclonal antibodies to maize auxin-binding protein. Planta 176: 519-526.
    • (1988) Planta , vol.176 , pp. 519-526
    • Napier, R.M.1    Venis, M.A.2    Bolton, M.A.3    Richardson, L.J.4    Butcher, G.W.5
  • 10
    • 0026752711 scopus 로고
    • Immunological evidence that plants use both HDEL and KDEL for targeting proteins to the endoplasmic reticulum
    • NAPIER RM, FOWKE LC, HAWES C, LEWIS M, PELHAM HRB, 1992. Immunological evidence that plants use both HDEL and KDEL for targeting proteins to the endoplasmic reticulum. J Cell Sci 102: 261-271.
    • (1992) J Cell Sci , vol.102 , pp. 261-271
    • Napier, R.M.1    Fowke, L.C.2    Hawes, C.3    Lewis, M.4    Pelham, H.R.B.5
  • 11
    • 0000810554 scopus 로고
    • Monoclonal antibodies detect an auxin-induced conformational change in the maize auxin-binding protein
    • NAPIER RM, VENIS MA, 1990. Monoclonal antibodies detect an auxin-induced conformational change in the maize auxin-binding protein. Planta 182: 313-318.
    • (1990) Planta , vol.182 , pp. 313-318
    • Napier, R.M.1    Venis, M.A.2
  • 12
    • 0029140360 scopus 로고
    • Tansley review no. 79: Auxin action and auxin-binding proteins
    • NAPIER RM, VENIS MA, 1995. Tansley review No. 79: Auxin action and auxin-binding proteins. New Phytol 129: 167-201.
    • (1995) New Phytol , vol.129 , pp. 167-201
    • Napier, R.M.1    Venis, M.A.2
  • 13
    • 0024852363 scopus 로고
    • Downstream sequences augment transcription from the essential initiation site of a baculovirus polyhedrin gene
    • OOI BG, RANKIN C, MILLER LK, 1989. Downstream sequences augment transcription from the essential initiation site of a baculovirus polyhedrin gene. J Mol Biol 210: 721-736.
    • (1989) J Mol Biol , vol.210 , pp. 721-736
    • Ooi, B.G.1    Rankin, C.2    Miller, L.K.3
  • 14
    • 0024427039 scopus 로고
    • Control of protein exit from the endoplasmic reticulum
    • PELHAM HRB, 1989. Control of protein exit from the endoplasmic reticulum. Ann Rev Cell Biol 5: 1-23.
    • (1989) Ann Rev Cell Biol , vol.5 , pp. 1-23
    • Pelham, H.R.B.1
  • 15
    • 0022761960 scopus 로고
    • Polyhedrin structure
    • ROHRMANN GF, 1986. Polyhedrin structure. J Gen Microsc 67: 1499-1513.
    • (1986) J Gen Microsc , vol.67 , pp. 1499-1513
    • Rohrmann, G.F.1
  • 16
    • 11944255947 scopus 로고
    • Evidence for the presence of two different types of protein bodies in wheat endosperm
    • RUBIN R, LEVAONY H, GALILI G, 1992. Evidence for the presence of two different types of protein bodies in wheat endosperm. Plant Physiol 99: 718-724.
    • (1992) Plant Physiol , vol.99 , pp. 718-724
    • Rubin, R.1    Levaony, H.2    Galili, G.3
  • 17
    • 0028100171 scopus 로고
    • Retention and retrieval: Both mechanisms cooperate to maintain calreticulin in the endoplasmic reticulum
    • SONNICHSEN B, FULLEKRUG J, NGUYEN VAN P, DIEKMANN W, ROBINSON DG, MIESKES G, 1994. Retention and retrieval: both mechanisms cooperate to maintain calreticulin in the endoplasmic reticulum. J Cell Sci 107: 2705-2717.
    • (1994) J Cell Sci , vol.107 , pp. 2705-2717
    • Sonnichsen, B.1    Fullekrug, J.2    Van Nguyen, P.3    Diekmann, W.4    Robinson, D.G.5    Mieskes, G.6
  • 18
    • 0014444144 scopus 로고
    • A low-viscosity epoxy resin embedding medium for electron microscopy
    • SPURR AR, 1969. A low-viscosity epoxy resin embedding medium for electron microscopy. J Ultrastruct Res 26: 31-43.
    • (1969) J Ultrastruct Res , vol.26 , pp. 31-43
    • Spurr, A.R.1
  • 19
    • 0025866855 scopus 로고
    • Regulating the retention of T-cell receptor alpha-chain variants within the endoplasmic reticulum-calcium-dependent association with BiP
    • SUZUKI CK, BONIFACINO JS, LIN AY, DAVIS MM, KLAUSNER RD, 1991. Regulating the retention of T-cell receptor alpha-chain variants within the endoplasmic reticulum-calcium-dependent association with BiP. J Cell Biol 114: 189-205.
    • (1991) J Cell Biol , vol.114 , pp. 189-205
    • Suzuki, C.K.1    Bonifacino, J.S.2    Lin, A.Y.3    Davis, M.M.4    Klausner, R.D.5
  • 21
    • 0002477090 scopus 로고
    • Immunogold labelling
    • Hall JL, Hawes CR, eds. Academic Press Ltd, London
    • VANDENBOSCH KA, 1991. Immunogold labelling. In: Hall JL, Hawes CR, eds. Electron Microscopy of Plant Cells. Academic Press Ltd, London, 181-218.
    • (1991) Electron Microscopy of Plant Cells , pp. 181-218
    • Vandenbosch, K.A.1
  • 22
    • 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. J Exp Bot 44: 1417-1444.
    • (1993) J Exp Bot , vol.44 , pp. 1417-1444
    • Vitale, A.1    Ceriotti, A.2    Denecke, J.3
  • 23
    • 0023986560 scopus 로고
    • Functional studies on the p10 gene of Autographa californica nuclear polyhedrosis virus using a recombinant expressing a p10-β-galactosidase fusion gene
    • VLAK JM, KLINKENBERG FA, ZAAL KJM, et al., 1988. Functional studies on the p10 gene of Autographa californica nuclear polyhedrosis virus using a recombinant expressing a p10-β-galactosidase fusion gene. J Gen Virol 69: 765-776.
    • (1988) J Gen Virol , vol.69 , pp. 765-776
    • Vlak, J.M.1    Klinkenberg, F.A.2    Zaal, K.J.M.3
  • 24
    • 0000758647 scopus 로고
    • Transformation of anterior midgut and hepatopancreas cells by monodon baculovirus (MBV) in Penaeus monodon post larvae
    • VOGT G, 1992. Transformation of anterior midgut and hepatopancreas cells by monodon baculovirus (MBV) in Penaeus monodon post larvae. Aquaculture 107: 239-248.
    • (1992) Aquaculture , vol.107 , pp. 239-248
    • Vogt, G.1
  • 25
    • 0026672695 scopus 로고
    • Site-directed mutagenesis of human protein disulfide isomerase - Effect on the assembly, activity and endoplasmic reticulum retention of human prolyl 4-hydroxylase in Spodoptera frugiperda insect cells
    • VUORI K, PIHLAJANIEMI T, MYLLYLA R, KIVIRIKKO KI, 1992. Site-directed mutagenesis of human protein disulfide isomerase - effect on the assembly, activity and endoplasmic reticulum retention of human prolyl 4-hydroxylase in Spodoptera frugiperda insect cells. EMBO J 11: 4213-4217.
    • (1992) EMBO J , vol.11 , pp. 4213-4217
    • Vuori, K.1    Pihlajaniemi, T.2    Myllyla, R.3    Kivirikko, K.I.4
  • 26
    • 0026834063 scopus 로고
    • Vicilin with carboxy-terminal KDEL is retained in the endoplasmic reticulum and accumulates to high levels in the leaves of transgenic plants
    • WANDELT CI, KHAN MRI, CRAIG S, SCHROEDER HE, SPENCER D, HIGGINS TJV, 1992. Vicilin with carboxy-terminal KDEL is retained in the endoplasmic reticulum and accumulates to high levels in the leaves of transgenic plants. Plant J 2: 181-192.
    • (1992) Plant J , vol.2 , pp. 181-192
    • Wandelt, C.I.1    Khan, M.R.I.2    Craig, S.3    Schroeder, H.E.4    Spencer, D.5    Higgins, T.J.V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.