메뉴 건너뛰기




Volumn 11, Issue 4, 1999, Pages 615-628

The endoplasmic reticulum - Gateway of the secretory pathway

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0032725633     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.11.4.615     Document Type: Article
Times cited : (243)

References (98)
  • 1
    • 0024978457 scopus 로고
    • Nucleotide sequence of cDNA for sulfhydryl-endopeptidase (SH-EP) from cotyledons of germinating Vigna mungo seeds
    • Akasofu, H., Yamauchi, D., Mitsuhashi, W., and Minamikawa, T. (1989). Nucleotide sequence of cDNA for sulfhydryl-endopeptidase (SH-EP) from cotyledons of germinating Vigna mungo seeds. Nucleic Acids Res. 17, 6733.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6733
    • Akasofu, H.1    Yamauchi, D.2    Mitsuhashi, W.3    Minamikawa, T.4
  • 2
    • 0031420939 scopus 로고    scopus 로고
    • Coexpression of the maize δ-zein and β-zein genes results in stable accumulation of δ-zein in endoplasmic reticulum-derived protein bodies formed by β-zein
    • Bagga, S., Adams, H.P., Rodriguez, F.D., Kemp, J.D., and Sengupta-Gopalan, C. (1997). Coexpression of the maize δ-zein and β-zein genes results in stable accumulation of δ-zein in endoplasmic reticulum-derived protein bodies formed by β-zein. Plant Cell 9, 1683-1696.
    • (1997) Plant Cell , vol.9 , pp. 1683-1696
    • Bagga, S.1    Adams, H.P.2    Rodriguez, F.D.3    Kemp, J.D.4    Sengupta-Gopalan, C.5
  • 3
    • 23444432144 scopus 로고
    • Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum
    • Balch, W.E., McCaffery, J.M., Plutner, H., and Farquhar, M.G. (1994). Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum. Cell 76, 841-852.
    • (1994) Cell , vol.76 , pp. 841-852
    • Balch, W.E.1    McCaffery, J.M.2    Plutner, H.3    Farquhar, M.G.4
  • 5
    • 0028837102 scopus 로고
    • Expression and regulation of aERD2, a gene encoding the KDEL receptor homolog in plants, and other genes encoding proteins involved in ER-Golgi vesicular trafficking
    • Bar-Peled, M., da Silva Conçeicão, A., Frigerio, L., and Raikhel, N.V. (1995). Expression and regulation of aERD2, a gene encoding the KDEL receptor homolog in plants, and other genes encoding proteins involved in ER-Golgi vesicular trafficking. Plant Cell 7, 667-676.
    • (1995) Plant Cell , vol.7 , pp. 667-676
    • Bar-Peled, M.1    Da Silva Conçeicão, A.2    Frigerio, L.3    Raikhel, N.V.4
  • 7
    • 0025574861 scopus 로고
    • A carboxy-terminal propeptide is necessary for proper sorting of barley lectin to vacuoles of tobacco
    • Bednarek, S.Y., Wilkins, T.A., Dombrowski, J.E., and Raikhel, N.V. (1990). A carboxy-terminal propeptide is necessary for proper sorting of barley lectin to vacuoles of tobacco. Plant Cell 2, 1145-1155.
    • (1990) Plant Cell , vol.2 , pp. 1145-1155
    • Bednarek, S.Y.1    Wilkins, T.A.2    Dombrowski, J.E.3    Raikhel, N.V.4
  • 8
    • 0030500417 scopus 로고    scopus 로고
    • Virus-mediated delivery of the green fluorescent protein to the endoplasmic reticulum of plant cells
    • Boevink, P., Santa Cruz, S., Hawes, C., Harris, N., and Oparka, K.J. (1996). Virus-mediated delivery of the green fluorescent protein to the endoplasmic reticulum of plant cells. Plant J. 10, 935-941.
    • (1996) Plant J. , vol.10 , pp. 935-941
    • Boevink, P.1    Santa Cruz, S.2    Hawes, C.3    Harris, N.4    Oparka, K.J.5
  • 9
    • 0032144201 scopus 로고    scopus 로고
    • Stacks on tracks: The plant Golgi apparatus traffics on an actin/ER network
    • Boevink, P., Oparka, K., Santa Cruz, S., Martin, B., Betteridge, A., and Hawes, C. (1998). Stacks on tracks: The plant Golgi apparatus traffics on an actin/ER network. Plant J. 15, 441-447.
    • (1998) Plant J. , vol.15 , pp. 441-447
    • Boevink, P.1    Oparka, K.2    Santa Cruz, S.3    Martin, B.4    Betteridge, A.5    Hawes, C.6
  • 10
    • 0026150603 scopus 로고
    • Increased expression of the maize immunoglobulin binding protein homolog b-70 in three zein regulatory mutants
    • Boston, R.S., Fontes, E.B.P., Shank, B.B., and Wrobel, R.L. (1991). Increased expression of the maize immunoglobulin binding protein homolog b-70 in three zein regulatory mutants. Plant Cell 3, 497-505.
    • (1991) Plant Cell , vol.3 , pp. 497-505
    • Boston, R.S.1    Fontes, E.B.P.2    Shank, B.B.3    Wrobel, R.L.4
  • 11
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • Boston, R.S., Viitanen, P.V., and Vierling, E. (1996). Molecular chaperones and protein folding in plants. Plant Mol. Biol. 32, 191-222.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 191-222
    • Boston, R.S.1    Viitanen, P.V.2    Vierling, E.3
  • 12
    • 0026508087 scopus 로고
    • Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum
    • Braakman, I., Helenius, J., and Helenius, A. (1992). Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature 356, 260-262.
    • (1992) Nature , vol.356 , pp. 260-262
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 13
    • 0020132174 scopus 로고
    • Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons
    • Chrispeels, M.J., Higgins, T.J.V., and Spencer, D. (1982). Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons. J. Cell Biol. 93, 306-313.
    • (1982) J. Cell Biol. , vol.93 , pp. 306-313
    • Chrispeels, M.J.1    Higgins, T.J.V.2    Spencer, D.3
  • 15
    • 0030339563 scopus 로고    scopus 로고
    • The maize γ-zein sequeters α-zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm
    • Coleman, C.E., Herman, E.M., Takasaki, K., and Larkins, B.A. (1996). The maize γ-zein sequeters α-zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm. Plant Cell 8, 2335-2345.
    • (1996) Plant Cell , vol.8 , pp. 2335-2345
    • Coleman, C.E.1    Herman, E.M.2    Takasaki, K.3    Larkins, B.A.4
  • 17
    • 0028181745 scopus 로고
    • Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
    • Cosson, P., and Letourneur, F. (1994). Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science 263, 1629-1631.
    • (1994) Science , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 18
    • 0031774263 scopus 로고    scopus 로고
    • BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress
    • Crofts, A.J., Leborgne-Castel, N., Pesca, M., Vitale, A., and Denecke, J. (1998). BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress. Plant Cell 10, 813-823.
    • (1998) Plant Cell , vol.10 , pp. 813-823
    • Crofts, A.J.1    Leborgne-Castel, N.2    Pesca, M.3    Vitale, A.4    Denecke, J.5
  • 19
    • 0027162564 scopus 로고
    • The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation
    • Crowley, K.S., Reinhart, G.D., and Johnson, A.E. (1993). The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation. Cell 73, 1101-1115.
    • (1993) Cell , vol.73 , pp. 1101-1115
    • Crowley, K.S.1    Reinhart, G.D.2    Johnson, A.E.3
  • 20
    • 0024982237 scopus 로고
    • Protein secretion in plant cells can occur via a default pathway
    • Denecke, J., Botterman, J., and Deblaere, R. (1990). Protein secretion in plant cells can occur via a default pathway. Plant Cell 2, 51-59.
    • (1990) Plant Cell , vol.2 , pp. 51-59
    • Denecke, J.1    Botterman, J.2    Deblaere, R.3
  • 21
    • 0026523624 scopus 로고
    • Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope
    • Denecke, J., Derycke, R., and Botterman, J. (1992). Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope. EMBO J. 11, 2345-2355.
    • (1992) EMBO J. , vol.11 , pp. 2345-2355
    • Denecke, J.1    Derycke, R.2    Botterman, J.3
  • 23
    • 0026670522 scopus 로고
    • Fission yeast and a plant have functional homologues of the Sari and Sec12 proteins involved in ER to Golgi traffic in budding yeast
    • d'Enfert, C., Gensse, M., and Gaillardin, C. (1992). Fission yeast and a plant have functional homologues of the Sari and Sec12 proteins involved in ER to Golgi traffic in budding yeast. EMBO J. 11, 4205-4211.
    • (1992) EMBO J. , vol.11 , pp. 4205-4211
    • D'Enfert, C.1    Gensse, M.2    Gaillardin, C.3
  • 24
    • 0000503283 scopus 로고
    • Self-assembly of proglycinin and hybrid proglycinin synthesized in vitro from cDNA
    • Dickinson, C.D., Floener, L.A., Lilley, G.G., and Nielsen, N.C. (1987). Self-assembly of proglycinin and hybrid proglycinin synthesized in vitro from cDNA. Proc. Natl. Acad. Sci. USA 84, 5525-5529.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5525-5529
    • Dickinson, C.D.1    Floener, L.A.2    Lilley, G.G.3    Nielsen, N.C.4
  • 25
    • 0029053448 scopus 로고
    • The role of N-glycans in the secretory pathway
    • Fiedler, K., and Simons, K. (1995). The role of N-glycans in the secretory pathway. Cell 81, 309-312.
    • (1995) Cell , vol.81 , pp. 309-312
    • Fiedler, K.1    Simons, K.2
  • 26
    • 0031829027 scopus 로고    scopus 로고
    • The enemy within: Ricin and plant cells
    • Frigerio, L., and Roberts, L.M. (1998). The enemy within: Ricin and plant cells. J. Exp. Bot. 49, 1473-1480.
    • (1998) J. Exp. Bot. , vol.49 , pp. 1473-1480
    • Frigerio, L.1    Roberts, L.M.2
  • 27
    • 0032100925 scopus 로고    scopus 로고
    • Sorting of phaseolin to the vacuole is saturable and requires a short C-terminal peptide
    • Frigerio, L., de Virgilio, M., Prada, A., Faoro, F., and Vitale, A. (1998a). Sorting of phaseolin to the vacuole is saturable and requires a short C-terminal peptide. Plant Cell 10, 1031-1042.
    • (1998) Plant Cell , vol.10 , pp. 1031-1042
    • Frigerio, L.1    De Virgilio, M.2    Prada, A.3    Faoro, F.4    Vitale, A.5
  • 28
    • 0032486270 scopus 로고    scopus 로고
    • Free ricin a chain, proricin, and native toxin have different cellular fates when expressed in tobacco protoplasts
    • Frigerio, L., Vitale, A., Lord, M.J., Ceriotti, A., and Roberts, L.M. (1998b). Free ricin A chain, proricin, and native toxin have different cellular fates when expressed in tobacco protoplasts. J. Biol. Chem. 273, 14194-14199.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14194-14199
    • Frigerio, L.1    Vitale, A.2    Lord, M.J.3    Ceriotti, A.4    Roberts, L.M.5
  • 29
    • 0031131581 scopus 로고    scopus 로고
    • A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane
    • Gillikin, J.W., Zhang, F., Coleman, C.E., Bass, H.W., Larkins, B.A., and Boston, R.S. (1997). A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane. Plant Physiol. 114, 345-352.
    • (1997) Plant Physiol. , vol.114 , pp. 345-352
    • Gillikin, J.W.1    Zhang, F.2    Coleman, C.E.3    Bass, H.W.4    Larkins, B.A.5    Boston, R.S.6
  • 30
    • 0001069047 scopus 로고
    • Tonoplast and soluble vacuolar proteins are targeted by different mechanisms
    • Gomez, L., and Chrispeels, M.J. (1993). Tonoplast and soluble vacuolar proteins are targeted by different mechanisms. Plant Cell 5, 1113-1124.
    • (1993) Plant Cell , vol.5 , pp. 1113-1124
    • Gomez, L.1    Chrispeels, M.J.2
  • 31
    • 0021076098 scopus 로고
    • Immunoglubulin heavy chain binding protein
    • Haas, I.G., and Wabl, M. (1983). Immunoglubulin heavy chain binding protein. Nature 306, 387-389.
    • (1983) Nature , vol.306 , pp. 387-389
    • Haas, I.G.1    Wabl, M.2
  • 32
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman, B.D., Hendershot, L.M., and Johnson, A.E. (1998). BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 92, 747-758.
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 33
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway: Retention of a misfolded viral membrane glycoprotein involves cycling between the ER, the intermediate compartment, and the Golgi apparatus
    • Hammond, C., and Helenius, A. (1994). Quality control in the secretory pathway: Retention of a misfolded viral membrane glycoprotein involves cycling between the ER, the intermediate compartment, and the Golgi apparatus. J. Cell Biol. 126, 41-52.
    • (1994) J. Cell Biol. , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 34
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C., and Helenius, A. (1995). Quality control in the secretory pathway. Curr. Opin. Cell Biol. 7, 523-529.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 35
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond, C., Braakman, I., and Helenius, A. (1994). Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. USA 91, 913-917.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 36
    • 0031795695 scopus 로고    scopus 로고
    • Transport of storage proteins to protein storage vacuoles is mediated by large precursor-accumulating vesicles
    • Hara-Nishimura, I., Shimada, T., Hatano, K., Takeuchi, Y., and Nishimura, M. (1998). Transport of storage proteins to protein storage vacuoles is mediated by large precursor-accumulating vesicles. Plant Cell 10, 825-836.
    • (1998) Plant Cell , vol.10 , pp. 825-836
    • Hara-Nishimura, I.1    Shimada, T.2    Hatano, K.3    Takeuchi, Y.4    Nishimura, M.5
  • 37
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 39
    • 0033545187 scopus 로고    scopus 로고
    • The in vivo association with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP
    • Hellman, R., Vanhove, M., Lejeune, A., Stevens, F.J., and Hendershot, L.M. (1999). The in vivo association with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP. J. Cell Biol. 144, 21-30.
    • (1999) J. Cell Biol. , vol.144 , pp. 21-30
    • Hellman, R.1    Vanhove, M.2    Lejeune, A.3    Stevens, F.J.4    Hendershot, L.M.5
  • 40
    • 0030787889 scopus 로고    scopus 로고
    • Retention of auxin-binding protein in the endoplasmic reticulum: Quantifying escape and the role of auxin
    • Henderson, J., Bauly, J.M., Ashford, D.A., Oliver, S.C., Hawes, C.R., Lazarus, C.M., Venis, M.A., and Napier, R.M. (1997). Retention of auxin-binding protein in the endoplasmic reticulum: Quantifying escape and the role of auxin. Planta 202, 313-323.
    • (1997) Planta , vol.202 , pp. 313-323
    • Henderson, J.1    Bauly, J.M.2    Ashford, D.A.3    Oliver, S.C.4    Hawes, C.R.5    Lazarus, C.M.6    Venis, M.A.7    Napier, R.M.8
  • 41
    • 0032718660 scopus 로고    scopus 로고
    • Protein storage bodies and vacuoles
    • Herman, E.M., and Larkins, B.A. (1999). Protein storage bodies and vacuoles. Plant Cell 11, 601-613.
    • (1999) Plant Cell , vol.11 , pp. 601-613
    • Herman, E.M.1    Larkins, B.A.2
  • 42
    • 0001286278 scopus 로고
    • Retention of phytohemagglutinin with carboxyterminal tetrapeptide KDEL in the nuclear envelope and the endoplasmic reticulum
    • Herman, E.M., Tague, B.W., Hoffman, L.M., Kjemtrup, S.E., and Chrispeels, M.J. (1990). Retention of phytohemagglutinin with carboxyterminal tetrapeptide KDEL in the nuclear envelope and the endoplasmic reticulum. Planta 182, 305-312.
    • (1990) Planta , vol.182 , pp. 305-312
    • Herman, E.M.1    Tague, B.W.2    Hoffman, L.M.3    Kjemtrup, S.E.4    Chrispeels, M.J.5
  • 43
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller, M.M., Finger, A., Schweiger, M., and Wolf, D.H. (1996). ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273, 1725-1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 44
    • 0032511128 scopus 로고    scopus 로고
    • Different degradation pathways for heterologous glycoproteins in yeast
    • Holkeri, H., and Makarow, M. (1998). Different degradation pathways for heterologous glycoproteins in yeast. FEBS Lett. 429, 162-166.
    • (1998) FEBS Lett. , vol.429 , pp. 162-166
    • Holkeri, H.1    Makarow, M.2
  • 45
    • 0029829005 scopus 로고    scopus 로고
    • A pathway for targeting soluble misfolded proteins to the yeast vacuole
    • Hong, E., Davidson, A.R., and Kaiser, C.A. (1996). A pathway for targeting soluble misfolded proteins to the yeast vacuole. J. Cell Biol. 135, 623-633.
    • (1996) J. Cell Biol. , vol.135 , pp. 623-633
    • Hong, E.1    Davidson, A.R.2    Kaiser, C.A.3
  • 46
    • 0002574503 scopus 로고
    • The signal peptide of a vacuolar protein is necessary and sufficient for the efficient secretion of a cytosolic protein
    • Hunt, D.C., and Chrispeels, M.J. (1991). The signal peptide of a vacuolar protein is necessary and sufficient for the efficient secretion of a cytosolic protein. Plant Physiol. 96, 18-25.
    • (1991) Plant Physiol. , vol.96 , pp. 18-25
    • Hunt, D.C.1    Chrispeels, M.J.2
  • 47
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley, S.M., and Helenius, A. (1989). Protein oligomerization in the endoplasmic reticulum. Annu. Rev. Cell Biol. 5, 277-307.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 48
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C., Sinskey, A.J., and Lodish, H.F. (1992). Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257, 1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 49
    • 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., and 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
  • 50
    • 0032583163 scopus 로고    scopus 로고
    • Integral membrane protein sorting to vacuoles in plant cells: Evidence for two pathways
    • Jiang, L., and Rogers, J.C. (1998). Integral membrane protein sorting to vacuoles in plant cells: Evidence for two pathways. J. Cell Biol. 143, 1183-1199.
    • (1998) J. Cell Biol. , vol.143 , pp. 1183-1199
    • Jiang, L.1    Rogers, J.C.2
  • 51
    • 0031278114 scopus 로고    scopus 로고
    • Role of the sulfhydryl redox state and disulfide bonds in processing and assembly of 11S seed globulins
    • Jung, R., Nam, Y.-W., Beaman, T.W., Saalbach, I., Müntz, K., and Nielsen, N.C. (1997). Role of the sulfhydryl redox state and disulfide bonds in processing and assembly of 11S seed globulins. Plant Cell 9, 2037-2050.
    • (1997) Plant Cell , vol.9 , pp. 2037-2050
    • Jung, R.1    Nam, Y.-W.2    Beaman, T.W.3    Saalbach, I.4    Müntz, K.5    Nielsen, N.C.6
  • 52
    • 0028815044 scopus 로고
    • Accumulation and proteolytic processing of vicilin deletion-mutant proteins in the leaf and seed of transgenic tobacco
    • Kermode, A.R., Fisher, S.A., Polishchuk, E., Wandelt, C., Spencer, D., and Higgins, T.J.V. (1995). Accumulation and proteolytic processing of vicilin deletion-mutant proteins in the leaf and seed of transgenic tobacco. Planta 197, 501-513.
    • (1995) Planta , vol.197 , pp. 501-513
    • Kermode, A.R.1    Fisher, S.A.2    Polishchuk, E.3    Wandelt, C.4    Spencer, D.5    Higgins, T.J.V.6
  • 55
    • 0026478698 scopus 로고
    • Evidence for a novel route of wheat storage proteins to vacuoles
    • Levanony, H., Rubin, R., Altshuler, Y., and Galili, G. (1992). Evidence for a novel route of wheat storage proteins to vacuoles. J. Cell Biol. 119, 1117-1128.
    • (1992) J. Cell Biol. , vol.119 , pp. 1117-1128
    • Levanony, H.1    Rubin, R.2    Altshuler, Y.3    Galili, G.4
  • 56
    • 0026604647 scopus 로고
    • Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum
    • Lewis, M.J., and Pelham, H.R.B. (1992). Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum. Cell 68, 353-364.
    • (1992) Cell , vol.68 , pp. 353-364
    • Lewis, M.J.1    Pelham, H.R.B.2
  • 57
    • 0030099075 scopus 로고    scopus 로고
    • Expression of protein disulfide isomerase is elevated in the endosperm of the maize floury-2 mutant
    • Li, C.P., and Larkins, B.A. (1996). Expression of protein disulfide isomerase is elevated in the endosperm of the maize floury-2 mutant. Plant Mol. Biol. 30, 873-882
    • (1996) Plant Mol. Biol. , vol.30 , pp. 873-882
    • Li, C.P.1    Larkins, B.A.2
  • 60
    • 0023749075 scopus 로고
    • Degradation from the endoplasmic reticulum: Disposing of newly synthesized proteins
    • Lippincott-Schwartz, J., Bonifacino, J.S., Yuan, L.C., and Klausner, R.D. (1988). Degradation from the endoplasmic reticulum: Disposing of newly synthesized proteins. Cell 54, 209-220.
    • (1988) Cell , vol.54 , pp. 209-220
    • Lippincott-Schwartz, J.1    Bonifacino, J.S.2    Yuan, L.C.3    Klausner, R.D.4
  • 61
    • 0030900410 scopus 로고    scopus 로고
    • The rate of phaseolin assembly is controlled by the glucosylation state of its N-linked oligosaocharide chains
    • Lupattelli, F., Pedrazzini, E., Bollini, R., Vitale, A., and Ceriotti, A. (1997). The rate of phaseolin assembly is controlled by the glucosylation state of its N-linked oligosaocharide chains. Plant Cell 9, 597-609.
    • (1997) Plant Cell , vol.9 , pp. 597-609
    • Lupattelli, F.1    Pedrazzini, E.2    Bollini, R.3    Vitale, A.4    Ceriotti, A.5
  • 63
    • 0031835622 scopus 로고    scopus 로고
    • Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans
    • Ma, J.K.-C., Hikmat, B.Y., Wycoff, K., Vine, N.D., Chargelegue, D., Yu, L., Hein, M.B., and Lehner, T. (1998). Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans. Nature Med. 4, 601-606.
    • (1998) Nature Med. , vol.4 , pp. 601-606
    • Ma, J.K.-C.1    Hikmat, B.Y.2    Wycoff, K.3    Vine, N.D.4    Chargelegue, D.5    Yu, L.6    Hein, M.B.7    Lehner, T.8
  • 64
    • 0032718565 scopus 로고    scopus 로고
    • Plant vacuoles
    • Marty, F. (1999). Plant vacuoles. Plant Cell 11, 587-599.
    • (1999) Plant Cell , vol.11 , pp. 587-599
    • Marty, F.1
  • 65
    • 0012682080 scopus 로고
    • The endomembrane concept: A functional integration of endoplasmic reticulum and Golgi apparatus
    • A.W. Robards, ed (London: McGraw-Hill)
    • Morré, D.J., and Mollenhauer, H.H. (1974). The endomembrane concept: A functional integration of endoplasmic reticulum and Golgi apparatus. In Dynamic Aspects of Plant Ultrastructure, A.W. Robards, ed (London: McGraw-Hill), pp. 64-137.
    • (1974) Dynamic Aspects of Plant Ultrastructure , pp. 64-137
    • Morré, D.J.1    Mollenhauer, H.H.2
  • 66
    • 0031115545 scopus 로고    scopus 로고
    • Molecular cloning, expression and subcellular localization of a BiP homolog from rice endosperm tissue
    • Muench, D.G., Wu, Y., Zhang, Y., Li, X., Boston, R.S., and Okita, T.W. (1997). Molecular cloning, expression and subcellular localization of a BiP homolog from rice endosperm tissue. Plant Cell Physiol. 38, 404-412.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 404-412
    • Muench, D.G.1    Wu, Y.2    Zhang, Y.3    Li, X.4    Boston, R.S.5    Okita, T.W.6
  • 67
    • 0023052239 scopus 로고
    • An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobilin heavy chain binding protein
    • Munro, S., and Pelham, H.R.B. (1986). An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobilin heavy chain binding protein. Cell 46, 291-300.
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.R.B.2
  • 68
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro, S., and Pelham, H.R.B. (1987). A C-terminal signal prevents secretion of luminal ER proteins. Cell 48, 899-907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.B.2
  • 69
    • 0031403738 scopus 로고    scopus 로고
    • Adenosine 5′-triphosphate is required for the assembly of 11S seed proglobulins in vitro
    • Nam, Y.-W., Jung, R., and Nielsen, N.C. (1997). Adenosine 5′-triphosphate is required for the assembly of 11S seed proglobulins in vitro. Plant Physiol. 115, 1629-1639.
    • (1997) Plant Physiol. , vol.115 , pp. 1629-1639
    • Nam, Y.-W.1    Jung, R.2    Nielsen, N.C.3
  • 70
    • 0028002143 scopus 로고
    • Mutation analysis of the C-terminal vacuolar targeting peptide of tobacco chitinase: Low specificity of the sorting system, and gradual transition between intracellular retention and secretion into the extracellular space
    • Neuhaus, J.-M., Pietrzak, M., and Boller, T. (1994). Mutation analysis of the C-terminal vacuolar targeting peptide of tobacco chitinase: Low specificity of the sorting system, and gradual transition between intracellular retention and secretion into the extracellular space. Plant J. 5, 45-54.
    • (1994) Plant J. , vol.5 , pp. 45-54
    • Neuhaus, J.-M.1    Pietrzak, M.2    Boller, T.3
  • 71
    • 0030812940 scopus 로고    scopus 로고
    • A di-acidic signal required for selective export from the endoplasmic reticulum
    • Nishimura, N., and Balch, W.E. (1997). A di-acidic signal required for selective export from the endoplasmic reticulum. Science 277, 556-558.
    • (1997) Science , vol.277 , pp. 556-558
    • Nishimura, N.1    Balch, W.E.2
  • 72
    • 0028041312 scopus 로고
    • Posttranslational processing of a carboxy-terminal propeptide containing a KDEL sequence of plant vacuolar cysteine endopeptidase (SH-EP)
    • Okomoto, T., Nakayama, H., Seta, K., Isobe, T., and Minamikawa, T. (1994). Posttranslational processing of a carboxy-terminal propeptide containing a KDEL sequence of plant vacuolar cysteine endopeptidase (SH-EP). FEBS Lett. 351, 31-34.
    • (1994) FEBS Lett. , vol.351 , pp. 31-34
    • Okomoto, T.1    Nakayama, H.2    Seta, K.3    Isobe, T.4    Minamikawa, T.5
  • 73
    • 0033574441 scopus 로고    scopus 로고
    • Posttranslational removal of the carboxyterminal KDEL of the cysteine protease SH-EP occurs prior to maturation of the enzyme
    • in press
    • Okomoto, T., Minamikawa, T., Edwards, G., Vakharia, V., and Herman, E. (1999). Posttranslational removal of the carboxyterminal KDEL of the cysteine protease SH-EP occurs prior to maturation of the enzyme. J. Biol. Chem., in press.
    • (1999) J. Biol. Chem.
    • Okomoto, T.1    Minamikawa, T.2    Edwards, G.3    Vakharia, V.4    Herman, E.5
  • 74
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade, G. (1975). Intracellular aspects of the process of protein synthesis. Science 189, 347-358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 76
    • 0028123665 scopus 로고
    • Novel inhibitory action of tunicamycin homologues suggests a role for dynamic protein fatty acylation in growth cone-mediated neurite extension
    • Patterson, S.I., and Pate Skene, J.H. (1994). Novel inhibitory action of tunicamycin homologues suggests a role for dynamic protein fatty acylation in growth cone-mediated neurite extension. J. Cell Biol. 124, 521-536.
    • (1994) J. Cell Biol. , vol.124 , pp. 521-536
    • Patterson, S.I.1    Pate Skene, J.H.2
  • 77
    • 0030038133 scopus 로고    scopus 로고
    • The binding protein (BiP) and the synthesis of secretory proteins
    • Pedrazzini, E., and Vitale, A. (1996). The binding protein (BiP) and the synthesis of secretory proteins. Plant Physiol. Biochem. 34, 207-216.
    • (1996) Plant Physiol. Biochem. , vol.34 , pp. 207-216
    • Pedrazzini, E.1    Vitale, A.2
  • 79
    • 0023988955 scopus 로고
    • Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment
    • Pelham, H.R.B. (1988). Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment. EMBO J. 7, 913-918.
    • (1988) EMBO J. , vol.7 , pp. 913-918
    • Pelham, H.R.B.1
  • 80
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper, R.K., Böhmler, S., Bordallo, J., Sommer, T., and Wolf, D.H. (1997). Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388, 891-895.
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Böhmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 81
    • 0028894404 scopus 로고
    • Degradation of transport-competent destabilized phaseolin with a signal for retention in the endoplasmic reticulum occurs in the vacuole
    • Pueyo, J.J., Chrispeels, M.J., and Herman, E.M. (1995). Degradation of transport-competent destabilized phaseolin with a signal for retention in the endoplasmic reticulum occurs in the vacuole. Planta 196, 586-596.
    • (1995) Planta , vol.196 , pp. 586-596
    • Pueyo, J.J.1    Chrispeels, M.J.2    Herman, E.M.3
  • 82
    • 0000367861 scopus 로고
    • One vacuole or two vacuoles: Do protein storage vacuoles arise de novo during pea cotyledon development? J
    • Robinson, D.G., Hoh, B., Hinz, G., and Jeong, B.-K. (1995). One vacuole or two vacuoles: Do protein storage vacuoles arise de novo during pea cotyledon development? J. Plant Physiol. 145, 654-664.
    • (1995) Plant Physiol. , vol.145 , pp. 654-664
    • Robinson, D.G.1    Hoh, B.2    Hinz, G.3    Jeong, B.-K.4
  • 83
    • 11944255947 scopus 로고
    • Evidence for the presence of two different types of protein bodies in wheat endosperm
    • Rubin, R., Levanony, H., and 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    Levanony, H.2    Galili, G.3
  • 84
    • 0033117122 scopus 로고    scopus 로고
    • The specificity of vesicle trafficking: Coat proteins and SNAREs
    • Sanderfoot, A.A., and Raikhel, N.V. (1999). The specificity of vesicle trafficking: Coat proteins and SNAREs. Plant Cell 11, 629-641.
    • (1999) Plant Cell , vol.11 , pp. 629-641
    • Sanderfoot, A.A.1    Raikhel, N.V.2
  • 85
    • 0029744854 scopus 로고    scopus 로고
    • Intramolecular disulfide bonds between conserved cysteines in wheat gliadins control their deposition into protein bodies
    • Shimoni, Y., and Galili, G. (1996). Intramolecular disulfide bonds between conserved cysteines in wheat gliadins control their deposition into protein bodies. J. Biol. Chem. 271, 18869-18874.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18869-18874
    • Shimoni, Y.1    Galili, G.2
  • 86
    • 0031879861 scopus 로고    scopus 로고
    • Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments
    • Shusta, E.V., Raines, R.T., Plückthun, A., and Wittrup, K.D. (1998). Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments. Nature Biotech. 16, 773-777.
    • (1998) Nature Biotech. , vol.16 , pp. 773-777
    • Shusta, E.V.1    Raines, R.T.2    Plückthun, A.3    Wittrup, K.D.4
  • 87
    • 0032539619 scopus 로고    scopus 로고
    • The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP
    • Skowronek, M.H., Hendershot, L.M., and Haas, I.G. (1998). The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP. Proc. Natl. Acad. Sci. USA 95, 1574-1578.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1574-1578
    • Skowronek, M.H.1    Hendershot, L.M.2    Haas, I.G.3
  • 88
    • 0031170901 scopus 로고    scopus 로고
    • The plant ER: A dynamic organelle composed of a large number of discrete functional domains
    • Staehelin, L.A. (1997). The plant ER: A dynamic organelle composed of a large number of discrete functional domains. Plant J. 11, 1151-1165.
    • (1997) Plant J. , vol.11 , pp. 1151-1165
    • Staehelin, L.A.1
  • 89
    • 0032718566 scopus 로고    scopus 로고
    • +-pumping ATPases: Regulation and biosynthesis
    • +-pumping ATPases: Regulation and biosynthesis. Plant Cell 11, 677-689.
    • (1999) Plant Cell , vol.11 , pp. 677-689
    • Sze, H.1    Li, X.2    Palmgren, M.G.3
  • 90
    • 0031045007 scopus 로고    scopus 로고
    • Interactions between newly-synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum
    • Tatu, U., and Helenius, A. (1997). Interactions between newly-synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J. Cell Biol. 136, 555-565.
    • (1997) J. Cell Biol. , vol.136 , pp. 555-565
    • Tatu, U.1    Helenius, A.2
  • 91
    • 0027326627 scopus 로고
    • Mutational analysis of the human KDEL receptor: Distinct structural requirements for Golgi retention, ligand binding and retrograde transport
    • Townsley, F.M., Wilson, D.W., and Pelham, H.R.B. (1993). Mutational analysis of the human KDEL receptor: Distinct structural requirements for Golgi retention, ligand binding and retrograde transport. EMBO J. 12, 2821-2829.
    • (1993) EMBO J. , vol.12 , pp. 2821-2829
    • Townsley, F.M.1    Wilson, D.W.2    Pelham, H.R.B.3
  • 92
    • 0023652379 scopus 로고
    • Protein sorting in yeast: The localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide
    • Valls, L.A., Hunter, C.P., Rothman, J.H., and Stevens, T.H. (1987). Protein sorting in yeast: The localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide. Cell 48, 887-897.
    • (1987) Cell , vol.48 , pp. 887-897
    • Valls, L.A.1    Hunter, C.P.2    Rothman, J.H.3    Stevens, T.H.4
  • 93
    • 0001143106 scopus 로고
    • The role of the endoplasmic reticulum in protein synthesis, modification and intracellular transport
    • Vitale, A., Ceriotti, A., and 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
  • 94
    • 0029167492 scopus 로고
    • The binding protein associates with monomeric phaseolin
    • Vitale, A., Bielli, A., and Ceriotti, A. (1995). The binding protein associates with monomeric phaseolin. Plant Physiol. 107, 1411-1418.
    • (1995) Plant Physiol. , vol.107 , pp. 1411-1418
    • Vitale, A.1    Bielli, A.2    Ceriotti, A.3
  • 95
    • 0023658351 scopus 로고
    • The rate of bulk flow from the endoplasmic reticulum to the cell surface
    • Wieland, F.T., Gleason, M.L., Serafini, T.A., and Rothman, J.E. (1987). The rate of bulk flow from the endoplasmic reticulum to the cell surface. Cell 50, 289-300.
    • (1987) Cell , vol.50 , pp. 289-300
    • Wieland, F.T.1    Gleason, M.L.2    Serafini, T.A.3    Rothman, J.E.4
  • 96
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
    • Wiertz, E.J.H.J., Jones, T.R., Sun, L., Bogyo, M., Geuze, H.J., and Ploegh, H.L. (1996). The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84, 769-779.
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.H.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5    Ploegh, H.L.6
  • 97
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz, E.J.H.J., Tortorella, D., Bogyo, M., Yu, J., Mothes, W., Jones, T.R., Rapoport, T.A., and Ploegh, H.L. (1997). Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384, 432-438.
    • (1997) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.H.J.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4    Mothes, W.5    Jones, T.R.6    Rapoport, T.A.7    Ploegh, H.L.8
  • 98
    • 0031426632 scopus 로고    scopus 로고
    • Aggregation as a determinant of protein fate in post-Golgi compartments: Role of the luminal domain of furin in lysosomal targeting
    • Wolins, N., Bosshart, H., Kuster, H., and Bonifacino, J.S. (1997). Aggregation as a determinant of protein fate in post-Golgi compartments: Role of the luminal domain of furin in lysosomal targeting. J. Cell Biol. 139, 1735-1745.
    • (1997) J. Cell Biol. , vol.139 , pp. 1735-1745
    • Wolins, N.1    Bosshart, H.2    Kuster, H.3    Bonifacino, J.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.