메뉴 건너뛰기




Volumn 90, Issue 2, 1997, Pages 335-349

Bidirectional transport by distinct populations of COPI-coated vesicles

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; PROINSULIN; RECEPTOR;

EID: 0030755580     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80341-4     Document Type: Article
Times cited : (362)

References (73)
  • 1
    • 0023019044 scopus 로고
    • A microtubule-binding protein associated with membranes of the Golgi apparatus
    • Allan, V.J., and Kreis, T.E. (1986). A microtubule-binding protein associated with membranes of the Golgi apparatus. J. Cell Biol. 103, 2229-2239.
    • (1986) J. Cell Biol. , vol.103 , pp. 2229-2239
    • Allan, V.J.1    Kreis, T.E.2
  • 2
    • 0021738607 scopus 로고
    • Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine
    • Balch, W.E., Dunphy, W.G., Braell, W.A., and Rothman, J.E. (1984). Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine. Cell 39, 405-416.
    • (1984) Cell , vol.39 , pp. 405-416
    • Balch, W.E.1    Dunphy, W.G.2    Braell, W.A.3    Rothman, J.E.4
  • 4
  • 5
    • 0028181745 scopus 로고
    • Coatomer interaction with dilysine endoplasmic reticulum retention motifs
    • Cosson, P., and Letourneur, F. (1994). Coatomer interaction with dilysine endoplasmic reticulum retention motifs. Science 263, 1629-1631.
    • (1994) Science , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 6
    • 0029988456 scopus 로고    scopus 로고
    • δ-and ζ-COP, two coatomer subunits homologous to clathrin-associated proteins, are involved in ER retrieval
    • Cosson, P., Démollière, C., Hennecke, S., Duden, R., and Letourneur, F. (1996). δ-and ζ-COP, two coatomer subunits homologous to clathrin-associated proteins, are involved in ER retrieval. EMBO J. 15, 1792-1798.
    • (1996) EMBO J. , vol.15 , pp. 1792-1798
    • Cosson, P.1    Démollière, C.2    Hennecke, S.3    Duden, R.4    Letourneur, F.5
  • 7
    • 0026677375 scopus 로고
    • Brefeldin a inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein
    • Donaldson, J.G., Finazzi, D., and Klausner, R.D. (1992). Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein. Nature 360, 350-352.
    • (1992) Nature , vol.360 , pp. 350-352
    • Donaldson, J.G.1    Finazzi, D.2    Klausner, R.D.3
  • 8
    • 0024308993 scopus 로고
    • Brefeldin aredistributes resident and itinerant Golgi proteins to the endoplasmic reticulum
    • Doms, R.W., Russ, G., and Yewdell, J.W. (1989). Brefeldin Aredistributes resident and itinerant Golgi proteins to the endoplasmic reticulum. J. Cell Biol. 109, 61-72.
    • (1989) J. Cell Biol. , vol.109 , pp. 61-72
    • Doms, R.W.1    Russ, G.2    Yewdell, J.W.3
  • 9
    • 0026034357 scopus 로고
    • β-COP, a 110 kD protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to β-adaptin
    • Duden, R., Griffiths, G., Frank, R., Argos, P., and Kreis, T.E. (1991). β-COP, a 110 kD protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to β-adaptin. Cell 64, 649-665.
    • (1991) Cell , vol.64 , pp. 649-665
    • Duden, R.1    Griffiths, G.2    Frank, R.3    Argos, P.4    Kreis, T.E.5
  • 10
    • 0028170420 scopus 로고
    • Yeast β-and β′-coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein traffic
    • Duden, R., Hosobuchi, M., Hamamoto, S., Winey, M., Byers, B., and Schekman, R. (1994). Yeast β-and β′-coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein traffic. J. Biol. Chem. 269, 24486-24495.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24486-24495
    • Duden, R.1    Hosobuchi, M.2    Hamamoto, S.3    Winey, M.4    Byers, B.5    Schekman, R.6
  • 11
    • 0011694340 scopus 로고
    • Early and late functions associated with the Golgi apparatus reside in distinct compartments
    • Dunphy, W.G., Fries, E., Urbani, L.J., and Rothman, J.E. (1981). Early and late functions associated with the Golgi apparatus reside in distinct compartments. Proc. Natl. Acad. Sci. USA 78, 7453-7457.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 7453-7457
    • Dunphy, W.G.1    Fries, E.2    Urbani, L.J.3    Rothman, J.E.4
  • 14
    • 0029796074 scopus 로고    scopus 로고
    • Bi-modal interaction of coatomer with the p24 family of putative cargo receptors
    • Fiedler, K., Veit, M., Stamnes, M.A., and Rothman, J.E. (1996). Bi-modal interaction of coatomer with the p24 family of putative cargo receptors. Science 273, 1396-1399.
    • (1996) Science , vol.273 , pp. 1396-1399
    • Fiedler, K.1    Veit, M.2    Stamnes, M.A.3    Rothman, J.E.4
  • 15
    • 0024237306 scopus 로고
    • Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum
    • Fujiwara, T., Oda, K.,Yokota, S.,Takatsuki, A., and Ikehara, Y. (1988). Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum. J. Biol. Chem. 263, 18545-18552.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18545-18552
    • Fujiwara, T.1    Oda, K.2    Yokota, S.3    Takatsuki, A.4    Ikehara, Y.5
  • 16
    • 0028029829 scopus 로고
    • Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast
    • Gaynor, E.C., te Heesen, S., Graham, T.R., Aebi, M., and Emr, S.D. (1994). Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast. J. Cell Biol. 127, 653-665.
    • (1994) J. Cell Biol. , vol.127 , pp. 653-665
    • Gaynor, E.C.1    Te Heesen, S.2    Graham, T.R.3    Aebi, M.4    Emr, S.D.5
  • 17
    • 0031027758 scopus 로고    scopus 로고
    • COPI-independent anterograde transport: Cargo-selective ER to Golgi protein transport in yeast COPI mutants
    • Gaynor, E.C., and Emr, S.D. (1997). COPI-independent anterograde transport: cargo-selective ER to Golgi protein transport in yeast COPI mutants. J. Cell Biol. 136, 789-802.
    • (1997) J. Cell Biol. , vol.136 , pp. 789-802
    • Gaynor, E.C.1    Emr, S.D.2
  • 18
    • 0028921607 scopus 로고
    • Non-clathrin-coat protein α is a conserved subunit of coatomer and in saccharomyces cerevisiae is essential for growth
    • Erratum Proc. Natl. Acad. Sci. USA 92, 8532
    • Gerich, B., Orci, L., Tschochner, H., Lottspeich, F., Ravazzola, M., Amherdt, M., Wieland, F., and Harter, C. (1995). Non-clathrin-coat protein α is a conserved subunit of coatomer and in Saccharomyces cerevisiae is essential for growth. Proc. Natl. Acad. Sci. USA 92, 3229-3233. Erratum Proc. Natl. Acad. Sci. USA 92, 8532.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3229-3233
    • Gerich, B.1    Orci, L.2    Tschochner, H.3    Lottspeich, F.4    Ravazzola, M.5    Amherdt, M.6    Wieland, F.7    Harter, C.8
  • 19
    • 0028091981 scopus 로고
    • Localization of the Lys, Asp, Glu, Leu tetrapeptide receptor to the Golgi complex and the intermediate compartment in mammalian cells
    • Griffiths, G., Ericsson, M., Krijnse-Locker, J., Nilsson, T., Goud, B., Soeling, H.D., Tang, B.L., Wong, S.H., and Hong, W. (1994). Localization of the Lys, Asp, Glu, Leu tetrapeptide receptor to the Golgi complex and the intermediate compartment in mammalian cells. J. Cell Biol. 127, 1557-1574.
    • (1994) J. Cell Biol. , vol.127 , pp. 1557-1574
    • Griffiths, G.1    Ericsson, M.2    Krijnse-Locker, J.3    Nilsson, T.4    Goud, B.5    Soeling, H.D.6    Tang, B.L.7    Wong, S.H.8    Hong, W.9
  • 20
    • 0028984235 scopus 로고
    • Immunocytochemical localization of β-COP to the ER-Golgi boundary and the TGN
    • Griffiths, G., Pepperkok, R., Krijnse-Locker, J., and Kreis, T.E. (1995). Immunocytochemical localization of β-COP to the ER-Golgi boundary and the TGN. J. Cell Sci. 108, 2839-2856.
    • (1995) J. Cell Sci. , vol.108 , pp. 2839-2856
    • Griffiths, G.1    Pepperkok, R.2    Krijnse-Locker, J.3    Kreis, T.E.4
  • 21
    • 0028264318 scopus 로고
    • Disruptions in Golgi structure and membrane traffic in a conditional lethal mammalian cell mutant are corrected by ε-COP
    • Guo, Q., Vasile, E., and Krieger, M. (1994). Disruptions in Golgi structure and membrane traffic in a conditional lethal mammalian cell mutant are corrected by ε-COP. J. Cell Biol. 125, 1213-1224.
    • (1994) J. Cell Biol. , vol.125 , pp. 1213-1224
    • Guo, Q.1    Vasile, E.2    Krieger, M.3
  • 23
    • 0026746713 scopus 로고
    • Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF
    • Helms, J.B., and Rothman, J.E. (1992). Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF. Nature 360, 352-354.
    • (1992) Nature , vol.360 , pp. 352-354
    • Helms, J.B.1    Rothman, J.E.2
  • 24
    • 0026620198 scopus 로고
    • SEC21 is a gene required for ER to Golgi protein transport that encodes a subunit of a yeast coatomer
    • Hosobuchi, M., Kreis, T., and Schekman, R. (1992). SEC21 is a gene required for ER to Golgi protein transport that encodes a subunit of a yeast coatomer. Nature 360, 603-605.
    • (1992) Nature , vol.360 , pp. 603-605
    • Hosobuchi, M.1    Kreis, T.2    Schekman, R.3
  • 25
    • 0022721628 scopus 로고
    • Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface
    • Kreis, T.E. (1986). Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface. EMBO J. 5, 931-941.
    • (1986) EMBO J. , vol.5 , pp. 931-941
    • Kreis, T.E.1
  • 26
    • 0028069572 scopus 로고
    • Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step
    • Krijnse-Locker, J., Ericsson, M., Rottier, P.J.M., and Griffiths, G. (1994). Characterization of the budding compartment of mouse hepatitis virus: evidence that transport from the RER to the Golgi complex requires only one vesicular transport step. J. Cell Biol. 724, 55-70.
    • (1994) J. Cell Biol. , vol.724 , pp. 55-70
    • Krijnse-Locker, J.1    Ericsson, M.2    Rottier, P.J.M.3    Griffiths, G.4
  • 29
    • 0025187298 scopus 로고
    • A human homologue of the yeast HDEL receptor
    • Lewis, M.J., and Pelham, H.R. (1990). A human homologue of the yeast HDEL receptor. Nature 348, 162-163.
    • (1990) Nature , vol.348 , pp. 162-163
    • Lewis, M.J.1    Pelham, H.R.2
  • 30
    • 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. (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.2
  • 31
    • 0029932226 scopus 로고    scopus 로고
    • SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum
    • Lewis, M.J., and Pelham, H.R. (1996). SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum. Cell 85, 205-215.
    • (1996) Cell , vol.85 , pp. 205-215
    • Lewis, M.J.1    Pelham, H.R.2
  • 32
    • 0025289981 scopus 로고
    • The ERD2 gene determines the specificity of the luminal ER protein retention system
    • Lewis, M.J., Sweet, D.J., and Pelham, H.R. (1990). The ERD2 gene determines the specificity of the luminal ER protein retention system. Cell 61, 1359-1363.
    • (1990) Cell , vol.61 , pp. 1359-1363
    • Lewis, M.J.1    Sweet, D.J.2    Pelham, H.R.3
  • 33
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin a: Evidence for membrane cycling from Golgi to ER
    • Lippincott-Schwartz, J., Yuan, L.C., Bonifacino, J.S., and Klausner, R.D. (1989). Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell 56, 801-813.
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 34
    • 0021047474 scopus 로고
    • The production and characterization of monoclonal antibodies specific for human proinsulin using a sensitive microdot assay procedure
    • Madsen, O.D., Cohen, R.M., Fitch, F.W., Rubenstein, A.H., and Steiner, D.F. (1983). The production and characterization of monoclonal antibodies specific for human proinsulin using a sensitive microdot assay procedure. Endocrinology 113, 2135-2144.
    • (1983) Endocrinology , vol.113 , pp. 2135-2144
    • Madsen, O.D.1    Cohen, R.M.2    Fitch, F.W.3    Rubenstein, A.H.4    Steiner, D.F.5
  • 35
    • 0023707176 scopus 로고
    • Role of an N-ethylmaleimide-sensitive transport component in promoting fusion of transport vesicles with cisternae of the Golgi stack
    • Malhotra, V., Orci, L., Click, B.S., Block, M.R., and Rothman, J.E. (1988). Role of an N-ethylmaleimide-sensitive transport component in promoting fusion of transport vesicles with cisternae of the Golgi stack. Cell 54, 221-227.
    • (1988) Cell , vol.54 , pp. 221-227
    • Malhotra, V.1    Orci, L.2    Click, B.S.3    Block, M.R.4    Rothman, J.E.5
  • 36
    • 0024340753 scopus 로고
    • Purification of a novel class of coated vesicles mediating biosynthetic protein transport through the Golgi stack
    • Malhotra, V., Serafini, T., Orci, L., Shepherd, J.C., and Rothman, J.E. (1989). Purification of a novel class of coated vesicles mediating biosynthetic protein transport through the Golgi stack. Cell 58, 329-336.
    • (1989) Cell , vol.58 , pp. 329-336
    • Malhotra, V.1    Serafini, T.2    Orci, L.3    Shepherd, J.C.4    Rothman, J.E.5
  • 39
    • 0017570023 scopus 로고
    • Dynamics of the Golgi apparatus: Membrane differentiation and membrane flow
    • Morré, D.J., and Ovtracht, L. (1977). Dynamics of the Golgi apparatus: membrane differentiation and membrane flow. Int. Rev. Cytol. (Suppl.) 5, 61-188.
    • (1977) Int. Rev. Cytol. (Suppl.) , vol.5 , pp. 61-188
    • Morré, D.J.1    Ovtracht, L.2
  • 40
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • Novick, P., Field, C., and Scheckman, R. (1980). Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21, 205-215.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Scheckman, R.3
  • 41
    • 0027499531 scopus 로고
    • β-COP localizes mainly to the cis-golgi side in exocrine pancreas
    • Oprins, A., Duden, R., Kreis, T.E., Geuze, H.J., and Slot, J.W. (1993). β-COP localizes mainly to the cis-Golgi side in exocrine pancreas. J. Cell Biol. 121, 49-59.
    • (1993) J. Cell Biol. , vol.121 , pp. 49-59
    • Oprins, A.1    Duden, R.2    Kreis, T.E.3    Geuze, H.J.4    Slot, J.W.5
  • 42
    • 0016190409 scopus 로고
    • A portrait of the pancreatic B-cell
    • Orci, L. (1974). A portrait of the pancreatic B-cell. Diabetologia 10, 163-187.
    • (1974) Diabetologia , vol.10 , pp. 163-187
    • Orci, L.1
  • 43
    • 0020069732 scopus 로고
    • Macro-and micro-domains in the endocrine pancreas
    • Orci, L. (1982). Macro-and micro-domains in the endocrine pancreas. Diabetes 31, 538-565.
    • (1982) Diabetes , vol.31 , pp. 538-565
    • Orci, L.1
  • 44
    • 0022529019 scopus 로고
    • The insulin cell: Its cellular environment and how it processes (pro)insulin
    • Orci, L. (1986). The insulin cell: its cellular environment and how it processes (pro)insulin. Diabetes-Metabolism Reviews 2, 71-106.
    • (1986) Diabetes-metabolism Reviews , vol.2 , pp. 71-106
    • Orci, L.1
  • 46
    • 0022129515 scopus 로고
    • Direct identification of prohormone conversion site in insulin-secreting cells
    • Orci, L., Ravazzola, M., Amherdt, M., Madsen, O., Vassalli, J.D., and Perrelet, A. (1985). Direct identification of prohormone conversion site in insulin-secreting cells. Cell 42, 671-681.
    • (1985) Cell , vol.42 , pp. 671-681
    • Orci, L.1    Ravazzola, M.2    Amherdt, M.3    Madsen, O.4    Vassalli, J.D.5    Perrelet, A.6
  • 47
    • 0023052287 scopus 로고
    • A new type of coated vesicular carrier that appears not to contain clathrin: Its possible role in protein transport within the Golgi stack
    • Orci, L., Click, B.S., and Rothman, J.E. (1986). A new type of coated vesicular carrier that appears not to contain clathrin: its possible role in protein transport within the Golgi stack. Cell 46, 171-184.
    • (1986) Cell , vol.46 , pp. 171-184
    • Orci, L.1    Click, B.S.2    Rothman, J.E.3
  • 48
    • 0023610730 scopus 로고
    • Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated secretory vesicles
    • Orci, L., Ravazzola, M., Storch, M.J., Anderson, R.G., Vassalli, J.D., and Perrelet, A. (1987). Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated secretory vesicles. Cell 49, 865-868.
    • (1987) Cell , vol.49 , pp. 865-868
    • Orci, L.1    Ravazzola, M.2    Storch, M.J.3    Anderson, R.G.4    Vassalli, J.D.5    Perrelet, A.6
  • 49
    • 0024966027 scopus 로고
    • Dissection of a single round of vesicular transport: Sequential intermediates for intercisternal movement in the Golgi stack
    • Orci, L., Malhotra, V., Amherdt, M., Serafini, T., and Rothman, J.E. (1989). Dissection of a single round of vesicular transport: sequential intermediates for intercisternal movement in the Golgi stack. Cell 56, 357-368.
    • (1989) Cell , vol.56 , pp. 357-368
    • Orci, L.1    Malhotra, V.2    Amherdt, M.3    Serafini, T.4    Rothman, J.E.5
  • 52
    • 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
  • 53
    • 0024427039 scopus 로고
    • Control of protein exit from the endoplasmic reticulum
    • Pelham, H.R. (1989). Control of protein exit from the endoplasmic reticulum. Annu. Rev. Cell Biol. 5, 1-23.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 1-23
    • Pelham, H.R.1
  • 54
    • 0025225456 scopus 로고
    • The retention signal for soluble proteins of the endoplasmic reticulum
    • Pelham, H.R. (1990). The retention signal for soluble proteins of the endoplasmic reticulum. Trends Biochem. Sci. 15, 483-486.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 483-486
    • Pelham, H.R.1
  • 55
    • 0028661187 scopus 로고
    • About turn for the COPs?
    • Pelham, H.R.B.(1994). About turn for the COPs? Cell 79, 1125-1127.
    • (1994) Cell , vol.79 , pp. 1125-1127
    • Pelham, H.R.B.1
  • 56
    • 0027220591 scopus 로고
    • β-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo
    • Pepperkok, R., Scheel, J., Horstmann, H., Hauri, H.P., Griffiths, G., and Kreis, T.E. (1993). β-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo. Cell 74, 71-82.
    • (1993) Cell , vol.74 , pp. 71-82
    • Pepperkok, R.1    Scheel, J.2    Horstmann, H.3    Hauri, H.P.4    Griffiths, G.5    Kreis, T.E.6
  • 57
    • 0027165412 scopus 로고
    • Beta-COP is essential for transport of protein from the endoplasmic reticulum to the Golgi in vitro
    • Peter, F., Plutner, H., Zhu, H., Kreis, T.E., and Balch, W.E. (1993). Beta-COP is essential for transport of protein from the endoplasmic reticulum to the Golgi in vitro. J. Cell Biol. 122, 1155-1167.
    • (1993) J. Cell Biol. , vol.122 , pp. 1155-1167
    • Peter, F.1    Plutner, H.2    Zhu, H.3    Kreis, T.E.4    Balch, W.E.5
  • 58
    • 0018082456 scopus 로고
    • Ultrastructural localization of intracellular antigens by the use of protein a-gold technique
    • Roth, J., Bendayan, M., and Orci, L. (1978). Ultrastructural localization of intracellular antigens by the use of protein A-gold technique. J. Histochem. Cytochem. 26, 1074-1081.
    • (1978) J. Histochem. Cytochem. , vol.26 , pp. 1074-1081
    • Roth, J.1    Bendayan, M.2    Orci, L.3
  • 59
    • 0019793823 scopus 로고
    • The Golgi apparatus: Two organelles in tandem
    • Rothman, J.E. (1981). The Golgi apparatus: two organelles in tandem. Science 273, 1212-1219.
    • (1981) Science , vol.273 , pp. 1212-1219
    • Rothman, J.E.1
  • 60
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J.E. (1994). Mechanisms of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 61
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman, J.E., and Wieland, F.T. (1996). Protein sorting by transport vesicles. Science 272, 227-234.
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 62
    • 0021148465 scopus 로고
    • Pre-and post-Golgi vacuoles operate in the transport of semliki forest virus membrane glycoproteins to the cell surface
    • Saraste, J., and Kuismanen, E. (1984). Pre-and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface. Cell 38, 535-549.
    • (1984) Cell , vol.38 , pp. 535-549
    • Saraste, J.1    Kuismanen, E.2
  • 63
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R., and Orci, L. (1996). Coat proteins and vesicle budding. Science 271, 1526-1533.
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 64
    • 0025362445 scopus 로고
    • ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway
    • Semenza, J.C., Hardwick, K.G., Dean, N., and Pelham, H.R. (1990). ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell 61, 1349-1357.
    • (1990) Cell , vol.61 , pp. 1349-1357
    • Semenza, J.C.1    Hardwick, K.G.2    Dean, N.3    Pelham, H.R.4
  • 65
    • 0026001029 scopus 로고
    • ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein
    • Serafini, T., Orci, L., Amherdt, M., Brunner, M., Kahn, R.A., and Rothman, J.E. (1991). ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. Cell 67, 239-253.
    • (1991) Cell , vol.67 , pp. 239-253
    • Serafini, T.1    Orci, L.2    Amherdt, M.3    Brunner, M.4    Kahn, R.A.5    Rothman, J.E.6
  • 66
    • 0029838658 scopus 로고    scopus 로고
    • Sorting by COPI-coated vesicles under interphase and mitotic conditions
    • Sonnichsen, B., Watson, R., Clausen, H., Misteli, T., and Warren, G. (1996). Sorting by COPI-coated vesicles under interphase and mitotic conditions. J. Cell Biol. 734, 1411-1425.
    • (1996) J. Cell Biol. , vol.734 , pp. 1411-1425
    • Sonnichsen, B.1    Watson, R.2    Clausen, H.3    Misteli, T.4    Warren, G.5
  • 69
    • 0021875781 scopus 로고
    • Recognition of human insulin and proinsulin by monoclonal antibodies
    • Storch, M.J., Petersen, K.G., Licht, T., and Kerp, L. (1985). Recognition of human insulin and proinsulin by monoclonal antibodies. Diabetes 34, 808-811.
    • (1985) Diabetes , vol.34 , pp. 808-811
    • Storch, M.J.1    Petersen, K.G.2    Licht, T.3    Kerp, L.4
  • 70
    • 0027724473 scopus 로고
    • Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles
    • Tanigawa, G., Orci, L., Amherdt, M., Ravazzola, M., Helms, J.B., and Rothman, J.E. (1993). Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles. J. Cell Biol. 723, 1365-1371.
    • (1993) J. Cell Biol. , vol.723 , pp. 1365-1371
    • Tanigawa, G.1    Orci, L.2    Amherdt, M.3    Ravazzola, M.4    Helms, J.B.5    Rothman, J.E.6
  • 71
    • 0025957468 scopus 로고
    • 'Coatomer': A cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles
    • Waters, M.G., Serafini, T., and Rothman, J.E. (1991). 'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. Nature 349, 248-251.
    • (1991) Nature , vol.349 , pp. 248-251
    • Waters, M.G.1    Serafini, T.2    Rothman, J.E.3
  • 73
    • 0024801630 scopus 로고
    • Nucleotide binding cofactor activities of purified bovine brain and bacterially expressed ADP-ribosylation factor
    • Weiss, O., Holden, L., Rulka, C., and Kahn, R.A. (1989). Nucleotide binding cofactor activities of purified bovine brain and bacterially expressed ADP-ribosylation factor. J. Biol. Chem. 264, 21066-21072.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21066-21072
    • Weiss, O.1    Holden, L.2    Rulka, C.3    Kahn, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.