메뉴 건너뛰기




Volumn 139, Issue 5, 1997, Pages 1109-1118

Role of NAD+ and ADP-ribosylation in the maintenance of the Golgi structure

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; BARBITURIC ACID DERIVATIVE; BREFELDIN A; CELL PROTEIN; COAT PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 0030827627     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.5.1109     Document Type: Article
Times cited : (45)

References (63)
  • 1
    • 0028960491 scopus 로고
    • Reconstitution of vesiculated Golgi membranes into stacks of cisternae: Requirement of NSF in stack formation
    • Acharya, U., J.M. McCaffery, R. Jacobs, and V. Malhotra. 1995a. Reconstitution of vesiculated Golgi membranes into stacks of cisternae: requirement of NSF in stack formation. J. Cell Biol. 129:577-589.
    • (1995) J. Cell Biol. , vol.129 , pp. 577-589
    • Acharya, U.1    McCaffery, J.M.2    Jacobs, R.3    Malhotra, V.4
  • 2
    • 0029084786 scopus 로고
    • The formation of Golgi stacks from vesiculated Golgi membranes requires two distinct fusion events
    • Acharya, U., R. Jacobs, J.-M. Peters, N. Watson, M.G. Farquhar, and V. Malhotra. 1995b. The formation of Golgi stacks from vesiculated Golgi membranes requires two distinct fusion events. Cell. 82:895-904.
    • (1995) Cell , vol.82 , pp. 895-904
    • Acharya, U.1    Jacobs, R.2    Peters, J.-M.3    Watson, N.4    Farquhar, M.G.5    Malhotra, V.6
  • 3
    • 0026543133 scopus 로고
    • Assembly and disassembly of the Golgi complex: Two processes arranged in a cis-trans direction
    • Alcalde, J., P. Bonay, A. Roa, S. Vilaro, and I.V. Sandoval. 1992. Assembly and disassembly of the Golgi complex: two processes arranged in a cis-trans direction. J. Cell Biol. 116:69-83.
    • (1992) J. Cell Biol. , vol.116 , pp. 69-83
    • Alcalde, J.1    Bonay, P.2    Roa, A.3    Vilaro, S.4    Sandoval, I.V.5
  • 4
    • 0027993053 scopus 로고
    • Golgi spectrin: Identification of an erythroid β-spectrin homologue associated with the Golgi complex
    • Beck, K.A., J.A. Buchanan, V. Malhotra, and W.J. Nelson. 1994. Golgi spectrin: identification of an erythroid β-spectrin homologue associated with the Golgi complex. J. Cell Biol. 127:707-723.
    • (1994) J. Cell Biol. , vol.127 , pp. 707-723
    • Beck, K.A.1    Buchanan, J.A.2    Malhotra, V.3    Nelson, W.J.4
  • 5
    • 0030918480 scopus 로고    scopus 로고
    • Golgi membrane skeleton: Identification and oligomerization of a 195-kD ankyrin isoform associated with the Golgi complex
    • Beck, K.A., J.A. Buchanan, and W.J. Nelson. 1997. Golgi membrane skeleton: identification and oligomerization of a 195-kD ankyrin isoform associated with the Golgi complex. J. Cell Sci. 110:1239-1249.
    • (1997) J. Cell Sci. , vol.110 , pp. 1239-1249
    • Beck, K.A.1    Buchanan, J.A.2    Nelson, W.J.3
  • 6
    • 0027183815 scopus 로고
    • A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes
    • Bhakdi, S., U. Weller, I. Walev, E. Martin, D. Jonas, and M. Palmer. 1993. A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes. Med. Microbiol. Immunol. 182:167-175.
    • (1993) Med. Microbiol. Immunol. , vol.182 , pp. 167-175
    • Bhakdi, S.1    Weller, U.2    Walev, I.3    Martin, E.4    Jonas, D.5    Palmer, M.6
  • 8
    • 0021804407 scopus 로고
    • Interaction of glyceraldehyde-3-phosphate dehydrogenase with isolated microsomal subfractions of skeletal muscle
    • Caswell, A.H., and A.M. Corbett. 1985. Interaction of glyceraldehyde-3-phosphate dehydrogenase with isolated microsomal subfractions of skeletal muscle. J. Biol. Chem. 260:6892-6898.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6892-6898
    • Caswell, A.H.1    Corbett, A.M.2
  • 9
    • 0028081835 scopus 로고
    • Connections between the various elements of the cis- and midcompartments of the Golgi apparatus of early rat spermatids
    • Clermont, Y., A. Rambourg, and L. Hermo. 1994. Connections between the various elements of the cis-and midcompartments of the Golgi apparatus of early rat spermatids. Anat. Rec. 240:469-480.
    • (1994) Anat. Rec. , vol.240 , pp. 469-480
    • Clermont, Y.1    Rambourg, A.2    Hermo, L.3
  • 10
    • 0027055402 scopus 로고
    • Adhesion of Golgi cisternae by proteinaceous interactions: Intercisternal bridges as putative adhesive structures
    • Cluett, E.B., and W.J. Brown. 1992. Adhesion of Golgi cisternae by proteinaceous interactions: intercisternal bridges as putative adhesive structures. J. Cell Sci. 103:773-784.
    • (1992) J. Cell Sci. , vol.103 , pp. 773-784
    • Cluett, E.B.1    Brown, W.J.2
  • 13
    • 0029898290 scopus 로고    scopus 로고
    • Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds βI∈* spectrin and associates with the Golgi apparatus
    • Devarajan, P., P.R., Stabach, A.S. Mann, T. Arbito, M. Kashagarian, and J.S. Morrow. 1996, Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds βI∈* spectrin and associates with the Golgi apparatus. J. Cell Biol. 133:819-830.
    • (1996) J. Cell Biol. , vol.133 , pp. 819-830
    • Devarajan, P.1    Stabach, P.R.2    Mann, A.S.3    Arbito, T.4    Kashagarian, M.5    Morrow, J.S.6
  • 15
    • 0024308993 scopus 로고
    • Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum
    • Doms, R.W., G. Russ, and J.W. Yewdell. 1989. Brefeldin A redistributes 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
  • 16
    • 0025968325 scopus 로고
    • Guanine nucleotides modulate the effects of brefeldin A in semipermeable cells: Regulation of the association of a 110-kD peripheral membrane protein with the Golgi apparatus
    • Donaldson, J.G., J. Lippincott-Schwartz, and R.D. Klausner. 1991. Guanine nucleotides modulate the effects of brefeldin A in semipermeable cells: regulation of the association of a 110-kD peripheral membrane protein with the Golgi apparatus. J. Cell Biol. 112:579-588.
    • (1991) J. Cell Biol. , vol.112 , pp. 579-588
    • Donaldson, J.G.1    Lippincott-Schwartz, J.2    Klausner, R.D.3
  • 17
    • 0026677375 scopus 로고
    • Brefeldin A inhibits Golgi membrane-catalyzed exchange of guanine nucleotide onto ARF protein
    • Donaldson, J.G., D. Finazzi, and R.D. Klausner. 1992. Brefeldin A inhibits Golgi membrane-catalyzed 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
  • 18
    • 0029998595 scopus 로고    scopus 로고
    • Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus
    • Erickson, J.W., C. Zhang, R.A. Kahan, T. Evans, and R.A. Cerione. 1996. Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus. J. Biol. Chem. 271:26850-26854.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26850-26854
    • Erickson, J.W.1    Zhang, C.2    Kahan, R.A.3    Evans, T.4    Cerione, R.A.5
  • 19
    • 0027198921 scopus 로고
    • Molecular characterization of two human autoantigens: Unique cDNAs encoding 95- and 160-kD proteins of a putative family in the Golgi complex
    • Fritzler, M.J., J.C. Hamel, R.L. Ochs, and E.K.L. Chan. 1993. Molecular characterization of two human autoantigens: unique cDNAs encoding 95-and 160-kD proteins of a putative family in the Golgi complex. J. Exp. Med. 178: 49-62.
    • (1993) J. Exp. Med. , vol.178 , pp. 49-62
    • Fritzler, M.J.1    Hamel, J.C.2    Ochs, R.L.3    Chan, E.K.L.4
  • 20
    • 0024237306 scopus 로고
    • Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum
    • Fujiwara, T., K. Oda, S. Yokota, A. Takatsuki, and Y. Ikehara. 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
  • 21
    • 0028264318 scopus 로고
    • Disruptions in Golgi structure and membrane traffic in a conditional lethal mammalian cell mutant are corrected by e-COP
    • Guo, Q., E. Vasile, and M. Krieger. 1994. Disruptions in Golgi structure and membrane traffic in a conditional lethal mammalian cell mutant are corrected by e-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
  • 22
    • 0026746713 scopus 로고
    • Inhibition by brefeldin A of a Golgi membrane enzyme that catalyzes exchange of guanine nucleotide bound to ARF
    • Helms, J.B., and J.E. Rothman. 1992. Inhibition by brefeldin A of a Golgi membrane enzyme that catalyzes 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
  • 23
    • 0029019737 scopus 로고
    • Human cyclins B1 and B2 are localized to strikingly different structures: B1 to microtubules, B2 primarily to the Golgi apparatus
    • Jackman, M., M. Firth, and J. Pines. 1995. Human cyclins B1 and B2 are localized to strikingly different structures: B1 to microtubules, B2 primarily to the Golgi apparatus. EMBO (Eur. Mol. Biol. Organ.) J. 8:1646-1654.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.8 , pp. 1646-1654
    • Jackman, M.1    Firth, M.2    Pines, J.3
  • 24
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R.D., J.G. Donaldson, and J. Lippincott-Schwartz. 1992. Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116:1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 26
    • 0026666672 scopus 로고
    • Human autoantibodies as reagents to conserved Golgi components. Characterization of a peripheral, 230-kD compartment-specific Golgi protein
    • Kooy, J., B.-H. Toh, J.M. Pettitt, R. Erlich, and P.A. Gleeson. 1992. Human autoantibodies as reagents to conserved Golgi components. Characterization of a peripheral, 230-kD compartment-specific Golgi protein. J. Biol. Chem. 267:20255-20263.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20255-20263
    • Kooy, J.1    Toh, B.-H.2    Pettitt, J.M.3    Erlich, R.4    Gleeson, P.A.5
  • 27
    • 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., L.C. Yuan, J.S. Bonifacino, and R.D. Klausner. 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
  • 28
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz, J., J.G. Donaldson, A. Schweizer, E.G. Berger, H.P. Hauri, L.C. Yuan, and R.D. Klausner. 1990. Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell. 60:821-836.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6    Klausner, R.D.7
  • 29
    • 0023441953 scopus 로고
    • Fragmentation and partitioning of the Golgi apparatus during mitosis in HeLa cells
    • Lucocq, J.M., and G. Warren. 1987. Fragmentation and partitioning of the Golgi apparatus during mitosis in HeLa cells. EMBO (Eur. Mol. Biol. Organ.) J. 6:3239-3246.
    • (1987) EMBO (Eur. Mol. Biol. Organ.) J. , vol.6 , pp. 3239-3246
    • Lucocq, J.M.1    Warren, G.2
  • 30
    • 0023252077 scopus 로고
    • A mitotic form of the Golgi apparatus in HeLa cells
    • Lucocq, J.M., J.G. Pryde, E.G. Berger, and G. Warren. 1987. A mitotic form of the Golgi apparatus in HeLa cells. J. Cell Biol. 104:865-874.
    • (1987) J. Cell Biol. , vol.104 , pp. 865-874
    • Lucocq, J.M.1    Pryde, J.G.2    Berger, E.G.3    Warren, G.4
  • 31
    • 0024409747 scopus 로고
    • Mitotic Golgi fragments in HeLa cells and their role in the reassembly pathway
    • Lucocq, J.M., E.G. Berger, and G. Warren. 1989. Mitotic Golgi fragments in HeLa cells and their role in the reassembly pathway. J. Cell Biol. 109:463-474.
    • (1989) J. Cell Biol. , vol.109 , pp. 463-474
    • Lucocq, J.M.1    Berger, E.G.2    Warren, G.3
  • 32
    • 0023903047 scopus 로고
    • Blockade by brefeldin A of intracellular transport of secretory proteins in mouse pituitary cells: Effects on the biosynthesis of thyrotropin and free a-subunits
    • Magner, J.A., and E. Papagiannes. 1988. Blockade by brefeldin A of intracellular transport of secretory proteins in mouse pituitary cells: effects on the biosynthesis of thyrotropin and free a-subunits. Endocrinology. 122:912-920.
    • (1988) Endocrinology , vol.122 , pp. 912-920
    • Magner, J.A.1    Papagiannes, E.2
  • 33
    • 0024340753 scopus 로고
    • Purification of a novel class of coated vesicles mediating biosynthetic protein transport through the Golgi stack
    • Malhotra, V., T. Serafini, L. Orci, J.C. Shepherd, and J.E. Rothman. 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
  • 34
    • 0028327124 scopus 로고
    • COP-coated vesicles are involved in the mitotic fragmentation of Golgi stacks in a cell-free system
    • Misteli, T., and G. Warren. 1994. COP-coated vesicles are involved in the mitotic fragmentation of Golgi stacks in a cell-free system. J. Cell Biol. 125: 269-282.
    • (1994) J. Cell Biol. , vol.125 , pp. 269-282
    • Misteli, T.1    Warren, G.2
  • 35
    • 0029168017 scopus 로고
    • Mitotic disassembly of the Golgi apparatus in vivo
    • Misteli, T., and G. Warren. 1995a. Mitotic disassembly of the Golgi apparatus in vivo. J. Cell Sci. 108:2715-2727.
    • (1995) J. Cell Sci. , vol.108 , pp. 2715-2727
    • Misteli, T.1    Warren, G.2
  • 36
    • 0029100979 scopus 로고
    • A role for tubular networks and COPI-independent pathway in the mitotic fragmentation of Golgi stacks in a cell-free system
    • Misteli, T., and G. Warren. 1995b. A role for tubular networks and COPI-independent pathway in the mitotic fragmentation of Golgi stacks in a cell-free system. J. Cell Biol. 130:1027-1039.
    • (1995) J. Cell Biol. , vol.130 , pp. 1027-1039
    • Misteli, T.1    Warren, G.2
  • 37
    • 0023008846 scopus 로고
    • Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes
    • Misumi, Y., K. Miki, A. Takatsuki, G. Tamura, and Y. Ikehara. 1986. Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes. J. Biol. Chem. 261:11398-11403.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11398-11403
    • Misumi, Y.1    Miki, K.2    Takatsuki, A.3    Tamura, G.4    Ikehara, Y.5
  • 38
    • 0025409872 scopus 로고
    • Disorganization and reorganization of the Golgi complex and the lysosomal system in association with mitosis
    • Moskalewski, S., and J. Thyberg. 1990. Disorganization and reorganization of the Golgi complex and the lysosomal system in association with mitosis. J. Submicrosc. Cytol. Pathol. 22:159-171.
    • (1990) J. Submicrosc. Cytol. Pathol. , vol.22 , pp. 159-171
    • Moskalewski, S.1    Thyberg, J.2
  • 39
    • 0023742061 scopus 로고
    • ADP-ribosylation of guanyl nueleotide-binding proteins by bacterial toxins
    • Moss, J., and M. Vaughan. 1988. ADP-ribosylation of guanyl nueleotide-binding proteins by bacterial toxins. Adv. Enzymol. Relat. Areas Mol. Biol. 61: 303-379.
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.61 , pp. 303-379
    • Moss, J.1    Vaughan, M.2
  • 42
    • 0027978637 scopus 로고
    • Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus
    • Nilsson, T., and G. Warren. 1994. Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus. Curr. Opin. Cell Biol. 6:517-521.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 517-521
    • Nilsson, T.1    Warren, G.2
  • 44
    • 0027945840 scopus 로고
    • Common structure of the catalytic sites of mammalian and bacterial toxin ADP-ribosyltransferases
    • Okazaki, I.J., and J. Moss. 1994. Common structure of the catalytic sites of mammalian and bacterial toxin ADP-ribosyltransferases. Mol. Cell. Biochem. 138:177-181.
    • (1994) Mol. Cell. Biochem. , vol.138 , pp. 177-181
    • Okazaki, I.J.1    Moss, J.2
  • 45
    • 0027499531 scopus 로고
    • β-COP localizes mainly to the cis-Golgi side in exocrine pancreas
    • Oprins, A., R. Duden, T.E. Kreis, H.J. Geuze, and J.W. Slot. 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
  • 47
    • 0027217617 scopus 로고
    • Early and late transformations occurring at organelles of the Golgi area under the influence of brefeldin A: An ultrastructural and lectin cytochemical study
    • Pavelka, M., and A. Ellinger. 1993. Early and late transformations occurring at organelles of the Golgi area under the influence of brefeldin A: an ultrastructural and lectin cytochemical study. J. Histochem. Cytochem. 41:1031-1042.
    • (1993) J. Histochem. Cytochem. , vol.41 , pp. 1031-1042
    • Pavelka, M.1    Ellinger, A.2
  • 48
    • 0028951905 scopus 로고
    • Overexpression of wild-type and mutant ARF1 and ARF6: Distinct perturbations of nonoverlapping membrane compartments
    • Peters, P.J., V.W. Hsu, C.E. Ooi, D. Finazzi, S.B. Teal, V. Oorschot, J.G. Donaldson, and R.D. Klausner. 1995. Overexpression of wild-type and mutant ARF1 and ARF6: distinct perturbations of nonoverlapping membrane compartments. J Cell Biol. 128:1003-1017.
    • (1995) J Cell Biol. , vol.128 , pp. 1003-1017
    • Peters, P.J.1    Hsu, V.W.2    Ooi, C.E.3    Finazzi, D.4    Teal, S.B.5    Oorschot, V.6    Donaldson, J.G.7    Klausner, R.D.8
  • 49
    • 0028027799 scopus 로고
    • LDLC encodes a brefeldin A-sensitive, peripheral Golgi protein required for normal Golgi function
    • Podos, S.D., P. Reddy, J. Ashkenas, and M. Krieger. 1994. LDLC encodes a brefeldin A-sensitive, peripheral Golgi protein required for normal Golgi function. J. Cell Biol. 127:679-691.
    • (1994) J. Cell Biol. , vol.127 , pp. 679-691
    • Podos, S.D.1    Reddy, P.2    Ashkenas, J.3    Krieger, M.4
  • 50
    • 0028930157 scopus 로고
    • Reassembly of Golgi stacks from mitotic Golgi fragments in a cell-free system
    • Rabouille, C., T. Misteli, R. Watson, and G. Warren. 1995a. Reassembly of Golgi stacks from mitotic Golgi fragments in a cell-free system. J. Cell Biol. 129:605-618.
    • (1995) J. Cell Biol. , vol.129 , pp. 605-618
    • Rabouille, C.1    Misteli, T.2    Watson, R.3    Warren, G.4
  • 51
    • 0029089959 scopus 로고
    • An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments
    • Rabouille, C., T.P. Levine, J.-M. Peters, and G. Warren. 1995b. An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments. Cell. 82:905-914.
    • (1995) Cell , vol.82 , pp. 905-914
    • Rabouille, C.1    Levine, T.P.2    Peters, J.-M.3    Warren, G.4
  • 52
    • 0025233925 scopus 로고
    • Three-dimensional electron microscopy: Structure of the Golgi apparatus
    • Rambourg, A., and Y. Clermont. 1990. Three-dimensional electron microscopy: structure of the Golgi apparatus. Eur. J. Cell Biol. 51:189-200.
    • (1990) Eur. J. Cell Biol. , vol.51 , pp. 189-200
    • Rambourg, A.1    Clermont, Y.2
  • 53
    • 0028364349 scopus 로고
    • A peripheral protein associated with the cis-Golgi network redistributes in the intermediate compartment upon brefeldin A treatment
    • Rios, R.M., A.-M. Tassin, C. Celati, C. Antony, M.-C. Boissier, J.-C. Homberg, and M. Bornens. 1994. A peripheral protein associated with the cis-Golgi network redistributes in the intermediate compartment upon brefeldin A treatment. J. Cell Biol. 125:997-1013.
    • (1994) J. Cell Biol. , vol.125 , pp. 997-1013
    • Rios, R.M.1    Tassin, A.-M.2    Celati, C.3    Antony, C.4    Boissier, M.-C.5    Homberg, J.-C.6    Bornens, M.7
  • 54
    • 0026627966 scopus 로고
    • Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: Effects of brefeldin A and G protein activators
    • Robinson, M.S., and T.E. Kreis. 1992. Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: effects of brefeldin A and G protein activators. Cell. 69:129-138.
    • (1992) Cell , vol.69 , pp. 129-138
    • Robinson, M.S.1    Kreis, T.E.2
  • 56
    • 0027274611 scopus 로고
    • The Golgi stack reassembles during telophase before arrival of proteins transported from the endoplasmic reticulum
    • Souter, E., M. Pypaert, and G. Warren. 1993. The Golgi stack reassembles during telophase before arrival of proteins transported from the endoplasmic reticulum. J. Cell Biol. 122:533-540.
    • (1993) J. Cell Biol. , vol.122 , pp. 533-540
    • Souter, E.1    Pypaert, M.2    Warren, G.3
  • 57
    • 84954944159 scopus 로고
    • Brefeldin A, a specific inhibitor of intracellular translocation of vesicular stomatitis virus G protein: Intracellular accumulation of high-mannose type G protein and inhibition of its cell surface expression
    • Takatsuki, A., and G. Tamura. 1985. Brefeldin A, a specific inhibitor of intracellular translocation of vesicular stomatitis virus G protein: intracellular accumulation of high-mannose type G protein and inhibition of its cell surface expression. Agric. Biol. Chem. 49:899-902.
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 899-902
    • Takatsuki, A.1    Tamura, G.2
  • 58
    • 0027174945 scopus 로고
    • Complete vesiculation of Golgi membranes and inhibition of protein transport by a novel sea sponge metabolite, Ilimaquinone
    • Takizawa, P.A., J.K. Yucel, B. Veit, D.J. Faulkner, T. Deerinck, G. Soto, M. Ellisman, and V. Malhotra. 1993. Complete vesiculation of Golgi membranes and inhibition of protein transport by a novel sea sponge metabolite, Ilimaquinone. Cell. 73:1079-1090.
    • (1993) Cell , vol.73 , pp. 1079-1090
    • Takizawa, P.A.1    Yucel, J.K.2    Veit, B.3    Faulkner, D.J.4    Deerinck, T.5    Soto, G.6    Ellisman, M.7    Malhotra, V.8
  • 59
    • 0022587346 scopus 로고
    • Three-dimensional architecture of the Golgi complex observed by high resolution scanning electron microscopy
    • Tanaka, K., A. Mitsushima, H. Fukudome, and Y. Kashima. 1986. Three-dimensional architecture of the Golgi complex observed by high resolution scanning electron microscopy. J. Submicrosc. Cytol. 18:1-9.
    • (1986) J. Submicrosc. Cytol. , vol.18 , pp. 1-9
    • Tanaka, K.1    Mitsushima, A.2    Fukudome, H.3    Kashima, Y.4
  • 60
    • 0030042322 scopus 로고    scopus 로고
    • Spectrin: On the path from structure to function
    • Viel, A., and D. Branton. 1996. Spectrin: on the path from structure to function. Curr. Opin. Cell Biol. 8:49-55.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 49-55
    • Viel, A.1    Branton, D.2
  • 61
    • 0028827095 scopus 로고
    • Mitotic disassembly of the mammalian Golgi apparatus
    • Warren, G., T. Levine, and T. Misteli. 1995. Mitotic disassembly of the mammalian Golgi apparatus. Trends Cell Biol. 5:413-416.
    • (1995) Trends Cell Biol. , vol.5 , pp. 413-416
    • Warren, G.1    Levine, T.2    Misteli, T.3
  • 63
    • 0027361181 scopus 로고
    • The actin-binding protein comitin (p24) is a component of the Golgi apparatus
    • Weiner, O.H., J. Murphy, G. Griffiths, M. Schleicher, and A.A. Noegel. 1993. The actin-binding protein comitin (p24) is a component of the Golgi apparatus. J. Cell Biol. 123:23-34.
    • (1993) J. Cell Biol. , vol.123 , pp. 23-34
    • Weiner, O.H.1    Murphy, J.2    Griffiths, G.3    Schleicher, M.4    Noegel, A.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.