메뉴 건너뛰기




Volumn 1404, Issue 1-2, 1998, Pages 231-244

Biogenesis of secretory granules in the trans-Golgi network of neuroendocrine and endocrine cells

Author keywords

Immature secretory granule; Regulated secretion; Secretion; trans Golgi network; Vesicle formation

Indexed keywords

LYSOSOME ENZYME; MEMBRANE PROTEIN; SECRETORY PROTEIN;

EID: 0032516858     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4889(98)00059-7     Document Type: Article
Times cited : (195)

References (110)
  • 2
    • 0026239981 scopus 로고
    • What the granins tell us about the formation of secretory granules in neuroendocrine cells
    • Chanat E., Pimplikar S.W., Stinchcombe J.C., Huttner W.B. What the granins tell us about the formation of secretory granules in neuroendocrine cells. Cell Biophys. 19:1991;85-91.
    • (1991) Cell Biophys. , vol.19 , pp. 85-91
    • Chanat, E.1    Pimplikar, S.W.2    Stinchcombe, J.C.3    Huttner, W.B.4
  • 3
    • 0029257381 scopus 로고
    • Regulated secretion. Helper proteins for neuroendocrine secretion
    • Huttner W.B., Natori S. Regulated secretion. Helper proteins for neuroendocrine secretion. Curr. Biol. 5:1995;242-245.
    • (1995) Curr. Biol. , vol.5 , pp. 242-245
    • Huttner, W.B.1    Natori, S.2
  • 4
    • 0029981209 scopus 로고    scopus 로고
    • Chromogranin B (secretogranin I) promotes sorting to the regulated secretory pathway of processing intermediates derived from a peptide hormone precursor
    • Natori S., Huttner W.B. Chromogranin B (secretogranin I) promotes sorting to the regulated secretory pathway of processing intermediates derived from a peptide hormone precursor. Proc. Natl. Acad. Sci. USA. 93:1996;4431-4436.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4431-4436
    • Natori, S.1    Huttner, W.B.2
  • 5
    • 0024344257 scopus 로고
    • The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- And calcium-induced aggregation
    • Gerdes H.-H., Rosa P., Phillips E., Baeuerle P.A., Frank R., Argos P., Huttner W.B. The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation. J. Biol. Chem. 264:1989;12009-12015.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12009-12015
    • Gerdes, H.-H.1    Rosa, P.2    Phillips, E.3    Baeuerle, P.A.4    Frank, R.5    Argos, P.6    Huttner, W.B.7
  • 6
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat E., Huttner W.B. Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J. Cell Biol. 115:1991;1505-1519.
    • (1991) J. Cell Biol. , vol.115 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 7
    • 0028238359 scopus 로고
    • Calcium- And pH-dependent aggregation and membrane association of the precursor of the prohormone convertase PC2
    • Shennan K.I., Taylor N.A., Docherty K. Calcium- and pH-dependent aggregation and membrane association of the precursor of the prohormone convertase PC2. J. Biol. Chem. 269:1994;18646-18650.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18646-18650
    • Shennan, K.I.1    Taylor, N.A.2    Docherty, K.3
  • 8
    • 0030043593 scopus 로고    scopus 로고
    • Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH
    • Colomer V., Kicska G.A., Rindler M.J. Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH. J. Biol. Chem. 271:1996;48-55.
    • (1996) J. Biol. Chem. , vol.271 , pp. 48-55
    • Colomer, V.1    Kicska, G.A.2    Rindler, M.J.3
  • 10
    • 0023008920 scopus 로고
    • Clathrin-coated vesicular transport of secretory proteins during the formation of ACTH-containing secretory granules in AtT20 cells
    • Tooze J., Tooze S.A. Clathrin-coated vesicular transport of secretory proteins during the formation of ACTH-containing secretory granules in AtT20 cells. J. Cell Biol. 103:1986;839-850.
    • (1986) J. Cell Biol. , vol.103 , pp. 839-850
    • Tooze, J.1    Tooze, S.A.2
  • 11
    • 0020684553 scopus 로고
    • Chloroquine diverts ACTH from a regulated to a constitutive secretory pathway in AtT-20 cells
    • Moore H.P., Gumbiner B., Kelly R.B. Chloroquine diverts ACTH from a regulated to a constitutive secretory pathway in AtT-20 cells. Nature. 302:1983;434-436.
    • (1983) Nature , vol.302 , pp. 434-436
    • Moore, H.P.1    Gumbiner, B.2    Kelly, R.B.3
  • 12
    • 0024278677 scopus 로고
    • The role of a low pH intracellular compartment in the processing, storage, and secretion of ATCH and endorphin
    • Mains R.E., May V. The role of a low pH intracellular compartment in the processing, storage, and secretion of ATCH and endorphin. J. Biol. Chem. 263:1988;7887-7894.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7887-7894
    • Mains, R.E.1    May, V.2
  • 13
    • 0028131971 scopus 로고
    • Transport via the regulated secretory pathway in semi-intact PC12 cells: Role of intra-cisternal calcium and pH in the transport and sorting of secretogranin II
    • Carnell L., Moore H.P. Transport via the regulated secretory pathway in semi-intact PC12 cells: role of intra-cisternal calcium and pH in the transport and sorting of secretogranin II. J. Cell Biol. 127:1994;693-705.
    • (1994) J. Cell Biol. , vol.127 , pp. 693-705
    • Carnell, L.1    Moore, H.P.2
  • 14
    • 0028929733 scopus 로고
    • Direct measurement of trans-Golgi pH in living cells and regulation by second messengers
    • Seksek O., Biwersi J., Verkman A.S. Direct measurement of trans-Golgi pH in living cells and regulation by second messengers. J. Biol. Chem. 270:1995;4967-4970.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4967-4970
    • Seksek, O.1    Biwersi, J.2    Verkman, A.S.3
  • 16
    • 0022254988 scopus 로고
    • The insulin factory: A tour of the plant surroundings and a visit to the assembly line
    • Orci L. The insulin factory: a tour of the plant surroundings and a visit to the assembly line. Diabetologia. 28:1985;528-546.
    • (1985) Diabetologia , vol.28 , pp. 528-546
    • Orci, L.1
  • 17
    • 0028329930 scopus 로고
    • Sorting and processing of secretory proteins
    • Halban P.A., Irminger J.C. Sorting and processing of secretory proteins. Biochem. J. 299:1994;1-18.
    • (1994) Biochem. J. , vol.299 , pp. 1-18
    • Halban, P.A.1    Irminger, J.C.2
  • 18
    • 0027199869 scopus 로고
    • Prohormone processing in the trans-Golgi network: Endoproteolytic cleavage of prosomatostatin and formation of nascent secretory vesicles in permeabilized cells
    • Xu H., Shields D. Prohormone processing in the trans-Golgi network: endoproteolytic cleavage of prosomatostatin and formation of nascent secretory vesicles in permeabilized cells. J. Cell Biol. 122:1993;1169-1184.
    • (1993) J. Cell Biol. , vol.122 , pp. 1169-1184
    • Xu, H.1    Shields, D.2
  • 19
    • 0024380456 scopus 로고
    • Proteolytic processing of pro-ACTH/endorphin begins in the Golgi complex of pituitary corticotropes and AtT-20 cells
    • Schnabel E., Mains R.E., Farquhar M.G. Proteolytic processing of pro-ACTH/endorphin begins in the Golgi complex of pituitary corticotropes and AtT-20 cells. Mol. Endocrinol. 3:1989;1223-1235.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1223-1235
    • Schnabel, E.1    Mains, R.E.2    Farquhar, M.G.3
  • 20
    • 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., Perrelet A. Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated secretory vesicles. Cell. 49:1987;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
  • 21
    • 0023178004 scopus 로고
    • An antibody specific for an endoproteolytic cleavage site provides evidence that pro-opiomelanocortin is packaged into secretory granules in AtT20 cells before its cleavage
    • Tooze J., Hollinshead M., Frank R., Burke B. An antibody specific for an endoproteolytic cleavage site provides evidence that pro-opiomelanocortin is packaged into secretory granules in AtT20 cells before its cleavage. J. Cell Biol. 105:1987;155-162.
    • (1987) J. Cell Biol. , vol.105 , pp. 155-162
    • Tooze, J.1    Hollinshead, M.2    Frank, R.3    Burke, B.4
  • 22
    • 0031033158 scopus 로고    scopus 로고
    • PH-dependent processing of secretogranin II by the endopeptidase PC2 in isolated immature secretory granules
    • Urbé S., Dittié A.S., Tooze S.A. pH-dependent processing of secretogranin II by the endopeptidase PC2 in isolated immature secretory granules. Biochemical J. 321:1997;65-74.
    • (1997) Biochemical J. , vol.321 , pp. 65-74
    • Urbé, S.1    Dittié, A.S.2    Tooze, S.A.3
  • 24
    • 0028074665 scopus 로고
    • Formation of the insulin-containing secretory granule core occurs within immature beta-granules
    • Huang X.F., Arvan P. Formation of the insulin-containing secretory granule core occurs within immature beta-granules. J. Biol. Chem. 269:1994;20838-20844.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20838-20844
    • Huang, X.F.1    Arvan, P.2
  • 26
    • 0028241106 scopus 로고
    • Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic β-cells
    • Kuliawat R., Arvan P. Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic β-cells. J. Cell Biol. 126:1994;77-86.
    • (1994) J. Cell Biol. , vol.126 , pp. 77-86
    • Kuliawat, R.1    Arvan, P.2
  • 27
    • 0025174781 scopus 로고
    • Sorting within the regulated secretory pathway occurs in the trans-Golgi network
    • Sossin W.S., Fisher J.M., Scheller R.H. Sorting within the regulated secretory pathway occurs in the trans-Golgi network. J. Cell Biol. 110:1990;1-12.
    • (1990) J. Cell Biol. , vol.110 , pp. 1-12
    • Sossin, W.S.1    Fisher, J.M.2    Scheller, R.H.3
  • 28
    • 0029808688 scopus 로고    scopus 로고
    • Cell type-specific sorting of neuropeptides: A mechanism to modulate peptide composition of large dense-core vesicles
    • Klumperman J., Spiker S., Minnen J., Baker-Sharp H., Smit A.B., Geraerts W.P.M. Cell type-specific sorting of neuropeptides: a mechanism to modulate peptide composition of large dense-core vesicles. J. Neurosci. 16:1996;7930-7940.
    • (1996) J. Neurosci. , vol.16 , pp. 7930-7940
    • Klumperman, J.1    Spiker, S.2    Minnen, J.3    Baker-Sharp, H.4    Smit, A.B.5    Geraerts, W.P.M.6
  • 29
    • 0023463127 scopus 로고
    • Constitutive and regulated secretion of proteins
    • Burgess T.L., Kelly R.B. Constitutive and regulated secretion of proteins. Annu. Rev. Cell Biol. 3:1987;243-293.
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 243-293
    • Burgess, T.L.1    Kelly, R.B.2
  • 30
    • 0030943904 scopus 로고    scopus 로고
    • Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic β-cells
    • Kuliawat R., Klumperman J., Ludwig T., Arvan P. Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic β-cells. J. Cell Biol. 137:1997;595-608.
    • (1997) J. Cell Biol. , vol.137 , pp. 595-608
    • Kuliawat, R.1    Klumperman, J.2    Ludwig, T.3    Arvan, P.4
  • 31
  • 32
    • 0022402201 scopus 로고
    • Pathways of protein secretion in eukaryotes
    • Kelly R.B. Pathways of protein secretion in eukaryotes. Science. 230:1985;25-32.
    • (1985) Science , vol.230 , pp. 25-32
    • Kelly, R.B.1
  • 33
    • 0028958751 scopus 로고
    • Identification of the sorting signal motif within pro-opiomelanocortin for the regulated secretory pathway
    • Cool D.R., Fenger M., Snell C.R., Loh Y.P. Identification of the sorting signal motif within pro-opiomelanocortin for the regulated secretory pathway. J. Biol. Chem. 270:1995;8723-8729.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8723-8729
    • Cool, D.R.1    Fenger, M.2    Snell, C.R.3    Loh, Y.P.4
  • 35
    • 0027933035 scopus 로고
    • The disulfide bond in chromogranin B, which is essential for its sorting to secretory granules, is not required for its aggregation in the trans-Golgi network
    • Chanat E., Weiss U., Huttner W.B. The disulfide bond in chromogranin B, which is essential for its sorting to secretory granules, is not required for its aggregation in the trans-Golgi network. FEBS Lett. 351:1994;225-230.
    • (1994) FEBS Lett. , vol.351 , pp. 225-230
    • Chanat, E.1    Weiss, U.2    Huttner, W.B.3
  • 36
    • 0026731817 scopus 로고
    • Chromogranin B (Secretogranin I), a secretory protein of the regulated pathway, is also present in a tightly membrane-associated form in PC12 cells
    • Pimplikar S.W., Huttner W.B. Chromogranin B (Secretogranin I), a secretory protein of the regulated pathway, is also present in a tightly membrane-associated form in PC12 cells. J. Biol. Chem. 267:1992;4110-4118.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4110-4118
    • Pimplikar, S.W.1    Huttner, W.B.2
  • 41
    • 0028223178 scopus 로고
    • PH-dependent interaction of an intraluminal loop of inositol 1,4,5-triphosphate receptor with chromogranin A
    • Yoo S.H., Lewis M.S. pH-dependent interaction of an intraluminal loop of inositol 1,4,5-triphosphate receptor with chromogranin A. FEBS Lett. 341:1994;28-32.
    • (1994) FEBS Lett. , vol.341 , pp. 28-32
    • Yoo, S.H.1    Lewis, M.S.2
  • 42
    • 0001537740 scopus 로고
    • PH-dependent interaction of chromogranin A with integral membrane proteins of secretory vesicle including 260-kDa protein reactive to inositol 1,4,5-triphosphate receptor antibody
    • Yoo S.H. pH-dependent interaction of chromogranin A with integral membrane proteins of secretory vesicle including 260-kDa protein reactive to inositol 1,4,5-triphosphate receptor antibody. J. Biol. Chem. 269:1994;12001-12006.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12001-12006
    • Yoo, S.H.1
  • 43
    • 0025688843 scopus 로고
    • A targeting sequence for dense secretory granules resides in the active renin protein moiety of human preprorenin
    • Chu W.N., Baxter J.D., Reudelhuber T.L. A targeting sequence for dense secretory granules resides in the active renin protein moiety of human preprorenin. Mol. Endocrinol. 4:1990;1905-1913.
    • (1990) Mol. Endocrinol. , vol.4 , pp. 1905-1913
    • Chu, W.N.1    Baxter, J.D.2    Reudelhuber, T.L.3
  • 44
    • 0021997190 scopus 로고
    • The exocrine protein trypsinogen is targeted into the secretory granules of an endocrine cell line: Studies by gene transfer
    • Burgess T.L., Craik C.S., Kelly R.G. The exocrine protein trypsinogen is targeted into the secretory granules of an endocrine cell line: studies by gene transfer. J. Cell Biol. 101:1985;639-645.
    • (1985) J. Cell Biol. , vol.101 , pp. 639-645
    • Burgess, T.L.1    Craik, C.S.2    Kelly, R.G.3
  • 45
    • 0029102873 scopus 로고
    • A Chimeric proinsulin-CD5 protein expressed in AtT20 cells is directed to the cell surface via the constitutive pathway
    • Mbikay M., Grondin G., Rondeau N., Talbot B.G., Chrétien M. A Chimeric proinsulin-CD5 protein expressed in AtT20 cells is directed to the cell surface via the constitutive pathway. Exp. Cell Res. 220:1995;79-91.
    • (1995) Exp. Cell Res. , vol.220 , pp. 79-91
    • Mbikay, M.1    Grondin, G.2    Rondeau, N.3    Talbot, B.G.4    Chrétien, M.5
  • 46
    • 0020062469 scopus 로고
    • Two distinct intracellular pathways transport secretory and membrane glycoproteins to the surface of pituitary tumor cells
    • Gumbiner B., Kelly R.B. Two distinct intracellular pathways transport secretory and membrane glycoproteins to the surface of pituitary tumor cells. Cell. 28:1982;51-59.
    • (1982) Cell , vol.28 , pp. 51-59
    • Gumbiner, B.1    Kelly, R.B.2
  • 47
    • 0025072339 scopus 로고
    • Requirement for GTP hydrolysis in the formation of secretory vesicles
    • Tooze S.A., Weiss U., Huttner W.B. Requirement for GTP hydrolysis in the formation of secretory vesicles. Nature. 347:1990;207-208.
    • (1990) Nature , vol.347 , pp. 207-208
    • Tooze, S.A.1    Weiss, U.2    Huttner, W.B.3
  • 48
    • 0030001418 scopus 로고    scopus 로고
    • The in vitro generation of post-Golgi vesicles carrying viral envelope glycoproteins requires an ARF-like GTP-binding protein and a protein kinase C associated with the Golgi apparatus
    • Simon J.-P., Ivanov I.E., Shopsin B., Hersh D., Adesnik M., Sabatini D.D. The in vitro generation of post-Golgi vesicles carrying viral envelope glycoproteins requires an ARF-like GTP-binding protein and a protein kinase C associated with the Golgi apparatus. J. Biol. Chem. 271:1996;16952-16961.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16952-16961
    • Simon, J.-P.1    Ivanov, I.E.2    Shopsin, B.3    Hersh, D.4    Adesnik, M.5    Sabatini, D.D.6
  • 49
    • 0027072502 scopus 로고
    • Multiple trimeric G-proteins on the trans-Golgi network exert stimulatory and inhibitory effects on secretory vesicle formation
    • Leyte A., Barr F.A., Kehlenbach R.H., Huttner W.B. Multiple trimeric G-proteins on the trans-Golgi network exert stimulatory and inhibitory effects on secretory vesicle formation. EMBO J. 11:1992;4795-4804.
    • (1992) EMBO J. , vol.11 , pp. 4795-4804
    • Leyte, A.1    Barr, F.A.2    Kehlenbach, R.H.3    Huttner, W.B.4
  • 50
    • 0028033742 scopus 로고
    • An elevation of cytosolic protein phosphorylation modulates trimeric G-protein regulation of secretory vesicle formation from the trans-Golgi network
    • Ohashi M., Huttner W.B. An elevation of cytosolic protein phosphorylation modulates trimeric G-protein regulation of secretory vesicle formation from the trans-Golgi network. J. Biol. Chem. 269:1994;24897-24905.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24897-24905
    • Ohashi, M.1    Huttner, W.B.2
  • 51
    • 0029881303 scopus 로고    scopus 로고
    • A role for ADP-ribosylation factor1, but not COP I, in secretory vesicle biogenesis from the trans-Golgi network
    • Barr F., Huttner W.B. A role for ADP-ribosylation factor1, but not COP I, in secretory vesicle biogenesis from the trans-Golgi network. FEBS Lett. 384:1996;65-70.
    • (1996) FEBS Lett. , vol.384 , pp. 65-70
    • Barr, F.1    Huttner, W.B.2
  • 52
    • 0029935172 scopus 로고    scopus 로고
    • ADP-ribosylation factor-1 stimulates formation of nascent secretory vesicles from the trans-Golgi network of endocrine cells
    • Chen Y.-G., Shields D. ADP-ribosylation factor-1 stimulates formation of nascent secretory vesicles from the trans-Golgi network of endocrine cells. J. Biol. Chem. 271:1996;5297-5300.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5297-5300
    • Chen, Y.-G.1    Shields, D.2
  • 53
    • 0026525382 scopus 로고
    • Intermediates in the constitutive and regulated secretory pathways released in vitro from semi-intact cells
    • Grimes M., Kelly R.B. Intermediates in the constitutive and regulated secretory pathways released in vitro from semi-intact cells. J. Cell Biol. 117:1992;539-549.
    • (1992) J. Cell Biol. , vol.117 , pp. 539-549
    • Grimes, M.1    Kelly, R.B.2
  • 54
    • 0026353850 scopus 로고
    • Protein discharge from immature secretory granules displays both regulated and constitutive characteristics
    • Arvan P., Kuliawat R., Prabakaran D., Zavacki A.-M., Elahi D., Wang S., Pilkey D. Protein discharge from immature secretory granules displays both regulated and constitutive characteristics. J. Biol. Chem. 266:1991;14171-14174.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14171-14174
    • Arvan, P.1    Kuliawat, R.2    Prabakaran, D.3    Zavacki, A.-M.4    Elahi, D.5    Wang, S.6    Pilkey, D.7
  • 55
    • 0023663868 scopus 로고
    • The trans-most cisternae of the Golgi complex: A compartment for sorting of secretory and plasma membrane proteins
    • Orci L., Ravazzola M., Amherdt M., Perrelet A., Powell S.K., Quinn D.L., Moore H.-P.H. The trans-most cisternae of the Golgi complex: a compartment for sorting of secretory and plasma membrane proteins. Cell. 51:1987;1039-1051.
    • (1987) Cell , vol.51 , pp. 1039-1051
    • Orci, L.1    Ravazzola, M.2    Amherdt, M.3    Perrelet, A.4    Powell, S.K.5    Quinn, D.L.6    Moore, H.-P.H.7
  • 56
    • 0023601046 scopus 로고
    • Sorting of progeny coronavirus from condensed secretory proteins at the exit from the trans-Golgi network of AtT20 cells
    • Tooze J., Tooze S.A., Fuller S.D. Sorting of progeny coronavirus from condensed secretory proteins at the exit from the trans-Golgi network of AtT20 cells. J. Cell Biol. 105:1987;1215-1226.
    • (1987) J. Cell Biol. , vol.105 , pp. 1215-1226
    • Tooze, J.1    Tooze, S.A.2    Fuller, S.D.3
  • 57
    • 0028866530 scopus 로고
    • Intracellular trafficking of furin is modulated by the phosphorylation state of a casein kinase II site in its cytoplasmic tail
    • Jones B.G., Thomas L., Molloy S.S., Thulin C.D., Fry M.D., Walsh K.A., Thomas G. Intracellular trafficking of furin is modulated by the phosphorylation state of a casein kinase II site in its cytoplasmic tail. EMBO J. 14:1995;5869-5883.
    • (1995) EMBO J. , vol.14 , pp. 5869-5883
    • Jones, B.G.1    Thomas, L.2    Molloy, S.S.3    Thulin, C.D.4    Fry, M.D.5    Walsh, K.A.6    Thomas, G.7
  • 58
    • 0029071584 scopus 로고
    • Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localization and endosomal trafficking of the proprotein convertase furin
    • Schäfer W., Stroh A., Berghöfer S., Seiler J., Vey M., Kruse M.-L., Kern H.F., Klenk H.-D., Garten W. Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localization and endosomal trafficking of the proprotein convertase furin. EMBO J. 14:1995;2424-2435.
    • (1995) EMBO J. , vol.14 , pp. 2424-2435
    • Schäfer, W.1    Stroh, A.2    Berghöfer, S.3    Seiler, J.4    Vey, M.5    Kruse, M.-L.6    Kern, H.F.7    Klenk, H.-D.8    Garten, W.9
  • 59
    • 0028839910 scopus 로고
    • An acidic sequence within the cytoplasmic domain of furin functions as a determinant of trans-Golgi network localization and internalization from the cell surface
    • Voorhees P., Deignan E., van Donselaar E., Humphrey J., Marks M.S., Peters P.J., Bonifacino J.S. An acidic sequence within the cytoplasmic domain of furin functions as a determinant of trans-Golgi network localization and internalization from the cell surface. EMBO J. 14:1995;4961-4975.
    • (1995) EMBO J. , vol.14 , pp. 4961-4975
    • Voorhees, P.1    Deignan, E.2    Van Donselaar, E.3    Humphrey, J.4    Marks, M.S.5    Peters, P.J.6    Bonifacino, J.S.7
  • 60
    • 0028990820 scopus 로고
    • Cysteine proteinases in Gh4C1 cells, a rat pituitary tumor cell line, are secreted by the constitutive and regulated secretory pathways
    • Waguri S., Sato N., Watanabe T., Ishidoh K., Kominami E., Sato K., Uchiyama Y. Cysteine proteinases in Gh4C1 cells, a rat pituitary tumor cell line, are secreted by the constitutive and regulated secretory pathways. Eur. J. Cell Biol. 67:1995;308-318.
    • (1995) Eur. J. Cell Biol. , vol.67 , pp. 308-318
    • Waguri, S.1    Sato, N.2    Watanabe, T.3    Ishidoh, K.4    Kominami, E.5    Sato, K.6    Uchiyama, Y.7
  • 61
    • 0029089823 scopus 로고
    • Mannose 6-phosphate receptors in sorting and transport of lysosomal enzymes
    • Hille-Rehfeld A. Mannose 6-phosphate receptors in sorting and transport of lysosomal enzymes. Biochim. Biophys. Acta. 1241:1995;177-194.
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 177-194
    • Hille-Rehfeld, A.1
  • 62
    • 0030051441 scopus 로고    scopus 로고
    • The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor
    • Dittié A.S., Hajibagheri N., Tooze S.A. The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor. J. Cell Biol. 132:1996;523-536.
    • (1996) J. Cell Biol. , vol.132 , pp. 523-536
    • Dittié, A.S.1    Hajibagheri, N.2    Tooze, S.A.3
  • 63
    • 0030792177 scopus 로고    scopus 로고
    • Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation
    • Dittié A.S., Thomas L., Thomas G., Tooze S.A. Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation. EMBO J. 16:1997;4859-4870.
    • (1997) EMBO J. , vol.16 , pp. 4859-4870
    • Dittié, A.S.1    Thomas, L.2    Thomas, G.3    Tooze, S.A.4
  • 64
    • 0026695156 scopus 로고
    • Protein targeting via the 'constitutive-like' secretory pathway in isolated pancreatic islets: Passive sorting in the immature granule compartment
    • Kuliawat R., Arvan P. Protein targeting via the 'constitutive-like' secretory pathway in isolated pancreatic islets: passive sorting in the immature granule compartment. J. Cell Biol. 118:1992;521-529.
    • (1992) J. Cell Biol. , vol.118 , pp. 521-529
    • Kuliawat, R.1    Arvan, P.2
  • 65
    • 0023077578 scopus 로고
    • Biosynthetic protein transport and sorting by endoplasmic reticulum
    • Pfeffer S.R., Rothman J.E. Biosynthetic protein transport and sorting by endoplasmic reticulum. Annu. Rev. Biochem. 56:1987;829-852.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 829-852
    • Pfeffer, S.R.1    Rothman, J.E.2
  • 66
    • 0028136433 scopus 로고
    • HVEM tomography of the trans-Golgi network: Structural insights and identification of a lace-like vesicle coat
    • Ladinsky M.S., Kremer J.R., Furcinitti P.S., McIntosh J.R., Howell K.E. HVEM tomography of the trans-Golgi network: structural insights and identification of a lace-like vesicle coat. J. Cell Biol. 127:1994;29-38.
    • (1994) J. Cell Biol. , vol.127 , pp. 29-38
    • Ladinsky, M.S.1    Kremer, J.R.2    Furcinitti, P.S.3    McIntosh, J.R.4    Howell, K.E.5
  • 67
    • 0027240379 scopus 로고
    • A cytosolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network
    • Jones S.M., Crosby J.R., Salamero J., Howell K.E. A cytosolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network. J. Cell Biol. 122:1993;775-788.
    • (1993) J. Cell Biol. , vol.122 , pp. 775-788
    • Jones, S.M.1    Crosby, J.R.2    Salamero, J.3    Howell, K.E.4
  • 68
    • 0028920639 scopus 로고
    • Distinct coated vesicles labeled for p200 bud from trans-Golgi network membranes
    • Narula N., Stow J.L. Distinct coated vesicles labeled for p200 bud from trans-Golgi network membranes. Proc. Natl. Acad. Sci. USA. 92:1995;2874-2878.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2874-2878
    • Narula, N.1    Stow, J.L.2
  • 69
    • 0021869149 scopus 로고
    • Clathrin-immunoreactive sites in the Golgi apparatus are concentrated at the trans pole in polypeptide hormone-secreting cells
    • Orci L., Ravazzola M., Amherdt M., Louvard D., Perrelet A. Clathrin-immunoreactive sites in the Golgi apparatus are concentrated at the trans pole in polypeptide hormone-secreting cells. Proc. Natl. Acad. Sci. USA. 82:1985;5385-5389.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5385-5389
    • Orci, L.1    Ravazzola, M.2    Amherdt, M.3    Louvard, D.4    Perrelet, A.5
  • 70
    • 0025248051 scopus 로고
    • Cell-free protein sorting to the regulated and constitutive secretory pathways
    • Tooze S.A., Huttner W.B. Cell-free protein sorting to the regulated and constitutive secretory pathways. Cell. 60:1990;837-847.
    • (1990) Cell , vol.60 , pp. 837-847
    • Tooze, S.A.1    Huttner, W.B.2
  • 72
    • 0030454535 scopus 로고    scopus 로고
    • Formation of nascent secretory vesicles from the trans-Golgi network of endocrine cells is inhibited by tyrosine kinase and phosphatase inhibitors
    • Austin C.D., Shields D. Formation of nascent secretory vesicles from the trans-Golgi network of endocrine cells is inhibited by tyrosine kinase and phosphatase inhibitors. J. Cell Biol. 135:1996;1471-1483.
    • (1996) J. Cell Biol. , vol.135 , pp. 1471-1483
    • Austin, C.D.1    Shields, D.2
  • 73
    • 0028859466 scopus 로고
    • Regulated formation of Golgi secretory vesicles containing Alzheimer beta-amyloid precursor protein
    • Xu H., Greengard P., Gandy S. Regulated formation of Golgi secretory vesicles containing Alzheimer beta-amyloid precursor protein. J. Biol. Chem. 270:1995;23243-23245.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23243-23245
    • Xu, H.1    Greengard, P.2    Gandy, S.3
  • 74
    • 0029863203 scopus 로고    scopus 로고
    • Metabolism of Alzheimer beta-amyloid precursor protein: Regulation by protein kinase A in intact cells and in a cell-free system
    • Xu H., Sweeney D., Greengard P., Gandy S. Metabolism of Alzheimer beta-amyloid precursor protein: regulation by protein kinase A in intact cells and in a cell-free system. Proc. Natl. Acad. Sci. USA. 93:1996;4081-4084.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4081-4084
    • Xu, H.1    Sweeney, D.2    Greengard, P.3    Gandy, S.4
  • 76
    • 0029999246 scopus 로고    scopus 로고
    • Molecular cloning of phogrin, a protein-tyrosine phosphatase homologue localized to insulin secretory granule membranes
    • Wasmeier C., Hutton J.C. Molecular cloning of phogrin, a protein-tyrosine phosphatase homologue localized to insulin secretory granule membranes. J. Biol. Chem. 271:1996;18161-18170.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18161-18170
    • Wasmeier, C.1    Hutton, J.C.2
  • 77
    • 0027155088 scopus 로고
    • The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein
    • Stamnes M.A., Rothman J.E. The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein. Cell. 73:1993;999-1005.
    • (1993) Cell , vol.73 , pp. 999-1005
    • Stamnes, M.A.1    Rothman, J.E.2
  • 78
    • 0030053198 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors and ADP-ribosylation factors cooperate for high affinity interaction of the AP-1 Golgi assembly proteins with membranes
    • Le Borgne R., Griffiths G., Hoflack B. Mannose 6-phosphate receptors and ADP-ribosylation factors cooperate for high affinity interaction of the AP-1 Golgi assembly proteins with membranes. J. Biol. Chem. 271:1996;2162-2170.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2162-2170
    • Le Borgne, R.1    Griffiths, G.2    Hoflack, B.3
  • 79
    • 0027142022 scopus 로고
    • ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity
    • Brown H.A., Gutowski S., Moomaw C.R., Slaughter C., Sternweis P.C. ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell. 75:1993;1137-1144.
    • (1993) Cell , vol.75 , pp. 1137-1144
    • Brown, H.A.1    Gutowski, S.2    Moomaw, C.R.3    Slaughter, C.4    Sternweis, P.C.5
  • 81
    • 0029564902 scopus 로고
    • Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family
    • Hammond S.M., Altshuller Y.M., Sung T.C., Rudge S.A., Rose K., Engebrecht J., Morris A.J., Frohman M.A. Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. J. Biol. Chem. 270:1995;29640-29643.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29640-29643
    • Hammond, S.M.1    Altshuller, Y.M.2    Sung, T.C.3    Rudge, S.A.4    Rose, K.5    Engebrecht, J.6    Morris, A.J.7    Frohman, M.A.8
  • 82
    • 0028904466 scopus 로고
    • Arf proteins: The membrane traffic police?
    • Boman A.L., Kahn R.A. Arf proteins: the membrane traffic police? Trends Biochem. Sci. 20:1995;147-150.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 147-150
    • Boman, A.L.1    Kahn, R.A.2
  • 84
    • 0030881255 scopus 로고    scopus 로고
    • The role of ADP-ribosylation factor and phospholipase D in adaptor recruitment
    • West M.A., Bright N.A., Robinson M.S. The role of ADP-ribosylation factor and phospholipase D in adaptor recruitment. J. Cell Biol. 138:1997;1239-1254.
    • (1997) J. Cell Biol. , vol.138 , pp. 1239-1254
    • West, M.A.1    Bright, N.A.2    Robinson, M.S.3
  • 85
    • 0028346383 scopus 로고
    • Type I phosphatidylinositol 4-phosphate 5-kinase isoforms are specifically stimulated by phosphatidic acid
    • Jenkins G.H., Fisette P.L., Anderson R.A. Type I phosphatidylinositol 4-phosphate 5-kinase isoforms are specifically stimulated by phosphatidic acid. J. Biol. Chem. 269:1994;11547-11554.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11547-11554
    • Jenkins, G.H.1    Fisette, P.L.2    Anderson, R.A.3
  • 86
    • 0029968296 scopus 로고    scopus 로고
    • Phosphoinositides as regulators in membrane traffic
    • De Camilli P., Emr S.D., McPherson P.S., Novick P. Phosphoinositides as regulators in membrane traffic. Science. 271:1996;1533-1539.
    • (1996) Science , vol.271 , pp. 1533-1539
    • De Camilli, P.1    Emr, S.D.2    McPherson, P.S.3    Novick, P.4
  • 87
    • 0028030072 scopus 로고
    • Effects of acid phospholipids on nucleotide exchange properties of ADP-ribosylation factor 1. Evidence for specific interaction with phosphatidylinositol 4,5-bisphosphate
    • Terui T., Kahn R.A., Randazzo P.A. Effects of acid phospholipids on nucleotide exchange properties of ADP-ribosylation factor 1. Evidence for specific interaction with phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 269:1994;28130-28135.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28130-28135
    • Terui, T.1    Kahn, R.A.2    Randazzo, P.A.3
  • 88
    • 0028278346 scopus 로고
    • GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase-activating protein and acid phospholipids
    • Randazzo P.A., Kahn R.A. GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase-activating protein and acid phospholipids. J. Biol. Chem. 269:1994;10758-10763.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10758-10763
    • Randazzo, P.A.1    Kahn, R.A.2
  • 89
    • 0027965240 scopus 로고
    • Novel function of phosphatidylinositol 4,5-bisphosphate as a cofactor for brain membrane phospholipase D
    • Liscovitch M., Chalifa V., Pertile P., Chen C.S., Cantley L.C. Novel function of phosphatidylinositol 4,5-bisphosphate as a cofactor for brain membrane phospholipase D. J. Biol. Chem. 269:1994;21403-21406.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21403-21406
    • Liscovitch, M.1    Chalifa, V.2    Pertile, P.3    Chen, C.S.4    Cantley, L.C.5
  • 91
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer protein in yeast Golgi function [see comments]
    • Bankaitis V.A., Aitken J.R., Cleves A.E., Dowhan W. An essential role for a phospholipid transfer protein in yeast Golgi function [see comments]. Nature. 347:1990;561-562.
    • (1990) Nature , vol.347 , pp. 561-562
    • Bankaitis, V.A.1    Aitken, J.R.2    Cleves, A.E.3    Dowhan, W.4
  • 93
    • 0030971047 scopus 로고    scopus 로고
    • Greasing the Golgi budding machine
    • Martin T.F.J. Greasing the Golgi budding machine. Nature. 387:1997;21-22.
    • (1997) Nature , vol.387 , pp. 21-22
    • Martin, T.F.J.1
  • 94
    • 0028110018 scopus 로고
    • Vps34p required for yeast vacuolar protein sorting is a multiple specificity kinase that exhibits both protein kinase and phosphatidylinositol-specific PI 3-kinase activities
    • Stack J.H., Emr S.D. Vps34p required for yeast vacuolar protein sorting is a multiple specificity kinase that exhibits both protein kinase and phosphatidylinositol-specific PI 3-kinase activities. J. Biol. Chem. 269:1994;31552-31562.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31552-31562
    • Stack, J.H.1    Emr, S.D.2
  • 95
    • 0029618201 scopus 로고
    • Receptor-mediated protein sorting to the vacuole in yeast: Roles for a protein kinase, a lipid kinase and GTP-binding proteins
    • Stack J.H., Horazdovsky B., Emr S.D. Receptor-mediated protein sorting to the vacuole in yeast: roles for a protein kinase, a lipid kinase and GTP-binding proteins. Annu. Rev. Cell Dev. Biol. 11:1995;1-33.
    • (1995) Annu. Rev. Cell Dev. Biol. , vol.11 , pp. 1-33
    • Stack, J.H.1    Horazdovsky, B.2    Emr, S.D.3
  • 97
    • 0030720512 scopus 로고    scopus 로고
    • Phospatidylinositol 3-kinase is required for the formation of constitutive transport vesicles from the TGN
    • Jones S.M., Howell K.E. Phospatidylinositol 3-kinase is required for the formation of constitutive transport vesicles from the TGN. J. Cell Biol. 139:1997;339-349.
    • (1997) J. Cell Biol. , vol.139 , pp. 339-349
    • Jones, S.M.1    Howell, K.E.2
  • 98
    • 0026742127 scopus 로고
    • The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase
    • Attree O., Olivos I.M., Okabe I., Bailey L.C., Nelson D.L., Lewis R.A., McInnes R.R., Nussbaum R.L. The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase. Nature. 358:1992;239-242.
    • (1992) Nature , vol.358 , pp. 239-242
    • Attree, O.1    Olivos, I.M.2    Okabe, I.3    Bailey, L.C.4    Nelson, D.L.5    Lewis, R.A.6    McInnes, R.R.7    Nussbaum, R.L.8
  • 99
    • 0029120280 scopus 로고
    • The oculocerebrorenal syndrome gene product is a 105-kD protein localized to the Golgi complex
    • Olivos-Glander I.M., Jänne P.A., Nussbaum R.L. The oculocerebrorenal syndrome gene product is a 105-kD protein localized to the Golgi complex. Am. J. Hum. Genet. 57:1995;817-823.
    • (1995) Am. J. Hum. Genet. , vol.57 , pp. 817-823
    • Olivos-Glander, I.M.1    Jänne, P.A.2    Nussbaum, R.L.3
  • 100
    • 0029060795 scopus 로고
    • The protein deficient in Lowe syndrome is a phosphatidylinositol-4,5-bisphosphate 5-phosphatase
    • Zhang X., Jefferson A.B., Auethavekiat V., Majerus P.W. The protein deficient in Lowe syndrome is a phosphatidylinositol-4,5-bisphosphate 5-phosphatase. Proc. Natl. Acad. Sci. USA. 92:1995;4853-4856.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4853-4856
    • Zhang, X.1    Jefferson, A.B.2    Auethavekiat, V.3    Majerus, P.W.4
  • 102
    • 0030060326 scopus 로고    scopus 로고
    • A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals
    • David C., McPherson P.S., Mundigl O., de Camilli P. A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals. Proc. Natl. Acad. Sci. USA. 93:1996;331-335.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 331-335
    • David, C.1    McPherson, P.S.2    Mundigl, O.3    De Camilli, P.4
  • 103
    • 0028026793 scopus 로고
    • The role of clathrin, adaptors and dynamin in endocytosis
    • Robinson M.S. The role of clathrin, adaptors and dynamin in endocytosis. Curr. Opin. Cell Biol. 6:1994;538-544.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 538-544
    • Robinson, M.S.1
  • 104
    • 0030600145 scopus 로고    scopus 로고
    • Dynamin and receptor-mediated endocytosis
    • Damke H. Dynamin and receptor-mediated endocytosis. FEBS Lett. 389:1996;48-51.
    • (1996) FEBS Lett. , vol.389 , pp. 48-51
    • Damke, H.1
  • 105
    • 0029985418 scopus 로고    scopus 로고
    • Molecular mechanisms in synaptic vesicle endocytosis and recycling
    • De Camilli P., Takei K. Molecular mechanisms in synaptic vesicle endocytosis and recycling. Neuron. 16:1996;481-486.
    • (1996) Neuron , vol.16 , pp. 481-486
    • De Camilli, P.1    Takei, K.2
  • 106
    • 0029083773 scopus 로고
    • Rapid endocytosis coupled to exocytosis in adrenal chromaffin cells involves Ca2+, GTP, and dynamin but not clathrin
    • Artalejo C.R., Henley J.R., McNiven M.A., Palfrey H.C. Rapid endocytosis coupled to exocytosis in adrenal chromaffin cells involves Ca2+, GTP, and dynamin but not clathrin. Proc. Natl. Acad. Sci. USA. 92:1995;8328-8332.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8328-8332
    • Artalejo, C.R.1    Henley, J.R.2    McNiven, M.A.3    Palfrey, H.C.4
  • 107
    • 0028957707 scopus 로고
    • Ringing necks with dynamin
    • Kelly R.B. Ringing necks with dynamin. Nature. 374:1995;116-117.
    • (1995) Nature , vol.374 , pp. 116-117
    • Kelly, R.B.1
  • 108
    • 0029942238 scopus 로고    scopus 로고
    • Association of a dynamin-like protein with the Golgi apparatus in mammalian cells
    • Henley J.R., McNiven M.A. Association of a dynamin-like protein with the Golgi apparatus in mammalian cells. J. Cell Biol. 133:1996;761-775.
    • (1996) J. Cell Biol. , vol.133 , pp. 761-775
    • Henley, J.R.1    McNiven, M.A.2
  • 109
    • 0030051441 scopus 로고    scopus 로고
    • The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor
    • Dittié A.S., Hajibagheri N., Tooze S.A. The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor. J. Cell Biol. 132:1996;523-536.
    • (1996) J. Cell Biol. , vol.132 , pp. 523-536
    • Dittié, A.S.1    Hajibagheri, N.2    Tooze, S.A.3
  • 110
    • 0039359126 scopus 로고    scopus 로고
    • Essential role of the disulfide-bonded loop of chromogranin B for sorting to secretory granules is revealed by expression of a deletion mutant in the absence of endogenous granin synthesis
    • Krömer A., Glombik M.M., Huttner W.B., Gerdes H.-H. Essential role of the disulfide-bonded loop of chromogranin B for sorting to secretory granules is revealed by expression of a deletion mutant in the absence of endogenous granin synthesis. J. Cell Biol. 140:1998;1331-1346.
    • (1998) J. Cell Biol. , vol.140 , pp. 1331-1346
    • Krömer, A.1    Glombik, M.M.2    Huttner, W.B.3    Gerdes, H.-H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.