메뉴 건너뛰기




Volumn 110, Issue 6, 1997, Pages 695-706

Localization of integral membrane peptidylglycine α-amidating monooxygenase in neuroendocrine cells

Author keywords

Neuroendocrine; Secretory granule; TGN

Indexed keywords

ALPHA AMIDATING ENZYME; FLUORESCEIN ISOTHIOCYANATE; MEMBRANE ENZYME; TRANSFERRIN; UNSPECIFIC MONOOXYGENASE;

EID: 0030913489     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (62)

References (64)
  • 1
    • 0026729952 scopus 로고
    • Protein sorting und secretion granule formation in regulated secretory cells
    • Arvan, P. and Castle, J. D. (1992). Protein sorting und secretion granule formation in regulated secretory cells. Trends Cell Biol. 2, 327-331.
    • (1992) Trends Cell Biol. , vol.2 , pp. 327-331
    • Arvan, P.1    Castle, J.D.2
  • 2
    • 0027401375 scopus 로고
    • Endocytotic pathways in the melantroph of the rat pituitary
    • Back, N., Soinila, S. and Virtanen, I. (1993). Endocytotic pathways in the melantroph of the rat pituitary. Histochem. J. 25, 133-139.
    • (1993) Histochem. J. , vol.25 , pp. 133-139
    • Back, N.1    Soinila, S.2    Virtanen, I.3
  • 3
    • 0027639817 scopus 로고
    • Biogenesis of constitutive secretory vesicles, secretory granules, and synaptic vesicles
    • Bauerfeind, R. and Huttner, W. B. (1993). Biogenesis of constitutive secretory vesicles, secretory granules, and synaptic vesicles. Curr. Opin. Cell Biol. 5, 628-635.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 628-635
    • Bauerfeind, R.1    Huttner, W.B.2
  • 4
    • 0028245594 scopus 로고
    • A molecular description of synaptic vesicle membrane trafficking
    • Bennett, M. K. and Scheller, R. H. (1994). A molecular description of synaptic vesicle membrane trafficking. Annu. Rev. Biochem. 63, 63-100.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 63-100
    • Bennett, M.K.1    Scheller, R.H.2
  • 5
    • 0029010706 scopus 로고
    • Comparative localization of inannose-6-phosphate receptor with 2, 6-sialyltransferase in HepG2 cells: An analysis by confocal double immunofluorescence microscopy
    • Berger, E. G., Burger, P., Hille, A. and Bachi, T. (1995). Comparative localization of inannose-6-phosphate receptor with 2, 6-sialyltransferase in HepG2 cells: an analysis by confocal double immunofluorescence microscopy. Eur. J. Cell Biol. 67, 106-111.
    • (1995) Eur. J. Cell Biol. , vol.67 , pp. 106-111
    • Berger, E.G.1    Burger, P.2    Hille, A.3    Bachi, T.4
  • 6
    • 0026636695 scopus 로고
    • Effects of tannic acid on antigenicity and membrane contrast in ultrastructural immunocytochemistry
    • Berryman, M. A., Porter, R. D., Rodewald, R. D. and Hubbard, A. H. (1992). Effects of tannic acid on antigenicity and membrane contrast in ultrastructural immunocytochemistry. J. Histochem. Cytochem. 40, 845-857.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 845-857
    • Berryman, M.A.1    Porter, R.D.2    Rodewald, R.D.3    Hubbard, A.H.4
  • 7
    • 0027317940 scopus 로고
    • SCAMP 37, a new marker within the general cell surface recycling system
    • Brand, S. H. and Castle, J. D. (1993). SCAMP 37, a new marker within the general cell surface recycling system. EMBO J. 12, 3753-3761.
    • (1993) EMBO J. , vol.12 , pp. 3753-3761
    • Brand, S.H.1    Castle, J.D.2
  • 8
    • 0023463127 scopus 로고
    • Constitutive and regulated secretion of proteins
    • Burgess, T. L. and Kelly, R. B. (1987). Constitutive and regulated secretion of proteins. Annu. Rev. Cell Biol. 3, 243-293.
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 243-293
    • Burgess, T.L.1    Kelly, R.B.2
  • 9
    • 0029088909 scopus 로고
    • The cytoplasmic tail domain of the vacuolar protein sorting receptor Vps10p and a subset of VPS gene products regulate receptor stability, function, and localization
    • Cereghino, J. L., Marcusson, E. G. and Emr, S. D. (1995). The cytoplasmic tail domain of the vacuolar protein sorting receptor Vps10p and a subset of VPS gene products regulate receptor stability, function, and localization. Mol. Biol. Cell 6, 1089-1102.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1089-1102
    • Cereghino, J.L.1    Marcusson, E.G.2    Emr, S.D.3
  • 10
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat, E. and Huttner, W. B. (1991). Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J. Cell Biol. 115, 1505-1519.
    • (1991) J. Cell Biol. , vol.115 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 11
    • 0027605112 scopus 로고
    • Protein targeting to dense-core secretory granules
    • Chidgey, M. A. J. (1993). Protein targeting to dense-core secretory granules. BioEssays 15, 317-321.
    • (1993) BioEssays , vol.15 , pp. 317-321
    • Chidgey, M.A.J.1
  • 12
    • 0029040979 scopus 로고
    • Trans-golgi network (TGN) of different cell types: Three dimensional structural characteristics and variability
    • Clermont, Y., Rambourg, A. and Hermo, L. (1995). Trans-golgi network (TGN) of different cell types: three dimensional structural characteristics and variability. Anat. Rec. 242, 289-301.
    • (1995) Anat. Rec. , vol.242 , pp. 289-301
    • Clermont, Y.1    Rambourg, A.2    Hermo, L.3
  • 13
    • 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., Kickska, G. A. and Rindler, M. J. (1996). Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH. J. Biol. Cheiu. 271, 48-55.
    • (1996) J. Biol. Cheiu. , vol.271 , pp. 48-55
    • Colomer, V.1    Kickska, G.A.2    Rindler, M.J.3
  • 14
    • 0027997875 scopus 로고
    • Transport into and out of the Golgi complex studied by transfecting cells with cDNAs encoding horseradish peroxidase
    • Connolly, C. N., Futter, C. E., Gibson, A., Hopkins, C. R. and Cutler, D. F. (1994). Transport into and out of the Golgi complex studied by transfecting cells with cDNAs encoding horseradish peroxidase. J. Cell Biol. 127, 641-652.
    • (1994) J. Cell Biol. , vol.127 , pp. 641-652
    • Connolly, C.N.1    Futter, C.E.2    Gibson, A.3    Hopkins, C.R.4    Cutler, D.F.5
  • 15
    • 0028106459 scopus 로고
    • Identification of a sorting signal for the regulated secretory pathway at the N-terminus of pro-opiomelanocortin
    • Cool, D. R. and Loh, Y. P. (1994). Identification of a sorting signal for the regulated secretory pathway at the N-terminus of pro-opiomelanocortin. Biochimie 76, 265-270.
    • (1994) Biochimie , vol.76 , pp. 265-270
    • Cool, D.R.1    Loh, Y.P.2
  • 16
    • 0025228404 scopus 로고
    • Tubulovesicular processes emerge from trans-Golgi cisternae, extend alone microtubules and interlink adjacent trans-Golgi elements into a reticulum
    • Cooper, M. S., Cornell-Bell, A. H., Chernjavsky, A., Dani, J. W. and Smith, S. J. (1990). Tubulovesicular processes emerge from trans-Golgi cisternae, extend alone microtubules and interlink adjacent trans-Golgi elements into a reticulum. Cell 61, 135-145.
    • (1990) Cell , vol.61 , pp. 135-145
    • Cooper, M.S.1    Cornell-Bell, A.H.2    Chernjavsky, A.3    Dani, J.W.4    Smith, S.J.5
  • 17
    • 0025309605 scopus 로고
    • Pathways to regulated exocytosis in neurons
    • De Camilli, P. and Jahn, R. (1990). Pathways to regulated exocytosis in neurons. Annu. Rev. Physiol. 52, 625-645.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 625-645
    • De Camilli, P.1    Jahn, R.2
  • 18
    • 0027067835 scopus 로고
    • Cytoplasmic domain of P-selectin (CD62) contains the signal for sorting into the regulated secretory pathway
    • Disdier, M., Morrissey, J. H., Fugate, R. D., Bainton, D. F. and McEver, R. P. (1992). Cytoplasmic domain of P-selectin (CD62) contains the signal for sorting into the regulated secretory pathway. Mol. Biol. Cell 3, 309-321.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 309-321
    • Disdier, M.1    Morrissey, J.H.2    Fugate, R.D.3    Bainton, D.F.4    McEver, R.P.5
  • 19
    • 0027418132 scopus 로고
    • Peptidylglycine α-amidating monooxygenase: A multifunctional protein with catalytic, processing, and routing domains
    • Eipper, B. A., Milgram, S. L., Husten, E. J., Yun, H.-Y. and Mains, R. E. (1993). Peptidylglycine α-amidating monooxygenase: A multifunctional protein with catalytic, processing, and routing domains. Prot. Sci. 2, 489-497.
    • (1993) Prot. Sci. , vol.2 , pp. 489-497
    • Eipper, B.A.1    Milgram, S.L.2    Husten, E.J.3    Yun, H.-Y.4    Mains, R.E.5
  • 20
    • 0025789665 scopus 로고
    • Lysosomal membrane glycoproteins
    • Fukuda, M. (1991). Lysosomal membrane glycoproteins. J. Biol. Chem. 266, 21327-21330.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21327-21330
    • Fukuda, M.1
  • 21
    • 0029979181 scopus 로고    scopus 로고
    • Multivesicular endosomes containing internalized EGF-EGF receptor complexes mature, then fuse directly with lysosomes
    • Futter, C. E., Pearse, A., Hewlett, L. J. and Hopkins, C. R. (1996). Multivesicular endosomes containing internalized EGF-EGF receptor complexes mature, then fuse directly with lysosomes. J. Cell Biol. 132, 1011-1023.
    • (1996) J. Cell Biol. , vol.132 , pp. 1011-1023
    • Futter, C.E.1    Pearse, A.2    Hewlett, L.J.3    Hopkins, C.R.4
  • 22
    • 0023236117 scopus 로고
    • Membranes of sorting organelles display lateral heterogeneity in receptor distribution
    • Geuze, H. J., Slot, J. W. and Schwartz, A. L. (1987). Membranes of sorting organelles display lateral heterogeneity in receptor distribution. J. Cell Biol. 104, 1715-1723.
    • (1987) J. Cell Biol. , vol.104 , pp. 1715-1723
    • Geuze, H.J.1    Slot, J.W.2    Schwartz, A.L.3
  • 23
    • 0024241414 scopus 로고
    • Sorting of mannose-6-phosphate receptor and lysosomal membrane proteins in endocytic vesicles
    • Geuze, H. J., Stoorvogel, W., Strous, G. J., Slot, J. W., Bleekemolen, J. E. and Mellman, I. (1988). Sorting of mannose-6-phosphate receptor and lysosomal membrane proteins in endocytic vesicles. J. Cell Biol. 107, 2491-2501.
    • (1988) J. Cell Biol. , vol.107 , pp. 2491-2501
    • Geuze, H.J.1    Stoorvogel, W.2    Strous, G.J.3    Slot, J.W.4    Bleekemolen, J.E.5    Mellman, I.6
  • 24
    • 0025610724 scopus 로고
    • Endocytic membrane traffic to the golgi apparatus in a regulated secretory cell line
    • Green, S. A. and Kelly, R. B. (1990). Endocytic membrane traffic to the golgi apparatus in a regulated secretory cell line. J. Biol. Chem. 265, 21269-21278.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21269-21278
    • Green, S.A.1    Kelly, R.B.2
  • 25
    • 0028140035 scopus 로고
    • The cytoplasmic domain of P-selectin contains a sorting determinant that mediates rapid degradation in lysosomes
    • Green, S. A., Setiadi, H., McEver, R. P. and Kelly, R. B. (1994). The cytoplasmic domain of P-selectin contains a sorting determinant that mediates rapid degradation in lysosomes. J. Cell Biol. 4, 435-448.
    • (1994) J. Cell Biol. , vol.4 , pp. 435-448
    • Green, S.A.1    Setiadi, H.2    McEver, R.P.3    Kelly, R.B.4
  • 26
    • 0022187987 scopus 로고
    • Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane
    • Griffiths, G., Pfeiffer, S., Simons, K. and Matlin, K. (1985). Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane. J. Cell Biol. 101, 949-964.
    • (1985) J. Cell Biol. , vol.101 , pp. 949-964
    • Griffiths, G.1    Pfeiffer, S.2    Simons, K.3    Matlin, K.4
  • 27
    • 0026525382 scopus 로고
    • Intermediates in the constitutive and regulated secretory pathways release in vitro from semi-intact cells
    • Grimes, M. and Kelly, R. B. (1992). Intermediates in the constitutive and regulated secretory pathways release in vitro from semi-intact cells. J. Cell Biol. 117, 539-549.
    • (1992) J. Cell Biol. , vol.117 , pp. 539-549
    • Grimes, M.1    Kelly, R.B.2
  • 28
    • 0011242494 scopus 로고
    • Luminal membrane retrieved after exocytosis reaches most Golgi cisternae in secretory cells
    • Herzog, V. and Farquhar, M. G. (1977). Luminal membrane retrieved after exocytosis reaches most Golgi cisternae in secretory cells. Proc. Nat. Acad. Sci. USA 74, 5073-5077.
    • (1977) Proc. Nat. Acad. Sci. USA , vol.74 , pp. 5073-5077
    • Herzog, V.1    Farquhar, M.G.2
  • 30
    • 0027193423 scopus 로고
    • Use of endoproteases to identify catalytic domains, linker regions, and functional interactions in soluble peptidylglycine α-umidating monooxygenase
    • Husten, E. J., Tausk, F. A., Keutmann, H. T. and Eipper, B. A. (1993 ). Use of endoproteases to identify catalytic domains, linker regions, and functional interactions in soluble peptidylglycine α-umidating monooxygenase. J. Biol. Chem. 268, 9709-9717.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9709-9717
    • Husten, E.J.1    Tausk, F.A.2    Keutmann, H.T.3    Eipper, B.A.4
  • 31
    • 0027392908 scopus 로고
    • Protein targeting in the neuron
    • Kelly, R. B. and Grote, E. (1993). Protein targeting in the neuron. Annu. Rev. Neurosci. 16, 95-127.
    • (1993) Annu. Rev. Neurosci. , vol.16 , pp. 95-127
    • Kelly, R.B.1    Grote, E.2
  • 32
    • 0024410381 scopus 로고
    • Sorting and traffic in the central vacuolar system
    • Klausner, R. D. (1989). Sorting and traffic in the central vacuolar system. Cell 57, 703-706.
    • (1989) Cell , vol.57 , pp. 703-706
    • Klausner, R.D.1
  • 33
    • 0029024637 scopus 로고
    • Membrane protein trafficking through the common apical endosome compartment of polarized Caco-2 cells
    • Knight, A., Hughson, E., Hopkins, C. R. and Cutler, D. F. (1995). Membrane protein trafficking through the common apical endosome compartment of polarized Caco-2 cells. Mol. Biol. Cell 6, 597-610.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 597-610
    • Knight, A.1    Hughson, E.2    Hopkins, C.R.3    Cutler, D.F.4
  • 34
    • 0026517633 scopus 로고
    • P-Selectin, a granule membrane protein of platelets and endothelial cells, follows the regulated secretory pathway in AtT-20 cells
    • Koedam, J. A., Cramer, E. M., Briend, E., Furie, B., Furie, B. C. and Wagner, D. D. (1992). P-Selectin, a granule membrane protein of platelets and endothelial cells, follows the regulated secretory pathway in AtT-20 cells. J. Cell Biol. 116, 617-625.
    • (1992) J. Cell Biol. , vol.116 , pp. 617-625
    • Koedam, J.A.1    Cramer, E.M.2    Briend, E.3    Furie, B.4    Furie, B.C.5    Wagner, D.D.6
  • 35
    • 0028817907 scopus 로고
    • The organization of the endoplasmic reticulum and the intermediate compartment in cultured rat hippocampal neurons
    • Krijnse-Locker, J., Parton, R. G., Fuller, S. D., Griffiths, G. and Dotti, C. G. (1995). The organization of the endoplasmic reticulum and the intermediate compartment in cultured rat hippocampal neurons. Mol. Biol. Cell 6, 1315-1332.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1315-1332
    • Krijnse-Locker, J.1    Parton, R.G.2    Fuller, S.D.3    Griffiths, G.4    Dotti, C.G.5
  • 36
    • 0026695156 scopus 로고
    • Protein targeting via the 'constitutive-like' secretory pathway in isolated pancreatic islets: Passive sorting in the immature granule compartment
    • Kuliawat, R. and Arvan, P. (1992). Protein targeting via the 'constitutive-like' secretory pathway in isolated pancreatic islets: passive sorting in the immature granule compartment. J. Cell Biol. 118, 521-529.
    • (1992) J. Cell Biol. , vol.118 , pp. 521-529
    • Kuliawat, R.1    Arvan, P.2
  • 37
    • 0028241106 scopus 로고
    • Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic β-cells
    • Kuliawat, R. and Arvan, P. (1994). Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic β-cells. J. Cell Biol. 126, 77-86.
    • (1994) J. Cell Biol. , vol.126 , pp. 77-86
    • Kuliawat, R.1    Arvan, P.2
  • 38
    • 0026472647 scopus 로고
    • The trans-Golgi network can be dissected structurally and functionally from the cisternae of the Golgi complex by brefeldin A
    • Ladinsky, M. S. and Howell, K. E. (1992). The trans-Golgi network can be dissected structurally and functionally from the cisternae of the Golgi complex by brefeldin A. Eur. J. Cell Biol. 59, 92-105.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 92-105
    • Ladinsky, M.S.1    Howell, K.E.2
  • 39
    • 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. and Howell, K. E. (1994). HVEM tomography of the trans-Golgi network: Structural insights and identification of a lace-like vesicle coat. J. Cell Biol. 127, 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
  • 40
    • 0025148186 scopus 로고
    • Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN38)
    • Luzio, J. P., Brake, B., Banting, G., Howell, K. E., Braghetta, P. and Stanley, K. K. (1990). Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN38). Biochem. J. 270, 97-102.
    • (1990) Biochem. J. , vol.270 , pp. 97-102
    • Luzio, J.P.1    Brake, B.2    Banting, G.3    Howell, K.E.4    Braghetta, P.5    Stanley, K.K.6
  • 41
    • 0027146118 scopus 로고
    • Maturation, internalization, and turnover of soluble and integral membrane proteins associated with atrial myocyte secretory granules
    • Maltese, J.-Y. and Eipper, B. A. (1993). Maturation, internalization, and turnover of soluble and integral membrane proteins associated with atrial myocyte secretory granules. Endocrinology 133, 2579-2587.
    • (1993) Endocrinology , vol.133 , pp. 2579-2587
    • Maltese, J.-Y.1    Eipper, B.A.2
  • 42
    • 0026750461 scopus 로고
    • Expression of individual forms of peptidylglycine α-amidating monooxygenase in AtT-20 cells: Endoproteolytic processing and routing to secretory granules
    • Milgram, S. L., Johnson, R. C. and Mains, R. E. (1992). Expression of individual forms of peptidylglycine α-amidating monooxygenase in AtT-20 cells: endoproteolytic processing and routing to secretory granules. J. Cell Biol. 117, 717-728.
    • (1992) J. Cell Biol. , vol.117 , pp. 717-728
    • Milgram, S.L.1    Johnson, R.C.2    Mains, R.E.3
  • 43
    • 0027528799 scopus 로고
    • COOH-terminal signals mediate the trafficking of a peptide processing enzyme in endocrine cells
    • Milgram, S. L., Mains, R. E. and Eipper, B. A. (1993). COOH-terminal signals mediate the trafficking of a peptide processing enzyme in endocrine cells. J. Cell Biol. 121, 23-36.
    • (1993) J. Cell Biol. , vol.121 , pp. 23-36
    • Milgram, S.L.1    Mains, R.E.2    Eipper, B.A.3
  • 44
    • 0027976518 scopus 로고
    • Differential trafficking of soluble and integral membrane secretory granule-associated proteins
    • Milgram, S. L., Eipper, B. A. and Mains, R. E. (1994). Differential trafficking of soluble and integral membrane secretory granule-associated proteins. J. Cell Biol. 124, 33-41.
    • (1994) J. Cell Biol. , vol.124 , pp. 33-41
    • Milgram, S.L.1    Eipper, B.A.2    Mains, R.E.3
  • 45
    • 0028203583 scopus 로고
    • Differential effects of temperature blockade on the proteolytic processing of three secretory granule-associated proteins
    • Milgram, S. L. and Mains, R. E. (1994). Differential effects of temperature blockade on the proteolytic processing of three secretory granule-associated proteins. J. Cell Sci. 107, 737-745.
    • (1994) J. Cell Sci. , vol.107 , pp. 737-745
    • Milgram, S.L.1    Mains, R.E.2
  • 46
    • 0030035227 scopus 로고    scopus 로고
    • Identification of routing determinants in the cytosolic domain of a secretory granule-associated integral membrane protein
    • Milgram, S. L., Mains, R. E. and Eipper, B. A. (1996). Identification of routing determinants in the cytosolic domain of a secretory granule-associated integral membrane protein. J. Biol. Chem. 271, 17526-17535.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17526-17535
    • Milgram, S.L.1    Mains, R.E.2    Eipper, B.A.3
  • 47
    • 0022773447 scopus 로고
    • Transport of horseradish peroxidase from the cell surface to the Golgi in insulin-secreting cells: Preferential labeling of cisternae located in an intermediate position in the stack
    • Orci, L., Ravazzola, M., Amherdt, M., Brown, D. and Perrelet, A. (1986). Transport of horseradish peroxidase from the cell surface to the Golgi in insulin-secreting cells: preferential labeling of cisternae located in an intermediate position in the stack. EMBO J. 5, 2097-2101.
    • (1986) EMBO J. , vol.5 , pp. 2097-2101
    • Orci, L.1    Ravazzola, M.2    Amherdt, M.3    Brown, D.4    Perrelet, A.5
  • 48
    • 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. and Moore, H.-P. H. (1987). The trans-most cisternae of the Golgi complex: a compartment for sorting of secretory and plasma membrane proteins. Cell 51, 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
  • 49
    • 0028817223 scopus 로고
    • Identification of subcellular compartments containing peptidylglycine α-amidating monooxygenase in rat anterior pituitary
    • Oyarce, A. M. and Eipper, B. A. (1995). Identification of subcellular compartments containing peptidylglycine α-amidating monooxygenase in rat anterior pituitary. J. Cell Sci. 108, 287-297.
    • (1995) J. Cell Sci. , vol.108 , pp. 287-297
    • Oyarce, A.M.1    Eipper, B.A.2
  • 50
    • 0025233925 scopus 로고
    • Three-dimensional electron microscopy: Structure of the Golgi apparatus
    • Rambourg, A. and Clermont, Y. (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
  • 51
    • 0022343674 scopus 로고
    • Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation
    • Roth, J., Taatjes, D. J., Lucocq, J. M., Weinstein, J. and Paulson, J. C. (1985). Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation. Cell 43, 287.
    • (1985) Cell , vol.43 , pp. 287
    • Roth, J.1    Taatjes, D.J.2    Lucocq, J.M.3    Weinstein, J.4    Paulson, J.C.5
  • 52
    • 0023830811 scopus 로고
    • Two distinct subpopulations of endosomes involved in membrane recycling and transport to lysosomes
    • Schmid, S. L., Fuchs, R., Male, P. and Mellman, I. (1988). Two distinct subpopulations of endosomes involved in membrane recycling and transport to lysosomes. Cell 52, 73-83.
    • (1988) Cell , vol.52 , pp. 73-83
    • Schmid, S.L.1    Fuchs, R.2    Male, P.3    Mellman, I.4
  • 53
    • 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. and Karquhar, M. G. (1989). Proteolytic processing of Pro-ACTH/endorphin begins in the Golgi complex of pituitary corticotropes and AtT-20 cells. Mol. Endocrinol. 3, 1223-1235.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1223-1235
    • Schnabel, E.1    Mains, R.E.2    Karquhar, M.G.3
  • 54
    • 0025174781 scopus 로고
    • Sorting within the regulated secretory pathway occurs in the trans-Golgi network
    • Sossin, W. S., Fisher, J. M. and Scheller, R. H. (1990). Sorting within the regulated secretory pathway occurs in the trans-Golgi network. J. Cell Biol. 110, 1-12.
    • (1990) J. Cell Biol. , vol.110 , pp. 1-12
    • Sossin, W.S.1    Fisher, J.M.2    Scheller, R.H.3
  • 55
    • 0027178838 scopus 로고
    • TGN38: A molecule on the move
    • Stanley, K. K. and Howell, K. E. (1993). TGN38: a molecule on the move. Trends Cell Biol. 3, 252-255.
    • (1993) Trends Cell Biol. , vol.3 , pp. 252-255
    • Stanley, K.K.1    Howell, K.E.2
  • 56
    • 0025828234 scopus 로고
    • Proteins of synaptic vesicles involved in exocytosis and membrane recycling
    • Sudhof, T. C. and Jahn, R. (1991). Proteins of synaptic vesicles involved in exocytosis and membrane recycling. Neuron 6, 665-677.
    • (1991) Neuron , vol.6 , pp. 665-677
    • Sudhof, T.C.1    Jahn, R.2
  • 57
    • 0027067004 scopus 로고
    • Expression of a peptide processing enzyme in cultured cells: Truncation mutants reveal a routing domain
    • Tausk, F. A., Milgram, S. L., Mains, R. E. and Eipper, B. A. (1992). Expression of a peptide processing enzyme in cultured cells: Truncation mutants reveal a routing domain. Mol. Endocrinol. 6, 2185-2196.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 2185-2196
    • Tausk, F.A.1    Milgram, S.L.2    Mains, R.E.3    Eipper, B.A.4
  • 58
    • 0028963094 scopus 로고
    • Maturation of early endosomes and vesicular traffic to lysosomes in relation to membrane recycling
    • Thilo, L., Stroud, E. and Haylett, T. (1995). Maturation of early endosomes and vesicular traffic to lysosomes in relation to membrane recycling. J. Cell Sci. 108, 1791-1803.
    • (1995) J. Cell Sci. , vol.108 , pp. 1791-1803
    • Thilo, L.1    Stroud, E.2    Haylett, T.3
  • 59
    • 0024318954 scopus 로고
    • Use of poly(vinylpyrrolidone) and poly(vinyl alcohol) for cryoultramicrotomy
    • Tokuyasu, K. T. (1989). Use of poly(vinylpyrrolidone) and poly(vinyl alcohol) for cryoultramicrotomy. Histochem. J. 21, 163-171.
    • (1989) Histochem. J. , vol.21 , pp. 163-171
    • Tokuyasu, K.T.1
  • 60
    • 0023601046 scopus 로고
    • Sorting of progeny coronavirus from condensed secretory proteins at the exit from the trans-Golgi network of AtT-20 cells
    • Tooze, J., Tooze, S. A. and Fuller, S. D. (1987). Sorting of progeny coronavirus from condensed secretory proteins at the exit from the trans-Golgi network of AtT-20 cells. J. Cell Biol. 105, 1215-1226.
    • (1987) J. Cell Biol. , vol.105 , pp. 1215-1226
    • Tooze, J.1    Tooze, S.A.2    Fuller, S.D.3
  • 61
    • 0026702055 scopus 로고
    • In AtT20 and HeLa cells brefeldin a induces the fusion of tubular endosomes and changes their distribution and some of their endocytic properties
    • Tooze, J. and Hollinshead, M. (1992). In AtT20 and HeLa cells brefeldin A induces the fusion of tubular endosomes and changes their distribution and some of their endocytic properties. J. Cell Biol. 118, 813-830.
    • (1992) J. Cell Biol. , vol.118 , pp. 813-830
    • Tooze, J.1    Hollinshead, M.2
  • 62
    • 0026332190 scopus 로고
    • Characterization of the immature secretory granule, an intermediate in granule biogenesis
    • Tooze, S. A., Flatmark, T., Tooze, J. and Huttner, W. B. (1991) Characterization of the immature secretory granule, an intermediate in granule biogenesis. J. Cell Biol. 115, 1491-1503.
    • (1991) J. Cell Biol. , vol.115 , pp. 1491-1503
    • Tooze, S.A.1    Flatmark, T.2    Tooze, J.3    Huttner, W.B.4
  • 63
    • 0026786340 scopus 로고
    • Endocytosis: What goes in and how?
    • Watts, C. (1992). Endocytosis: what goes in and how? J. Cell Sci. 103, 1-8.
    • (1992) J. Cell Sci. , vol.103 , pp. 1-8
    • Watts, C.1
  • 64
    • 0027255381 scopus 로고
    • Topological switching of the COOH-terminal domain of peptidylglycine α-amidating monooxygenase by alternative RNA splicing
    • Yun, H.-Y., Johnson, R. C., Mains, R. E. and Eipper, B. A. (1993). Topological switching of the COOH-terminal domain of peptidylglycine α-amidating monooxygenase by alternative RNA splicing. Arch. Biochem. Biophys. 301, 77-84.
    • (1993) Arch. Biochem. Biophys. , vol.301 , pp. 77-84
    • Yun, H.-Y.1    Johnson, R.C.2    Mains, R.E.3    Eipper, B.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.