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Volumn 142, Issue 1, 1998, Pages 51-57

Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells

Author keywords

Apical; Lipid domain; Polarized epithelia; Protein traffic; Sorting

Indexed keywords

HEMAGGLUTININ;

EID: 0032514155     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.142.1.51     Document Type: Article
Times cited : (169)

References (52)
  • 1
    • 0027383316 scopus 로고
    • Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor
    • Aroeti, B., P.A. Kosen, I.D. Kuntz, F.E. Cohen, and K.E. Mostov. 1993. Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor. J. Cell Biol. 123:1149-1160.
    • (1993) J. Cell Biol. , vol.123 , pp. 1149-1160
    • Aroeti, B.1    Kosen, P.A.2    Kuntz, I.D.3    Cohen, F.E.4    Mostov, K.E.5
  • 2
    • 0028720467 scopus 로고
    • Cytomegalovirus plasmid vectors for permanent lines of polarized epithelial cells
    • Brewer, C.B. 1994. Cytomegalovirus plasmid vectors for permanent lines of polarized epithelial cells. Methods Cell Biol. 43:233-245.
    • (1994) Methods Cell Biol. , vol.43 , pp. 233-245
    • Brewer, C.B.1
  • 3
    • 0025913946 scopus 로고
    • A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin
    • Brewer, C.B., and M.G. Roth. 1991. A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin. J. Cell Biol. 114:413-421.
    • (1991) J. Cell Biol. , vol.114 , pp. 413-421
    • Brewer, C.B.1    Roth, M.G.2
  • 4
    • 0028900381 scopus 로고
    • Polarized exocytosis in MDCK cells is regulated by phosphorylation
    • Brewer, C.B., and M.G. Roth. 1995. Polarized exocytosis in MDCK cells is regulated by phosphorylation. J. Cell Sci. 108:789-796.
    • (1995) J. Cell Sci. , vol.108 , pp. 789-796
    • Brewer, C.B.1    Roth, M.G.2
  • 5
    • 0024433592 scopus 로고
    • Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells
    • Brown, D.A., B, Crise, and J.K. Rose. 1989. Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells. Science. 245: 1499-1501.
    • (1989) Science , vol.245 , pp. 1499-1501
    • Brown, D.A.1    Crise, B.2    Rose, J.K.3
  • 6
    • 0029123983 scopus 로고
    • Virus entry and release in polarized epithelial cells
    • Compans, R. 1995. Virus entry and release in polarized epithelial cells. Curr. Top. Microbiol. Immunol. 202:209-219.
    • (1995) Curr. Top. Microbiol. Immunol. , vol.202 , pp. 209-219
    • Compans, R.1
  • 7
    • 0023006195 scopus 로고
    • Assembly of influenza hemagglutinin trimers and its role in intracellular transport
    • Copeland, C.S., R.W. Doms, E.M. Bolzau, R.G. Webster, and A. Helenius. 1986. Assembly of influenza hemagglutinin trimers and its role in intracellular transport. J. Cell Biol. 103:1179-1191.
    • (1986) J. Cell Biol. , vol.103 , pp. 1179-1191
    • Copeland, C.S.1    Doms, R.W.2    Bolzau, E.M.3    Webster, R.G.4    Helenius, A.5
  • 8
    • 0029155983 scopus 로고
    • Intracellular routing of wild-type and mutated polymeric immunoglobulin receptor in hippocampal neurons in culture
    • de Hoop, M., C. von Poser, C. Lange, E. Ikonen, W. Hunziker, and C.G. Dotti. 1995. Intracellular routing of wild-type and mutated polymeric immunoglobulin receptor in hippocampal neurons in culture. J. Cell Biol. 130:1447-1459.
    • (1995) J. Cell Biol. , vol.130 , pp. 1447-1459
    • De Hoop, M.1    Von Poser, C.2    Lange, C.3    Ikonen, E.4    Hunziker, W.5    Dotti, C.G.6
  • 9
    • 0026017320 scopus 로고
    • Polarized sorting of glypiated proteins in hippocampal neurons
    • Dotti, C.G., R.G. Parton, and K. Simons. 1991. Polarized sorting of glypiated proteins in hippocampal neurons. Nature. 349:158-161.
    • (1991) Nature , vol.349 , pp. 158-161
    • Dotti, C.G.1    Parton, R.G.2    Simons, K.3
  • 10
    • 0025361892 scopus 로고
    • Polarized sorting of viral glycoproteins to the axon and dendrites of hippocampal neurons in culture
    • Dotti, C.G., and K. Simons. 1990. Polarized sorting of viral glycoproteins to the axon and dendrites of hippocampal neurons in culture. Cell. 62:63-72.
    • (1990) Cell , vol.62 , pp. 63-72
    • Dotti, C.G.1    Simons, K.2
  • 11
    • 0029068244 scopus 로고
    • Apical, basal, and lateral cues for epithelial polarization
    • Eaton, S., and K. Simons. 1995. Apical, basal, and lateral cues for epithelial polarization. Cell. 82:5-8.
    • (1995) Cell , vol.82 , pp. 5-8
    • Eaton, S.1    Simons, K.2
  • 12
    • 0027380624 scopus 로고
    • Related signals for endocytosis and basolateral sorting of the asialoglycoprotein receptor
    • Geffen, I., C. Fuhrer, B. Leitinger, M. Weiss, K. Huggel, G. Griffiths, and M. Spiess. 1993. Related signals for endocytosis and basolateral sorting of the asialoglycoprotein receptor. J. Biol. Chem. 268:20772-20777.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20772-20777
    • Geffen, I.1    Fuhrer, C.2    Leitinger, B.3    Weiss, M.4    Huggel, K.5    Griffiths, G.6    Spiess, M.7
  • 13
    • 0022552149 scopus 로고
    • Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellutar transport
    • Gething, M.J., K. McCammon, and J. Sambrook. 1986. Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellutar transport. Cell. 46:939-950.
    • (1986) Cell , vol.46 , pp. 939-950
    • Gething, M.J.1    McCammon, K.2    Sambrook, J.3
  • 14
    • 0027415668 scopus 로고
    • Apical secretion of hepatitis B surface antigen from transfected Madin-Darby canine kidney cells
    • Gonzalez, A., S. Nicovani, and F. Juica. 1993. Apical secretion of hepatitis B surface antigen from transfected Madin-Darby canine kidney cells. J. Biol. Chem. 268:6662-6667.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6662-6667
    • Gonzalez, A.1    Nicovani, S.2    Juica, F.3
  • 15
    • 0019795259 scopus 로고
    • Glycosylation does not determine segregation of viral envelope proteins in the plasma membrane of epithelial cells
    • Green, R.F., H.K. Meiss, and E. Rodriguez-Boulan. 1981. Glycosylation does not determine segregation of viral envelope proteins in the plasma membrane of epithelial cells. J. Cell Biol. 89:230-239.
    • (1981) J. Cell Biol. , vol.89 , pp. 230-239
    • Green, R.F.1    Meiss, H.K.2    Rodriguez-Boulan, E.3
  • 16
    • 0028985176 scopus 로고
    • Polarized sorting of beta-amyloid precursor protein and its proteolytic products in MDCK cells is regulated by two independent signals
    • Haass, C. E.H. Koo, A. Capell, D.B. Teplow, and D.J. Selkoe. 1995. Polarized sorting of beta-amyloid precursor protein and its proteolytic products in MDCK cells is regulated by two independent signals. J. Cell Biol. 128:537-547.
    • (1995) J. Cell Biol. , vol.128 , pp. 537-547
    • Haass, C.1    Koo, E.H.2    Capell, A.3    Teplow, D.B.4    Selkoe, D.J.5
  • 17
    • 0027451285 scopus 로고
    • Nonpolarized surface distribution and delivery of human CD7 in polarized MDCK cells
    • Haller, C., and S.L. Alper. 1993. Nonpolarized surface distribution and delivery of human CD7 in polarized MDCK cells. Am. J. Physiol. 265:C1069-C1079.
    • (1993) Am. J. Physiol. , vol.265
    • Haller, C.1    Alper, S.L.2
  • 18
    • 0028929058 scopus 로고
    • Cytoplasmic determinants involved in direct lysosomal sorting, endocytosis, and basolateral targeting of rat lgp120 (lamp-I) in MDCK cells
    • Honing, S., and W. Hunziker. 1995. Cytoplasmic determinants involved in direct lysosomal sorting, endocytosis, and basolateral targeting of rat lgp120 (lamp-I) in MDCK cells. J. Cell Biol. 128:321-332.
    • (1995) J. Cell Biol. , vol.128 , pp. 321-332
    • Honing, S.1    Hunziker, W.2
  • 19
    • 0029878960 scopus 로고    scopus 로고
    • Regulated cleavage of sterol regulatory clement binding proteins requires sequences on both sides of the endoplasmic reticulum membrane
    • Hua, X., J. Sakai, M.S. Brown, and J.L. Goldstein. 1996. Regulated cleavage of sterol regulatory clement binding proteins requires sequences on both sides of the endoplasmic reticulum membrane. J. Biol. Chem. 271:10379-10384.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10379-10384
    • Hua, X.1    Sakai, J.2    Brown, M.S.3    Goldstein, J.L.4
  • 20
    • 0030736714 scopus 로고    scopus 로고
    • Polarized apical targeting directed by the signal/anchor region of simian virus 5 hemagglutinin-neuraminidase
    • Huang, X.F., R.W. Compans, S. Chen, R.A. Lamb, and P. Arvan. 1997. Polarized apical targeting directed by the signal/anchor region of simian virus 5 hemagglutinin-neuraminidase. J. Biol. Chem. 272:27598-27604.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27598-27604
    • Huang, X.F.1    Compans, R.W.2    Chen, S.3    Lamb, R.A.4    Arvan, P.5
  • 21
    • 0028200044 scopus 로고
    • A di-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fc receptors in MDCK cells
    • Hunziker, W., and C. Fumey. 1994. A di-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fc receptors in MDCK cells. EMBO (Eur. Mol. Biol. Organ.) J. 13:2963-2967.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 2963-2967
    • Hunziker, W.1    Fumey, C.2
  • 22
    • 0032559854 scopus 로고    scopus 로고
    • Cholesterol is required for surface transport of influenza virus hemagglutinin
    • Keller, P., and K. Simons. 1998. Cholesterol is required for surface transport of influenza virus hemagglutinin. J. Cell Biol. 140:1357-1367.
    • (1998) J. Cell Biol. , vol.140 , pp. 1357-1367
    • Keller, P.1    Simons, K.2
  • 23
    • 0029839393 scopus 로고    scopus 로고
    • Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells
    • Kundu, A., R.T. Avalos, C.M. Sanderson and D.P. Nayak. 1996. Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells. J. Virol. 70:6508-6515.
    • (1996) J. Virol. , vol.70 , pp. 6508-6515
    • Kundu, A.1    Avalos, R.T.2    Sanderson, C.M.3    Nayak, D.P.4
  • 24
    • 0025239640 scopus 로고
    • The effects of foreign transmembrane domains on the biosynthesis of the influenza virus hemagglutinin
    • Lazarovits, J., S.P. Shia, N. Ktistakis, M.S. Lee, C. Bird, and M.G. Roth. 1990. The effects of foreign transmembrane domains on the biosynthesis of the influenza virus hemagglutinin. J. Biol. Chem. 265:4760-4767.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4760-4767
    • Lazarovits, J.1    Shia, S.P.2    Ktistakis, N.3    Lee, M.S.4    Bird, C.5    Roth, M.G.6
  • 25
    • 0031041239 scopus 로고    scopus 로고
    • The neural cell adhesion molecule expresses a tyrosine-independent basolateral sorting signal
    • Le Gall, A.H., S.K. Powell, C.A. Yeaman, and E. Rodriguez-Boulan. 1997. The neural cell adhesion molecule expresses a tyrosine-independent basolateral sorting signal. J. Biol. Chem. 272:4559-4567.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4559-4567
    • Le Gall, A.H.1    Powell, S.K.2    Yeaman, C.A.3    Rodriguez-Boulan, E.4
  • 26
    • 0030685122 scopus 로고    scopus 로고
    • Tyrosine-dependent basolateral sorting signals are distinct from tyrosine-dependent internalization signals
    • Lin, S., H.Y. Naim, and M.G. Roth. 1997. Tyrosine-dependent basolateral sorting signals are distinct from tyrosine-dependent internalization signals. J. Biol. Chem. 272:26300-26305.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26300-26305
    • Lin, S.1    Naim, H.Y.2    Roth, M.G.3
  • 27
    • 0024468669 scopus 로고
    • A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells
    • Lisanti, M.P., I.W. Caras, M.A. Davitz, and E. Rodriguez-Boulan. 1989. A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells. J. Cell Biol. 109:2145-2156.
    • (1989) J. Cell Biol. , vol.109 , pp. 2145-2156
    • Lisanti, M.P.1    Caras, I.W.2    Davitz, M.A.3    Rodriguez-Boulan, E.4
  • 28
    • 0030838739 scopus 로고    scopus 로고
    • Membrane cofactor protein (CD46) is a basolateral protein that is not endocytosed. Importance of the tetrapeptide FTSL at the carboxyl terminus
    • Maisner, A., G. Zimmer, M.K. Liszewski, D.M. Lublin, J.P. Atkinson, and G. Herrler. 1997. Membrane cofactor protein (CD46) is a basolateral protein that is not endocytosed. Importance of the tetrapeptide FTSL at the carboxyl terminus. J. Biol. Chem. 272:20793-20799.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20793-20799
    • Maisner, A.1    Zimmer, G.2    Liszewski, M.K.3    Lublin, D.M.4    Atkinson, J.P.5    Herrler, G.6
  • 29
    • 0021684629 scopus 로고
    • Sorting of an apical plasma membrane glycoprotein occurs before it reaches the cell surface in cultured epithelial cells
    • Matlin, K.S., and K. Simons. 1984. Sorting of an apical plasma membrane glycoprotein occurs before it reaches the cell surface in cultured epithelial cells. J. Cell Biol. 99:2131-2139.
    • (1984) J. Cell Biol. , vol.99 , pp. 2131-2139
    • Matlin, K.S.1    Simons, K.2
  • 30
    • 0028068273 scopus 로고
    • Mechanisms of cell polarity: Sorting and transport in epithelial cells
    • Matter, K., and I. Mellman. 1994. Mechanisms of cell polarity: sorting and transport in epithelial cells. Curr. Opin. Cell Biol. 6:545-554.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 545-554
    • Matter, K.1    Mellman, I.2
  • 31
    • 0029166488 scopus 로고
    • Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells
    • Mays R.W. K.A. Siemers, B.A Fritz, A.W. Lowe, G. van Meer, and W.J. Nelson. 1995. Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells. J. Cell Biol. 130:1105-1115.
    • (1995) J. Cell Biol. , vol.130 , pp. 1105-1115
    • Mays, R.W.1    Siemers, K.A.2    Fritz, B.A.3    Lowe, A.W.4    Van Meer, G.5    Nelson, W.J.6
  • 32
    • 0029943503 scopus 로고    scopus 로고
    • Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells
    • Musch, A., H.X. Xu, D. Shields, and E. Rodriguez-Boulan. 1996. Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells. J. Cell Biol. 133:543-558.
    • (1996) J. Cell Biol. , vol.133 , pp. 543-558
    • Musch, A.1    Xu, H.X.2    Shields, D.3    Rodriguez-Boulan, E.4
  • 33
    • 0030905888 scopus 로고    scopus 로고
    • Structural requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells
    • Odorizzi, G., and I.S. Trowbridge. 1997. Structural requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells. J. Cell Biol. 137:1255-1264.
    • (1997) J. Cell Biol. , vol.137 , pp. 1255-1264
    • Odorizzi, G.1    Trowbridge, I.S.2
  • 34
    • 0027276052 scopus 로고
    • The cytoplasmic tail of lysosomal acid phosphatase contains overlapping but distinct signals for basolateral sorting and rapid internalization in polarized MDCK cells
    • Prill, V., L. Lehmann, K. von Figura, and C. Peters. 1993. The cytoplasmic tail of lysosomal acid phosphatase contains overlapping but distinct signals for basolateral sorting and rapid internalization in polarized MDCK cells. EMBO (Eur. Mol. Biol. Organ.) J. 12:2181-2193.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 2181-2193
    • Prill, V.1    Lehmann, L.2    Von Figura, K.3    Peters, C.4
  • 35
    • 0026486469 scopus 로고
    • Polarized secretion of urokinase-type plasminogen activator by epithelial cells
    • Ragno, P., A. Estreicher, A. Gos, A. Wohlwend, D. Belin, and J.D. Vassalli. 1992. Polarized secretion of urokinase-type plasminogen activator by epithelial cells. Exp. Cell Res. 203:236-243.
    • (1992) Exp. Cell Res. , vol.203 , pp. 236-243
    • Ragno, P.1    Estreicher, A.2    Gos, A.3    Wohlwend, A.4    Belin, D.5    Vassalli, J.D.6
  • 36
    • 0029831485 scopus 로고    scopus 로고
    • The basolateral sorting signal of the polymeric immunoglobulin receptor contains two functional domains
    • Reich, V., K. Mostov, and B. Aroeti. 1996. The basolateral sorting signal of the polymeric immunoglobulin receptor contains two functional domains. J. Cell Sci. 109:2133-2139.
    • (1996) J. Cell Sci. , vol.109 , pp. 2133-2139
    • Reich, V.1    Mostov, K.2    Aroeti, B.3
  • 38
    • 2642597134 scopus 로고
    • Polarity of influenza and vesicular stomatitis virus maturation in MDCK
    • Roth, M.G., J.P. Fitzpatrick, and R.W. Compans. 1979. Polarity of influenza and vesicular stomatitis virus maturation in MDCK Proc. Natl. Acad. Sci. USA. 76:6430-6434.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 6430-6434
    • Roth, M.G.1    Fitzpatrick, J.P.2    Compans, R.W.3
  • 39
    • 0025325983 scopus 로고
    • The "megaprimer" method of site-directed mutagenesis
    • Sarkar, G., and S.S. Sommer. 1993. The "megaprimer" method of site-directed mutagenesis. Biotechniques. 8:404-407.
    • (1993) Biotechniques , vol.8 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 40
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele, P., M.G. Roth, and K. Simons. 1997. Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO (Eur. Mol. Biol. Organ.) J. 16:5501-5508.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 41
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-linked proteins: GPI-linked proteins in liposomes and cells show similar behavior
    • Schroeder, R., E. London, and D. Brown. 1994. Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-linked proteins: GPI-linked proteins in liposomes and cells show similar behavior. Proc. Natl. Acad. Sci. USA. 91:12130-12134.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12130-12134
    • Schroeder, R.1    London, E.2    Brown, D.3
  • 42
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and E. Ikonen. 1997. Functional rafts in cell membranes. Nature. 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 43
    • 0024547523 scopus 로고
    • Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts
    • Skibbens, J.E., M.G. Roth, and K.S. Matlin. 1989. Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts. J. Cell Biol. 108:821-832.
    • (1989) J. Cell Biol. , vol.108 , pp. 821-832
    • Skibbens, J.E.1    Roth, M.G.2    Matlin, K.S.3
  • 45
    • 0022898169 scopus 로고
    • Nonpolarized expression of a secreted murine leukemia virus glycoprotein in polarized epithelial cells
    • Stephens, E.B., and R.W. Compans. 1986. Nonpolarized expression of a secreted murine leukemia virus glycoprotein in polarized epithelial cells. Cell. 47:1053-1059.
    • (1986) Cell , vol.47 , pp. 1053-1059
    • Stephens, E.B.1    Compans, R.W.2
  • 46
    • 0027407766 scopus 로고
    • Vesicular stomatitis virus glycoprotein contains a dominant cytoplasmic hasolateral sorting signal critically dependent upon a tyrosine
    • Thomas, D.C., C.B. Brewer, and M.G. Roth. 1993. Vesicular stomatitis virus glycoprotein contains a dominant cytoplasmic hasolateral sorting signal critically dependent upon a tyrosine. J. Biol. Chem. 268:3313-3320.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3313-3320
    • Thomas, D.C.1    Brewer, C.B.2    Roth, M.G.3
  • 47
    • 0028217859 scopus 로고
    • The basolateral targeting signal in the cytoplasmic domain of glycoprotein G from vesicular stomatitis virus resembles a variety of intracellular targeting motifs related by primary sequence hut having diverse targeting activities
    • Thomas, D.C., and M.G. Roth. 1994. The basolateral targeting signal in the cytoplasmic domain of glycoprotein G from vesicular stomatitis virus resembles a variety of intracellular targeting motifs related by primary sequence hut having diverse targeting activities. J. Biol. Chem. 269:15732-15739.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15732-15739
    • Thomas, D.C.1    Roth, M.G.2
  • 49
    • 0025774514 scopus 로고
    • Biosynthesis and secretion of an osteopontin-related 20-kDa polypeptide in the Madin-Darby canine kidney cell line
    • Ullrich, O., K. Mann, W. Haase, and C. Koch-Brandt. 1991. Biosynthesis and secretion of an osteopontin-related 20-kDa polypeptide in the Madin-Darby canine kidney cell line. J. Biol. Chem. 266:3518-3525.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3518-3525
    • Ullrich, O.1    Mann, K.2    Haase, W.3    Koch-Brandt, C.4
  • 50
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley, D.C., and J.J. Skehel. 1987. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56: 365-394.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 51
    • 0030726211 scopus 로고    scopus 로고
    • The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK Cells
    • Yeaman, C., A.H. Le Gall, A.N. Baldwin, L. Monlauzeur, A. Le Bivic, and E. Rodriguez-Boulan. 1997. The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK Cells. J. Cell Biol. 139:929-940.
    • (1997) J. Cell Biol. , vol.139 , pp. 929-940
    • Yeaman, C.1    Le Gall, A.H.2    Baldwin, A.N.3    Monlauzeur, L.4    Le Bivic, A.5    Rodriguez-Boulan, E.6
  • 52
    • 0029879919 scopus 로고    scopus 로고
    • Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells
    • Yoshimori, T., P. Keller, M.G. Roth, and K. Simons. 1996. Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells. J. Cell Biol. 133:247-256.
    • (1996) J. Cell Biol. , vol.133 , pp. 247-256
    • Yoshimori, T.1    Keller, P.2    Roth, M.G.3    Simons, K.4


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