메뉴 건너뛰기




Volumn 109, Issue 6, 1996, Pages 1195-1201

Cell surface expression of a functional rubella virus E1 glycoprotein by addition of a GPI anchor

Author keywords

GPI anchor; Hemagglutinin; Rubella virus (RV)

Indexed keywords

GLYCOSYLPHOSPHATIDYLINOSITOL; PHOSPHOLIPASE D; VIRUS GLYCOPROTEIN;

EID: 0029999173     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (23)

References (50)
  • 1
    • 0024270874 scopus 로고
    • Characterisation of a hydrophilic form of Thy-1 purified from human cerebrospinal fluid
    • Almqvist, P. and Carlsson, S. R. (1988). Characterisation of a hydrophilic form of Thy-1 purified from human cerebrospinal fluid. J. Biol. Chem. 263, 12709-12715.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12709-12715
    • Almqvist, P.1    Carlsson, S.R.2
  • 2
    • 0018330405 scopus 로고
    • Rubella virus maturation and production in two host cell systems
    • Bardeltti, G., Tektoff, J. and Gautheron, D. (1979). Rubella virus maturation and production in two host cell systems. Intervirology 11, 97-103.
    • (1979) Intervirology , vol.11 , pp. 97-103
    • Bardeltti, G.1    Tektoff, J.2    Gautheron, D.3
  • 4
    • 0026596506 scopus 로고
    • Intracellular transport of rubella virus structural proteins expressed from cloned cDNA
    • Baron, M. D., Ebel, T. and Suomalainen, M. (1992). Intracellular transport of rubella virus structural proteins expressed from cloned cDNA. J. Gen. Virol. 73, 1073-1086.
    • (1992) J. Gen. Virol. , vol.73 , pp. 1073-1086
    • Baron, M.D.1    Ebel, T.2    Suomalainen, M.3
  • 5
    • 0027258223 scopus 로고
    • Carboxyl terminus structural requirements for glycosyl-phosphatidylinositol anchor addition to cell surface proteins
    • Beghdadi-Rais, C., Schreyer, M., Rousseaux, M., Borel, P., Eisenberg, R. J., Cohen, G. H., Bron, C. and Fasel, N. (1993). Carboxyl terminus structural requirements for glycosyl-phosphatidylinositol anchor addition to cell surface proteins. J. Cell Sci. 105, 831-840
    • (1993) J. Cell Sci. , vol.105 , pp. 831-840
    • Beghdadi-Rais, C.1    Schreyer, M.2    Rousseaux, M.3    Borel, P.4    Eisenberg, R.J.5    Cohen, G.H.6    Bron, C.7    Fasel, N.8
  • 6
    • 0025891401 scopus 로고
    • Glycolipid-anchored membrane proteins
    • Bron, C. and Fasel, N. (1991). Glycolipid-anchored membrane proteins. Bull Inst. Pasteur 89, 59-69.
    • (1991) Bull Inst. Pasteur , vol.89 , pp. 59-69
    • Bron, C.1    Fasel, N.2
  • 7
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D. and Rose, J. K. (1992). Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533-544
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.1    Rose, J.K.2
  • 8
    • 0026685052 scopus 로고
    • Localization of the virus neutralizing and hemagglutinin epitopes of E1 glycoprotein of rubella virus
    • Chaye, H., Chong, P., Tripet, B., Brush, B. and Gillam, S. (1992). Localization of the virus neutralizing and hemagglutinin epitopes of E1 glycoprotein of rubella virus Virology 189, 483-492.
    • (1992) Virology , vol.189 , pp. 483-492
    • Chaye, H.1    Chong, P.2    Tripet, B.3    Brush, B.4    Gillam, S.5
  • 9
    • 0023655970 scopus 로고
    • Glycolipid anchors are attached to Thy-1 glycoprotein rapidly after translation
    • Conzelmann, A., Spiazzi, A. and Bron, C. (1987) Glycolipid anchors are attached to Thy-1 glycoprotein rapidly after translation. Biochem. J 246, 605-610.
    • (1987) Biochem. J , vol.246 , pp. 605-610
    • Conzelmann, A.1    Spiazzi, A.2    Bron, C.3
  • 10
    • 0028110022 scopus 로고
    • Mutational analysis of polymeric immunoglobulin receptor/ligand interactions
    • Coyne, R. S., Siebrecht, M., Peitsch, M. C. and Casanova, J. E. (1994). Mutational analysis of polymeric immunoglobulin receptor/ligand interactions. J. Biol. Chem. 269, 31620-31625.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31620-31625
    • Coyne, R.S.1    Siebrecht, M.2    Peitsch, M.C.3    Casanova, J.E.4
  • 11
    • 0024455507 scopus 로고
    • Oligomerization of glycolipid-anchored and soluble forms of the vesicular stomatitis virus glycoprotein
    • Crise, B., Ruusala, A., Zagouras, P., Shaw, A. and Rose, J. K. (1989). Oligomerization of glycolipid-anchored and soluble forms of the vesicular stomatitis virus glycoprotein. J. Virol. 63, 5328-5333.
    • (1989) J. Virol. , vol.63 , pp. 5328-5333
    • Crise, B.1    Ruusala, A.2    Zagouras, P.3    Shaw, A.4    Rose, J.K.5
  • 12
    • 0025203675 scopus 로고
    • Glycolipid anchoring of plasma membrane proteins
    • Cross, G. A. M. (1990). Glycolipid anchoring of plasma membrane proteins. Annu. Rev. Cell Biol. 6, 1-39.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 1-39
    • Cross, G.A.M.1
  • 13
    • 0022465626 scopus 로고
    • Release of decay-accelerating factor (DAF) from the cell membrane by phosphatidylinositol-specific phospholipase C (PI-PLC): Selective modification of a complement regulatory protein
    • Davitz, M. A., Low, M. G. and Nussenzweig, V. (1986). Release of decay-accelerating factor (DAF) from the cell membrane by phosphatidylinositol-specific phospholipase C (PI-PLC): Selective modification of a complement regulatory protein. J. Exp. Med 163, 1150.
    • (1986) J. Exp. Med , vol.163 , pp. 1150
    • Davitz, M.A.1    Low, M.G.2    Nussenzweig, V.3
  • 14
    • 0025287319 scopus 로고
    • Sequence of the genome RNA of rubella virus: Evidence for genetic rearrangement during togavirus evolution
    • Dominguez, G., Wang, C.-Y. and Frey, T. K. (1990). Sequence of the genome RNA of rubella virus: evidence for genetic rearrangement during togavirus evolution. Virology 177, 225-238.
    • (1990) Virology , vol.177 , pp. 225-238
    • Dominguez, G.1    Wang, C.-Y.2    Frey, T.K.3
  • 15
    • 0026555240 scopus 로고
    • Multi-level regulation of Thy-1 antigen expression in mouse T lymphomas
    • Fasel, N. J. and Déglon, N. (1992). Multi-level regulation of Thy-1 antigen expression in mouse T lymphomas. Immunogenetics 35, 126-130.
    • (1992) Immunogenetics , vol.35 , pp. 126-130
    • Fasel, N.J.1    Déglon, N.2
  • 16
    • 0023944337 scopus 로고
    • Cell-surface anchoring of proteins via glycosylphosphatidylinositol structures
    • Ferguson, M. A. J. and Williams, A. F. (1988). Cell-surface anchoring of proteins via glycosylphosphatidylinositol structures. Annu. Rev. Biochem. 57, 285-320
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 285-320
    • Ferguson, M.A.J.1    Williams, A.F.2
  • 17
    • 0027241128 scopus 로고
    • Characterization of structural and functional phosphoinositide domains in human erythrocyte membranes
    • Gascard, P., Sauvage, M., Sulpice, J.-C. and Giraud, F. (1993). Characterization of structural and functional phosphoinositide domains in human erythrocyte membranes Biochemistry 32, 5941-5948.
    • (1993) Biochemistry , vol.32 , pp. 5941-5948
    • Gascard, P.1    Sauvage, M.2    Sulpice, J.-C.3    Giraud, F.4
  • 18
    • 0022636135 scopus 로고
    • Rubella virus antigen: Localization of epitopes involved in hemagglutuiation and neutralization by using monoclonal antibodies
    • Green, K. Y. and Dorsett, P. H. (1986). Rubella virus antigen: localization of epitopes involved in hemagglutuiation and neutralization by using monoclonal antibodies. J. Virol. 57, 893-898.
    • (1986) J. Virol. , vol.57 , pp. 893-898
    • Green, K.Y.1    Dorsett, P.H.2
  • 19
    • 0026775265 scopus 로고
    • The rubella virus E1 glycoprotein is arrested in a novel post-ER, pre-Golgi compartment
    • Hobman, T. C., Woodward, L. and Farquhar, M. G. (1992). The rubella virus E1 glycoprotein is arrested in a novel post-ER, pre-Golgi compartment. J. Cell Biol. 118, 795-811.
    • (1992) J. Cell Biol. , vol.118 , pp. 795-811
    • Hobman, T.C.1    Woodward, L.2    Farquhar, M.G.3
  • 20
    • 0027469910 scopus 로고
    • The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex
    • Hobman, T. C., Woodward, L. and Farquhar, M. G. (1993). The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex. J. Cell Biol. 121, 269-281.
    • (1993) J. Cell Biol. , vol.121 , pp. 269-281
    • Hobman, T.C.1    Woodward, L.2    Farquhar, M.G.3
  • 21
    • 0028065160 scopus 로고
    • Assembly of rubella virus structural proteins into virus-like particles in transfected cells
    • Hobman, T. C., Lundstrom, M. L., Mauracher, C. A., Woodward, L., Gillam, S. and Farquhar, M. G. (1994a). Assembly of rubella virus structural proteins into virus-like particles in transfected cells. Virology 202, 574-585.
    • (1994) Virology , vol.202 , pp. 574-585
    • Hobman, T.C.1    Lundstrom, M.L.2    Mauracher, C.A.3    Woodward, L.4    Gillam, S.5    Farquhar, M.G.6
  • 22
    • 0028266760 scopus 로고
    • Expression of soluble forms of rubella virus glycoproteins in mammalian cells
    • Hobman, T. C., Seto, N. O. L. and Gillam, S. (1994b). Expression of soluble forms of rubella virus glycoproteins in mammalian cells. Virus Res. 31, 277-289.
    • (1994) Virus Res. , vol.31 , pp. 277-289
    • Hobman, T.C.1    Seto, N.O.L.2    Gillam, S.3
  • 23
    • 0029064295 scopus 로고
    • Targeting of a heterodimeric membrane protein complex to the Golgi: Rubella virus E2 glycoprotein contains a transmembrane Golgi retention signal
    • Hobman, T. C., Woodward, L. and Farquhar, M. G. (1995). Targeting of a heterodimeric membrane protein complex to the Golgi: Rubella virus E2 glycoprotein contains a transmembrane Golgi retention signal. Mol. Biol Cell 6, 7-20.
    • (1995) Mol. Biol Cell , vol.6 , pp. 7-20
    • Hobman, T.C.1    Woodward, L.2    Farquhar, M.G.3
  • 24
    • 0024988572 scopus 로고
    • Complete and partial glycophospholipid anchors are found on a fusion protein consisting of luteinizing hormone β subunit followed by a carboxyl-terminal domain of Thy-1
    • Kaetzel, D. M., Singh, N., Kennedy, G. C., Virgin, J. B., Farr, G., Kitagawa, Y., Nilson, J. H. and Tartakoff, A. M. (1990). Complete and partial glycophospholipid anchors are found on a fusion protein consisting of luteinizing hormone β subunit followed by a carboxyl-terminal domain of Thy-1. J. Biol. Chem. 265, 15932-15937.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15932-15937
    • Kaetzel, D.M.1    Singh, N.2    Kennedy, G.C.3    Virgin, J.B.4    Farr, G.5    Kitagawa, Y.6    Nilson, J.H.7    Tartakoff, A.M.8
  • 25
    • 0025102021 scopus 로고
    • Expression of T cell antigen receptor heterodimers in a lipid-linked form
    • Lin, A. Y., Devaux, B., Green, A., Sagerström, C., Elliott, J. and Davis, M. M. (1990). Expression of T cell antigen receptor heterodimers in a lipid-linked form. Science 249, 677-679.
    • (1990) Science , vol.249 , pp. 677-679
    • Lin, A.Y.1    Devaux, B.2    Green, A.3    Sagerström, C.4    Elliott, J.5    Davis, M.M.6
  • 26
    • 0023795425 scopus 로고
    • Cell-specific heterogeneity in sensitivity of phosphatidylinositol-anchored membrane antigens to release by phospholipase C
    • Low, M. G., Stiernberg, J., Waneck, G. L., Flavell, R. A. and Kincade, P. W. (1988). Cell-specific heterogeneity in sensitivity of phosphatidylinositol-anchored membrane antigens to release by phospholipase C. J. Immunol. Meth. 113, 101-111.
    • (1988) J. Immunol. Meth. , vol.113 , pp. 101-111
    • Low, M.G.1    Stiernberg, J.2    Waneck, G.L.3    Flavell, R.A.4    Kincade, P.W.5
  • 27
    • 0023879525 scopus 로고
    • Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding
    • Machamer, C. E. and Rose, J. K. (1988). Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding. J. Biol. Chem. 263, 5955-5960.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5955-5960
    • Machamer, C.E.1    Rose, J.K.2
  • 28
    • 0025049127 scopus 로고
    • The E1 glycoprotein of an avian coronavirus is targeted to the cis Golgi complex
    • Machamer, C. E., Mentone, S. A., Rose, J. K. and Farquhar, M. G. (1990). The E1 glycoprotein of an avian coronavirus is targeted to the cis Golgi complex. Proc Nat. Acad. Sci. USA 87, 6944-6948.
    • (1990) Proc Nat. Acad. Sci. USA , vol.87 , pp. 6944-6948
    • Machamer, C.E.1    Mentone, S.A.2    Rose, J.K.3    Farquhar, M.G.4
  • 29
    • 0027964967 scopus 로고
    • A signal for Golgi retention in the bunyavirus G1 glycoprotein
    • Matsuoka, Y., Chen, S.-Y. and Compans, R. W. (1994). A signal for Golgi retention in the bunyavirus G1 glycoprotein. J. Biol. Chem. 269, 22565-22573.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22565-22573
    • Matsuoka, Y.1    Chen, S.-Y.2    Compans, R.W.3
  • 30
    • 8944255050 scopus 로고
    • Physiological cleavage of the glycosylphosphatidylinositol (GPI)-anchored protein, decay accelerating factor (DAF) by a GPI-specific phospholipase D (GPI-PLD)
    • Metz, C. N., Choi, N. H., Garas, I. W., Patel, S. R., Altszuler, N. and Davitz, M. A. (1993). Physiological cleavage of the glycosylphosphatidylinositol (GPI)-anchored protein, decay accelerating factor (DAF) by a GPI-specific phospholipase D (GPI-PLD). FASEB J. 7, A1049.
    • (1993) FASEB J. , vol.7
    • Metz, C.N.1    Choi, N.H.2    Garas, I.W.3    Patel, S.R.4    Altszuler, N.5    Davitz, M.A.6
  • 32
    • 0025932246 scopus 로고
    • A non-functional sequence converted to a signal for glycophosphatidylinositol membrane anchor attachment
    • Moran, P. and Caras, I. W. (1991). A non-functional sequence converted to a signal for glycophosphatidylinositol membrane anchor attachment. J. Cell Biol. 115, 329-336.
    • (1991) J. Cell Biol. , vol.115 , pp. 329-336
    • Moran, P.1    Caras, I.W.2
  • 33
    • 0026488395 scopus 로고
    • Proteins containing an uncleaved signal for glycophosphatidylinositol membrane anchor attachment are retained in a post-ER compartment
    • Moran, P. and Caras, I. W. (1992). Proteins containing an uncleaved signal for glycophosphatidylinositol membrane anchor attachment are retained in a post-ER compartment. J. Cell Biol. 119, 763-772.
    • (1992) J. Cell Biol. , vol.119 , pp. 763-772
    • Moran, P.1    Caras, I.W.2
  • 34
    • 0026153377 scopus 로고
    • Structure and antigenic activity of rubella E1 glycoprotein synthetic peptides
    • Neri, P., Corti, M., Lozzi, L. and Valensin, P. E. (1991). Structure and antigenic activity of rubella E1 glycoprotein synthetic peptides. Biopolymers 31, 631-635.
    • (1991) Biopolymers , vol.31 , pp. 631-635
    • Neri, P.1    Corti, M.2    Lozzi, L.3    Valensin, P.E.4
  • 35
    • 0026760902 scopus 로고
    • Improved indirect fluorescence immunocytochemical method using counterstains
    • Newkirk, R. F. and Mack, J. (1992). Improved indirect fluorescence immunocytochemical method using counterstains. BioTechniques 13, 536-538.
    • (1992) BioTechniques , vol.13 , pp. 536-538
    • Newkirk, R.F.1    Mack, J.2
  • 36
    • 0020577797 scopus 로고
    • Rubella virus contains one capsid protein and three envelope glycoproteins, E1, E2a and E2b
    • Oker-Blom, C., Kalkkinen, N., Kaarianen, L. and Pettersson, R. F. (1983). Rubella virus contains one capsid protein and three envelope glycoproteins, E1, E2a and E2b. J. Virol. 46, 964-973.
    • (1983) J. Virol. , vol.46 , pp. 964-973
    • Oker-Blom, C.1    Kalkkinen, N.2    Kaarianen, L.3    Pettersson, R.F.4
  • 37
    • 0026076805 scopus 로고
    • Protein localization and virus assembly at intracellular membranes
    • Pettersson, R. F. (1991). Protein localization and virus assembly at intracellular membranes. Curr. Top. Microbiol. Immunol 170, 67-106.
    • (1991) Curr. Top. Microbiol. Immunol , vol.170 , pp. 67-106
    • Pettersson, R.F.1
  • 38
    • 0020398151 scopus 로고
    • Expression from cloned cDNA of cell-surface secreted forms of the glycoprotein of vesicular stomatitis virus in eucaryotic cells
    • Rose, J. K. and Bergmann, J. E. (1982). Expression from cloned cDNA of cell-surface secreted forms of the glycoprotein of vesicular stomatitis virus in eucaryotic cells. Cell 30, 753-762.
    • (1982) Cell , vol.30 , pp. 753-762
    • Rose, J.K.1    Bergmann, J.E.2
  • 39
    • 0027249613 scopus 로고
    • Expression and characterization of glycophospholipid-anchored human immunodeficiency virus type 1 envelope glycoproteins
    • Salzwedel, K., Johnston, P. B., Roberts, S. J., Dubay, J. W. and Hunter, E. (1993). Expression and characterization of glycophospholipid-anchored human immunodeficiency virus type 1 envelope glycoproteins. J. Virol. 67, 5279-5288
    • (1993) J. Virol. , vol.67 , pp. 5279-5288
    • Salzwedel, K.1    Johnston, P.B.2    Roberts, S.J.3    Dubay, J.W.4    Hunter, E.5
  • 40
    • 0021913633 scopus 로고
    • Lines of BPV-transformed murine cells that constitutively express influenza virus hemagglutinin
    • Sambrook, J., Rodgers, L., White, J. and Gething, M.-J. (1985). Lines of BPV-transformed murine cells that constitutively express influenza virus hemagglutinin. EMBO J. 4, 91-103.
    • (1985) EMBO J. , vol.4 , pp. 91-103
    • Sambrook, J.1    Rodgers, L.2    White, J.3    Gething, M.-J.4
  • 41
    • 0025847074 scopus 로고
    • Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D
    • Scallon, B. J., Fung, W.-J. C., Tsang, T. C., Li, S., Kado-Fong, H., Huang, K.-S. and Kochan, J. P. (1991). Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D. Science 252, 446-448.
    • (1991) Science , vol.252 , pp. 446-448
    • Scallon, B.J.1    Fung, W.-J.C.2    Tsang, T.C.3    Li, S.4    Kado-Fong, H.5    Huang, K.-S.6    Kochan, J.P.7
  • 42
    • 0028114828 scopus 로고
    • Expression and characterization of a soluble rubella virus E1 envelope protein
    • Seto, N. O. L. and Gillam, S. (1994). Expression and characterization of a soluble rubella virus E1 envelope protein. J. Med. Virol. 44, 192-199.
    • (1994) J. Med. Virol. , vol.44 , pp. 192-199
    • Seto, N.O.L.1    Gillam, S.2
  • 43
    • 0025037651 scopus 로고
    • Intracellular transport of soluble and membrane-bound glycoproteins: Folding, assembly and secretion of anchor-free influenza hemagglutinin
    • Singh, I., Doms, R. W., Wagner, K. R. and Helenius, A. (1990). Intracellular transport of soluble and membrane-bound glycoproteins: folding, assembly and secretion of anchor-free influenza hemagglutinin. EMBO J. 9, 631-639.
    • (1990) EMBO J. , vol.9 , pp. 631-639
    • Singh, I.1    Doms, R.W.2    Wagner, K.R.3    Helenius, A.4
  • 44
    • 0025940737 scopus 로고
    • A Golgi retention signal in a membrane-spanning domain of coronavirus. E1 protein
    • Swift, A. M. and Machamer, C. E. (1991). A Golgi retention signal in a membrane-spanning domain of coronavirus. E1 protein. J. Cell Biol. 115, 19-30.
    • (1991) J. Cell Biol. , vol.115 , pp. 19-30
    • Swift, A.M.1    Machamer, C.E.2
  • 46
    • 0024593699 scopus 로고
    • Addition of high-mannose sugars must precede disulfide bond formation for proper folding of Sendai virus glycoprotein
    • Vidal, S., Motter, G., Kolakofsky, D. and Roux, L. (1989). Addition of high-mannose sugars must precede disulfide bond formation for proper folding of Sendai virus glycoprotein. J. Virol. 63, 892-900.
    • (1989) J. Virol. , vol.63 , pp. 892-900
    • Vidal, S.1    Motter, G.2    Kolakofsky, D.3    Roux, L.4
  • 47
    • 0014549112 scopus 로고
    • Growth of rubella virus in BHK-21 cells: Electron microscopy of morphogenesis
    • von Bonsdorff, C. and Vaheri, A. (1969). Growth of rubella virus in BHK-21 cells: electron microscopy of morphogenesis. J. Gen. Virol. 5, 47-51.
    • (1969) J. Gen. Virol. , vol.5 , pp. 47-51
    • Von Bonsdorff, C.1    Vaheri, A.2
  • 48
    • 0021996319 scopus 로고
    • Detailed immunologic analysis of the structural polypeptides of rubella virus using monoclonal antibodies
    • Waxham, M. N. and Wolinsky, J. S. (1985). Detailed immunologic analysis of the structural polypeptides of rubella virus using monoclonal antibodies. Virology 143, 153-165.
    • (1985) Virology , vol.143 , pp. 153-165
    • Waxham, M.N.1    Wolinsky, J.S.2
  • 49
    • 0027500352 scopus 로고
    • An antibody- and synthetic peptide-defined rubella virus E1 glycoprotein neutralization domain
    • Wolinsky, J. S., Sukholutsky, E., Moore, W. T., Lovett, A., McCarthy, M. and Adame, B. (1993). An antibody- and synthetic peptide-defined rubella virus E1 glycoprotein neutralization domain. J. Virol. 67, 961-968.
    • (1993) J. Virol. , vol.67 , pp. 961-968
    • Wolinsky, J.S.1    Sukholutsky, E.2    Moore, W.T.3    Lovett, A.4    McCarthy, M.5    Adame, B.6
  • 50
    • 0028107582 scopus 로고
    • Expression and secretion of glycosylphosphatidylinositol-specific phospholipase D by myeloid cell lines
    • Xie, M. and Low, M. G. (1994). Expression and secretion of glycosylphosphatidylinositol-specific phospholipase D by myeloid cell lines. Biochem J. 297, 547-554.
    • (1994) Biochem J. , vol.297 , pp. 547-554
    • Xie, M.1    Low, M.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.