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Volumn 124, Issue 4, 2011, Pages 578-588

Annexin A1 is a new functional linker between actin filaments and phagosomes during phagocytosis

Author keywords

Annexin A1; F actin; LBP; Phagocytosis

Indexed keywords

CALCIUM ION; F ACTIN; LIPOCORTIN 1;

EID: 79951847407     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.076208     Document Type: Article
Times cited : (39)

References (69)
  • 1
    • 0037067651 scopus 로고    scopus 로고
    • How to eat something bigger than your head
    • Aderem, A. (2002). How to eat something bigger than your head. Cell 110, 5-8.
    • (2002) Cell , vol.110 , pp. 5-8
    • Aderem, A.1
  • 2
    • 0033046220 scopus 로고    scopus 로고
    • Mechanisms of phagocytosis in macrophages
    • Aderem, A. and Underhill, D. M. (1999). Mechanisms of phagocytosis in macrophages. Annu. Rev. Immunol. 17, 593-623.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 593-623
    • Aderem, A.1    Underhill, D.M.2
  • 5
    • 0029829896 scopus 로고    scopus 로고
    • Molecular definition of distinct cytoskeletal structures involved in complement- And Fc receptor-mediated phagocytosis in macrophages
    • Allen, L. A. and Aderem, A. (1996). Molecular definition of distinct cytoskeletal structures involved in complement- and Fc receptor-mediated phagocytosis in macrophages. J. Exp. Med. 184, 627-637.
    • (1996) J. Exp. Med. , vol.184 , pp. 627-637
    • Allen, L.A.1    Aderem, A.2
  • 7
    • 0030987790 scopus 로고    scopus 로고
    • Effects of profilin-annexin I association on some properties of both profilin and annexin I: Modification of the inhibitory activity of profilin on actin polymerization and inhibition of the self-association of annexin I and its interactions with liposomes
    • Alvarez-Martinez, M. T., Porte, F., Liautard, J. P. and Sri, W. J. (1997). Effects of profilin-annexin I association on some properties of both profilin and annexin I: modification of the inhibitory activity of profilin on actin polymerization and inhibition of the self-association of annexin I and its interactions with liposomes. Biochim. Biophys. Acta 1339, 331-340.
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 331-340
    • Alvarez-Martinez, M.T.1    Porte, F.2    Liautard, J.P.3    Sri, W.J.4
  • 8
    • 0015222181 scopus 로고
    • Quantitative comparison of the binding of various glycolytic enzymes to F-actin and the interaction of aldolase with G-actin
    • Arnold, H., Henning, R. and Pette, D. (1971). Quantitative comparison of the binding of various glycolytic enzymes to F-actin and the interaction of aldolase with G-actin. Eur. J. Biochem. 22, 121-126.
    • (1971) Eur. J. Biochem. , vol.22 , pp. 121-126
    • Arnold, H.1    Henning, R.2    Pette, D.3
  • 9
    • 0028072134 scopus 로고
    • Interactions of eukaryotic elongation factor 2 with actin: A possible link between protein synthetic machinery and cytoskeleton
    • DOI 10.1016/0014-5793(94)01239-3
    • Bektas, M., Nurten, R., Gurel, Z., Sayers, Z. and Bermek, E. (1994). Interactions of eukaryotic elongation factor 2 with actin: a possible link between protein synthetic machinery and cytoskeleton. FEBS Lett. 356, 89-93. (Pubitemid 24374039)
    • (1994) FEBS Letters , vol.356 , Issue.1 , pp. 89-93
    • Bektas, M.1
  • 10
    • 0347753248 scopus 로고    scopus 로고
    • AHNAK interaction with the annexin 2/S100A10 complex regulates cell membrane cytoarchitecture
    • DOI 10.1083/jcb.200307098
    • Benaud, C., Gentil, B. J., Assard, N., Court, M., Garin, J., Delphin, C. and Baudier, J. (2004). AHNAK interaction with the annexin 2/S100A10 complex regulates cell membrane cytoarchitecture. J. Cell Biol. 164, 133-144. (Pubitemid 38082464)
    • (2004) Journal of Cell Biology , vol.164 , Issue.1 , pp. 133-144
    • Benaud, C.1    Gentil, B.J.2    Assard, N.3    Court, M.4    Garin, J.5    Delphin, C.6    Baudier, J.7
  • 11
    • 0025195030 scopus 로고
    • Characterization of Ca2(+)-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins
    • Blackwood, R. A. and Ernst, J. D. (1990). Characterization of Ca2(+)-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins. Biochem. J. 266, 195-200.
    • (1990) Biochem. J. , vol.266 , pp. 195-200
    • Blackwood, R.A.1    Ernst, J.D.2
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 0034524664 scopus 로고    scopus 로고
    • ERM-Merlin and EBP50 protein families in plasma membrane organization and function
    • Bretscher, A., Chambers, D., Nguyen, R. and Reczek, D. (2000). ERM-Merlin and EBP50 protein families in plasma membrane organization and function. Annu. Rev. Cell Dev. Biol. 16, 113-143.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 113-143
    • Bretscher, A.1    Chambers, D.2    Nguyen, R.3    Reczek, D.4
  • 14
    • 0032573378 scopus 로고    scopus 로고
    • Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases
    • Caron, E. and Hall, A. (1998). Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases. Science 282, 1717-1721. (Pubitemid 28549289)
    • (1998) Science , vol.282 , Issue.5394 , pp. 1717-1721
    • Caron, E.1    Hall, A.2
  • 17
    • 51349140308 scopus 로고    scopus 로고
    • Annexin-A1: A pivotal regulator of the innate and adaptive immune systems
    • D'Acquisto, F., Perretti, M. and Flower, R. J. (2008). Annexin-A1: a pivotal regulator of the innate and adaptive immune systems. Br. J. Pharmacol. 155, 152-169.
    • (2008) Br. J. Pharmacol. , vol.155 , pp. 152-169
    • D'Acquisto, F.1    Perretti, M.2    Flower, R.J.3
  • 21
    • 0028328732 scopus 로고
    • Biogenesis of phagolysosomes proceeds through a sequential series of interactions with the endocytic apparatus
    • Desjardins, M., Huber, L. A., Parton, R. G. and Griffiths, G. (1994b). Biogenesis of phagolysosomes proceeds through a sequential series of interactions with the endocytic apparatus. J. Cell Biol. 124, 677-688. (Pubitemid 24085778)
    • (1994) Journal of Cell Biology , vol.124 , Issue.5 , pp. 677-688
    • Desjardins, M.1    Huber, L.A.2    Parton, R.G.3    Griffiths, G.4
  • 23
    • 0036175145 scopus 로고    scopus 로고
    • Dynamics of cytoskeletal proteins during Fcgamma receptor-mediated phagocytosis in macrophages
    • Diakonova, M., Bokoch, G. and Swanson, J. A. (2002). Dynamics of cytoskeletal proteins during Fcgamma receptor-mediated phagocytosis in macrophages. Mol. Biol. Cell 13, 402-411.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 402-411
    • Diakonova, M.1    Bokoch, G.2    Swanson, J.A.3
  • 24
    • 0036359281 scopus 로고    scopus 로고
    • Moonlighting functions of polypeptide elongation factor 1, from actin bundling to zinc finger protein R1-associated nuclear localization
    • Ejiri, S. (2002). Moonlighting functions of polypeptide elongation factor 1, from actin bundling to zinc finger protein R1-associated nuclear localization. Biosci. Biotechnol. Biochem. 66, 1-21.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1-21
    • Ejiri, S.1
  • 25
    • 0032969183 scopus 로고    scopus 로고
    • Myosin light chain kinase from skeletal muscle regulates an ATP-dependent interaction between actin and myosin by binding to actin
    • Fujita, K., Ye, L. H., Sato, M., Okagaki, T., Nagamachi, Y. and Kohama, K. (1999). Myosin light chain kinase from skeletal muscle regulates an ATP-dependent interaction between actin and myosin by binding to actin. Mol. Cell Biochem. 190, 85-90.
    • (1999) Mol. Cell Biochem. , vol.190 , pp. 85-90
    • Fujita, K.1    Ye, L.H.2    Sato, M.3    Okagaki, T.4    Nagamachi, Y.5    Kohama, K.6
  • 26
    • 34447543021 scopus 로고    scopus 로고
    • Annexins and endocytosis
    • DOI 10.1111/j.1600-0854.2007.00590.x
    • Futter, C. E. and White, I. J. (2007). Annexins and endocytosis. Traffic. 8, 951-958. (Pubitemid 47074030)
    • (2007) Traffic , vol.8 , Issue.8 , pp. 951-958
    • Futter, C.E.1    White, I.J.2
  • 27
    • 0021299594 scopus 로고
    • Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and F-actin
    • Gerke, V. and Weber, K. (1984). Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and F-actin. EMBO J. 3, 227-233.
    • (1984) EMBO J. , vol.3 , pp. 227-233
    • Gerke, V.1    Weber, K.2
  • 28
    • 20344369564 scopus 로고    scopus 로고
    • Annexins: Linking Ca2+ signalling to membrane dynamics
    • Gerke, V., Creutz, C. E. and Moss, S. E. (2005). Annexins: linking Ca2+ signalling to membrane dynamics. Nat. Rev. Mol. Cell. Biol. 6, 449-461.
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 449-461
    • Gerke, V.1    Creutz, C.E.2    Moss, S.E.3
  • 29
    • 0023139338 scopus 로고
    • Calpactins: Two distinct Ca++- Regulated phospholipid- and actin-binding proteins isolated from lung and placenta
    • Glenney, J. R., Jr, Tack, B. and Powell, M. A. (1987). Calpactins: two distinct Ca++- regulated phospholipid- and actin-binding proteins isolated from lung and placenta. J. Cell Biol. 104, 503-511.
    • (1987) J. Cell Biol. , vol.104 , pp. 503-511
    • Glenney Jr., J.R.1    Tack, B.2    Powell, M.A.3
  • 31
    • 0025666318 scopus 로고
    • Colocalization of F-actin and talin during Fc receptor-mediated phagocytosis in mouse macrophages
    • Greenberg, S., Burridge, K. and Silverstein, S. C. (1990). Colocalization of F-actin and talin during Fc receptor-mediated phagocytosis in mouse macrophages. J. Exp. Med. 172, 1853-1856.
    • (1990) J. Exp. Med. , vol.172 , pp. 1853-1856
    • Greenberg, S.1    Burridge, K.2    Silverstein, S.C.3
  • 32
    • 34250169069 scopus 로고    scopus 로고
    • Phagosome proteomes open the way to a better understanding of phagosome function
    • Griffiths, G. and Mayorga, L. (2007). Phagosome proteomes open the way to a better understanding of phagosome function. Genome Biol. 8, 207.
    • (2007) Genome Biol. , vol.8 , pp. 207
    • Griffiths, G.1    Mayorga, L.2
  • 33
    • 33947194392 scopus 로고    scopus 로고
    • The phagosome: Compartment with a license to kill
    • Haas, A. (2007). The phagosome: compartment with a license to kill. Traffic. 8, 311-330.
    • (2007) Traffic , vol.8 , pp. 311-330
    • Haas, A.1
  • 35
    • 0029922802 scopus 로고    scopus 로고
    • Distribution of annexin I during non-pathogen or pathogen phagocytosis by confocal imaging and immunogold electron microscopy
    • Harricane, M. C., Caron, E., Porte, F. and Liautard, J. P. (1996). Distribution of annexin I during non-pathogen or pathogen phagocytosis by confocal imaging and immunogold electron microscopy. Cell Biol. Int. 20, 193-203.
    • (1996) Cell Biol. Int. , vol.20 , pp. 193-203
    • Harricane, M.C.1    Caron, E.2    Porte, F.3    Liautard, J.P.4
  • 37
  • 38
    • 0029948679 scopus 로고    scopus 로고
    • Translocation of annexin I to plasma membranes and phagosomes in human neutrophils upon stimulation with opsonized zymosan: Possible role in phagosome function
    • Kaufman, M., Leto, T. and Levy, R. (1996). Translocation of annexin I to plasma membranes and phagosomes in human neutrophils upon stimulation with opsonized zymosan: possible role in phagosome function. Biochem. J. 316, 35-42. (Pubitemid 26158199)
    • (1996) Biochemical Journal , vol.316 , Issue.1 , pp. 35-42
    • Kaufman, M.1    Leto, T.2    Levy, R.3
  • 39
    • 0033575216 scopus 로고    scopus 로고
    • Disturbed communication between actin- And nucleotide-binding sites in a myosin II with truncated 50/20-kDa junction
    • Knetsch, M. L., Uyeda, T. Q. and Manstein, D. J. (1999). Disturbed communication between actin- and nucleotide-binding sites in a myosin II with truncated 50/20-kDa junction. J. Biol. Chem. 274, 20133-20138.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20133-20138
    • Knetsch, M.L.1    Uyeda, T.Q.2    Manstein, D.J.3
  • 41
    • 0034885789 scopus 로고    scopus 로고
    • Implication of annexin 1 in phagocytosis: Effects of n-terminal domain deletions and point mutations of the phosphorylation site Ser-27
    • Kusumawati, A., Liautard, J. P. and Sri, W. J. (2001). Implication of annexin 1 in phagocytosis: effects of n-terminal domain deletions and point mutations of the phosphorylation site Ser-27. Cell Biol. Int. 25, 809-813.
    • (2001) Cell Biol. Int. , vol.25 , pp. 809-813
    • Kusumawati, A.1    Liautard, J.P.2    Sri, W.J.3
  • 42
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 43
    • 70350005334 scopus 로고    scopus 로고
    • Transient assembly of F-actin by phagosomes delays phagosome fusion with lysosomes in cargo-overloaded macrophages
    • Liebl, D. and Griffiths, G. (2009). Transient assembly of F-actin by phagosomes delays phagosome fusion with lysosomes in cargo-overloaded macrophages. J. Cell Sci. 122, 2935-2945.
    • (2009) J. Cell Sci. , vol.122 , pp. 2935-2945
    • Liebl, D.1    Griffiths, G.2
  • 44
    • 33947678705 scopus 로고    scopus 로고
    • Annexin 1: The new face of an old molecule
    • DOI 10.1096/fj.06-7464rev
    • Lim, L. H. and Pervaiz, S. (2007). Annexin 1, the new face of an old molecule. FASEB J. 21, 968-975. (Pubitemid 46495688)
    • (2007) FASEB Journal , vol.21 , Issue.4 , pp. 968-975
    • Lim, L.H.K.1    Pervaiz, S.2
  • 45
    • 34147130534 scopus 로고    scopus 로고
    • Differential protein expression of murine macrophages upon interaction with Candida albicans
    • Martinez-Solano, L., Nombela, C., Molero, G. and Gil, C. (2006). Differential protein expression of murine macrophages upon interaction with Candida albicans. Proteomics 6, S133-S144.
    • (2006) Proteomics , vol.6
    • Martinez-Solano, L.1    Nombela, C.2    Molero, G.3    Gil, C.4
  • 46
    • 0035067475 scopus 로고    scopus 로고
    • Phagocytosis and the actin cytoskeleton
    • May, R. C. and Machesky, L. M. (2001). Phagocytosis and the actin cytoskeleton. J. Cell Sci. 114, 1061-1077.
    • (2001) J. Cell Sci. , vol.114 , pp. 1061-1077
    • May, R.C.1    Machesky, L.M.2
  • 47
    • 52449105700 scopus 로고    scopus 로고
    • S100-annexin complexes-biology of conditional association
    • Miwa, N., Uebi, T. and Kawamura, S. (2008). S100-annexin complexes-biology of conditional association. FEBS J. 275, 4945-4955.
    • (2008) FEBS J. , vol.275 , pp. 4945-4955
    • Miwa, N.1    Uebi, T.2    Kawamura, S.3
  • 48
    • 59449109685 scopus 로고    scopus 로고
    • Annexin A2 binding to endosomes and functions in endosomal transport are regulated by tyrosine 23 phosphorylation
    • Morel, E. and Gruenberg, J. (2009). Annexin A2 binding to endosomes and functions in endosomal transport are regulated by tyrosine 23 phosphorylation. J. Biol. Chem. 284, 1604-1611.
    • (2009) J. Biol. Chem. , vol.284 , pp. 1604-1611
    • Morel, E.1    Gruenberg, J.2
  • 49
    • 0033373785 scopus 로고    scopus 로고
    • Isolation and characterization of monoclonal antibodies directed against novel components of macrophage phagosomes
    • Morrissette, N. S., Gold, E. S., Guo, J., Hamerman, J. A., Ozinsky, A., Bedian, V. and Aderem, A. A. (1999). Isolation and characterization of monoclonal antibodies directed against novel components of macrophage phagosomes. J. Cell Sci. 112, 4705-4713.
    • (1999) J. Cell Sci. , vol.112 , pp. 4705-4713
    • Morrissette, N.S.1    Gold, E.S.2    Guo, J.3    Hamerman, J.A.4    Ozinsky, A.5    Bedian, V.6    Aderem, A.A.7
  • 50
    • 0003988303 scopus 로고
    • London: Protland Press Limited
    • Moss, E. (1992). The Annexins. London: Protland Press Limited.
    • (1992) The Annexins
    • Moss, E.1
  • 51
    • 0032783917 scopus 로고    scopus 로고
    • Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides
    • Nakamura, F., Huang, L., Pestonjamasp, K., Luna, E. J. and Furthmayr, H. (1999). Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides. Mol. Biol. Cell 10, 2669-2685.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2669-2685
    • Nakamura, F.1    Huang, L.2    Pestonjamasp, K.3    Luna, E.J.4    Furthmayr, H.5
  • 52
    • 0029937217 scopus 로고    scopus 로고
    • Measurement of lipocortin 1 levels in murine peripheral blood leukocytes by flow cytometry: Modulation by glucocorticoids and inflammation
    • Perretti, M. and Flower, R. J. (1996). Measurement of lipocortin 1 levels in murine peripheral blood leukocytes by flow cytometry: modulation by glucocorticoids and inflammation. Br. J. Pharmacol. 118, 605-610.
    • (1996) Br. J. Pharmacol. , vol.118 , pp. 605-610
    • Perretti, M.1    Flower, R.J.2
  • 53
    • 0023226743 scopus 로고
    • Regulation of calpactin I phospholipid binding by calpactin I light-chain binding and phosphorylation by p60v-src
    • Powell, M. A. and Glenney, J. R. (1987). Regulation of calpactin I phospholipid binding by calpactin I light-chain binding and phosphorylation by p60v-src. Biochem. J. 247, 321-328.
    • (1987) Biochem. J. , vol.247 , pp. 321-328
    • Powell, M.A.1    Glenney, J.R.2
  • 54
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium- And phospholipid-binding proteins
    • Raynal, P. and Pollard, H. B. (1994). Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim. Biophys. Acta 1197, 63-93.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 55
    • 0023654670 scopus 로고
    • Characterization of Ca2+-dependent phospholipid binding and phosphorylation of lipocortin I
    • Schlaepfer, D. D. and Haigler, H. T. (1987). Characterization of Ca2+-dependent phospholipid binding and phosphorylation of lipocortin I. J. Biol. Chem. 262, 6931-6937.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6931-6937
    • Schlaepfer, D.D.1    Haigler, H.T.2
  • 57
    • 0029786326 scopus 로고    scopus 로고
    • The association of annexin I with early endosomes is regulated by Ca2+ and requires an intact N-terminal domain
    • Seemann, J., Weber, K., Osborn, M., Parton, R. G. and Gerke, V. (1996). The association of annexin I with early endosomes is regulated by Ca2+ and requires an intact N-terminal domain. Mol. Biol. Cell 7, 1359-1374.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1359-1374
    • Seemann, J.1    Weber, K.2    Osborn, M.3    Parton, R.G.4    Gerke, V.5
  • 60
    • 0026353858 scopus 로고
    • Characterization of a Ca(2+)-binding site in human annexin II by site-directed mutagenesis
    • Thiel, C., Weber, K. and Gerke, V. (1991). Characterization of a Ca(2+)-binding site in human annexin II by site-directed mutagenesis. J. Biol. Chem. 266, 14732-14739.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14732-14739
    • Thiel, C.1    Weber, K.2    Gerke, V.3
  • 61
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. and Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 62
    • 0036216769 scopus 로고    scopus 로고
    • Phagocytosis of microbes: Complexity in action
    • Underhill, D. M. and Ozinsky, A. (2002). Phagocytosis of microbes: complexity in action. Annu. Rev. Immunol. 20, 825-852.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 825-852
    • Underhill, D.M.1    Ozinsky, A.2
  • 63
    • 9444242125 scopus 로고    scopus 로고
    • Repeated cycles of rapid actin assembly and disassembly on epithelial cell phagosomes
    • Yam, P. T. and Theriot, J. A. (2004). Repeated cycles of rapid actin assembly and disassembly on epithelial cell phagosomes. Mol. Biol. Cell 15, 5647-5658.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5647-5658
    • Yam, P.T.1    Theriot, J.A.2
  • 65
    • 70249100681 scopus 로고    scopus 로고
    • Annexin- 1 regulates macrophage IL-6 and TNF via glucocorticoid-induced leucine zipper
    • Yang, Y. H., Aeberli, D., Dacumos, A., Xue, J. R. and Morand, E. F. (2009). Annexin- 1 regulates macrophage IL-6 and TNF via glucocorticoid-induced leucine zipper. J. Immunol. 183, 1435-1445.
    • (2009) J. Immunol. , vol.183 , pp. 1435-1445
    • Yang, Y.H.1    Aeberli, D.2    Dacumos, A.3    Xue, J.R.4    Morand, E.F.5
  • 66
    • 34548550595 scopus 로고    scopus 로고
    • Lipid signaling and the modulation of surface charge during phagocytosis
    • Yeung, T. and Grinstein, S. (2007). Lipid signaling and the modulation of surface charge during phagocytosis. Immunol. Rev. 219, 17-36.
    • (2007) Immunol. Rev. , vol.219 , pp. 17-36
    • Yeung, T.1    Grinstein, S.2
  • 67
    • 3242890010 scopus 로고    scopus 로고
    • Stimulus-specific defect in the phagocytic pathways of annexin 1 null macrophages
    • Yona, S., Buckingham, J. C., Perretti, M. and Flower, R. J. (2004). Stimulus-specific defect in the phagocytic pathways of annexin 1 null macrophages. Br. J. Pharmacol. 142, 890-898.
    • (2004) Br. J. Pharmacol. , vol.142 , pp. 890-898
    • Yona, S.1    Buckingham, J.C.2    Perretti, M.3    Flower, R.J.4


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