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Volumn 13, Issue 12, 2003, Pages 648-656

Cues for apoptotic cell engulfment: Eat-me, don't eat-me and come-get-me signals

Author keywords

[No Author keywords available]

Indexed keywords

INTERLEUKIN 10; LYSOPHOSPHATIDYLCHOLINE; PROTEIN; PROTEIN ANNEX; TRANSFORMING GROWTH FACTOR; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 0242559036     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2003.10.004     Document Type: Review
Times cited : (198)

References (75)
  • 1
    • 0033382802 scopus 로고    scopus 로고
    • Programmed cell death in the nematode C. elegans
    • Hengartner M.O. Programmed cell death in the nematode C. elegans. Recent Prog. Horm. Res. 54:1999;213-222.
    • (1999) Recent Prog. Horm. Res. , vol.54 , pp. 213-222
    • Hengartner, M.O.1
  • 2
    • 0034618113 scopus 로고    scopus 로고
    • A hierarchical role for classical pathway complement proteins in the clearance of apoptotic cells in vivo
    • Taylor P.R., et al. A hierarchical role for classical pathway complement proteins in the clearance of apoptotic cells in vivo. J. Exp. Med. 192:2000;359-366.
    • (2000) J. Exp. Med. , vol.192 , pp. 359-366
    • Taylor, P.R.1
  • 3
    • 0035837323 scopus 로고    scopus 로고
    • Phagocytosis and clearance of apoptotic cells is mediated by MER
    • Scott R.S., et al. Phagocytosis and clearance of apoptotic cells is mediated by MER. Nature. 411:2001;207-211.
    • (2001) Nature , vol.411 , pp. 207-211
    • Scott, R.S.1
  • 4
    • 0034795821 scopus 로고    scopus 로고
    • Phagocyte receptors for apoptotic cells: Recognition, uptake, and consequences
    • Fadok V.A., et al. Phagocyte receptors for apoptotic cells: recognition, uptake, and consequences. J. Clin. Invest. 108:2001;957-962.
    • (2001) J. Clin. Invest. , vol.108 , pp. 957-962
    • Fadok, V.A.1
  • 5
    • 0035797881 scopus 로고    scopus 로고
    • Apoptotic cell removal
    • Henson P.M., et al. Apoptotic cell removal. Curr. Biol. 11:2001;R795-R805.
    • (2001) Curr. Biol. , vol.11
    • Henson, P.M.1
  • 6
    • 0036884424 scopus 로고    scopus 로고
    • A blast from the past: Clearance of apoptotic cells regulates immune responses
    • Savill J., et al. A blast from the past: clearance of apoptotic cells regulates immune responses. Nat. Rev. Immunol. 2:2002;965-975.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 965-975
    • Savill, J.1
  • 7
    • 0036583320 scopus 로고    scopus 로고
    • Phagocytosis of apoptotic cells in mammal, Caenorhabditis elegans and Drosophila melanogaster: Molecular mechanisms and physiological consequencess
    • Franc N.C. Phagocytosis of apoptotic cells in mammal, Caenorhabditis elegans and Drosophila melanogaster: molecular mechanisms and physiological consequencess. Front. Biosci. 7:2002;d1298-d1313.
    • (2002) Front. Biosci. , vol.7
    • Franc, N.C.1
  • 8
    • 0034644114 scopus 로고    scopus 로고
    • Differences between the clearance of apoptotic cells by professional and non-professional phagocytes
    • Parnaik R., et al. Differences between the clearance of apoptotic cells by professional and non-professional phagocytes. Curr. Biol. 10:2000;857-860.
    • (2000) Curr. Biol. , vol.10 , pp. 857-860
    • Parnaik, R.1
  • 9
    • 0034521602 scopus 로고    scopus 로고
    • Mesenchymal cells engulf and clear apoptotic footplate cells in macrophageless PU.1 null mouse embryos
    • Wood W., et al. Mesenchymal cells engulf and clear apoptotic footplate cells in macrophageless PU.1 null mouse embryos. Development. 127:2000;5245-5252.
    • (2000) Development , vol.127 , pp. 5245-5252
    • Wood, W.1
  • 10
    • 0031761418 scopus 로고    scopus 로고
    • Morphogenesis of the retinal pigment epithelium: Toward understanding retinal degenerative diseases
    • Marmorstein A.D., et al. Morphogenesis of the retinal pigment epithelium: toward understanding retinal degenerative diseases. Ann N Y Acad Sci. 857:1998;1-12.
    • (1998) Ann N Y Acad Sci , vol.857 , pp. 1-12
    • Marmorstein, A.D.1
  • 11
    • 0030782158 scopus 로고    scopus 로고
    • Macrophages induce apoptosis in normal cells in vivo
    • Diez-Roux G., Lang R.A. Macrophages induce apoptosis in normal cells in vivo. Development. 124:1997;3633-3638.
    • (1997) Development , vol.124 , pp. 3633-3638
    • Diez-Roux, G.1    Lang, R.A.2
  • 12
    • 0035849886 scopus 로고    scopus 로고
    • Phagocytosis promotes programmed cell death in C. elegans
    • Reddien P.W., et al. Phagocytosis promotes programmed cell death in C. elegans. Nature. 412:2001;198-202.
    • (2001) Nature , vol.412 , pp. 198-202
    • Reddien, P.W.1
  • 13
    • 0035849895 scopus 로고    scopus 로고
    • Engulfment genes cooperate with ced-3 to promote cell death in Caenorhabditis elegans
    • Hoeppner D.J., et al. Engulfment genes cooperate with ced-3 to promote cell death in Caenorhabditis elegans. Nature. 412:2001;202-206.
    • (2001) Nature , vol.412 , pp. 202-206
    • Hoeppner, D.J.1
  • 14
    • 0031454570 scopus 로고    scopus 로고
    • Immunosuppressive effects of apoptotic cells
    • Voll R.E., et al. Immunosuppressive effects of apoptotic cells. Nature. 390:1997;350-351.
    • (1997) Nature , vol.390 , pp. 350-351
    • Voll, R.E.1
  • 15
    • 0032519925 scopus 로고    scopus 로고
    • Macrophages that have ingested apoptotic cells in vitro inhibit proinflammatory cytokine production through autocrine/paracrine mechanisms involving TGF-beta, PGE2, and PAF
    • Fadok V.A., et al. Macrophages that have ingested apoptotic cells in vitro inhibit proinflammatory cytokine production through autocrine/paracrine mechanisms involving TGF-beta, PGE2, and PAF. J. Clin. Invest. 101:1998;890-898.
    • (1998) J. Clin. Invest. , vol.101 , pp. 890-898
    • Fadok, V.A.1
  • 16
    • 0036143018 scopus 로고    scopus 로고
    • Phosphatidylserine-dependent ingestion of apoptotic cells promotes TGF-beta1 secretion and the resolution of inflammation
    • Huynh M.L., et al. Phosphatidylserine-dependent ingestion of apoptotic cells promotes TGF-beta1 secretion and the resolution of inflammation. J. Clin. Invest. 109:2002;41-50.
    • (2002) J. Clin. Invest. , vol.109 , pp. 41-50
    • Huynh, M.L.1
  • 17
    • 0035960718 scopus 로고    scopus 로고
    • Apoptotic mimicry by an obligate intracellular parasite downregulates macrophage microbicidal activity
    • de Freitas Balanco J.M., et al. Apoptotic mimicry by an obligate intracellular parasite downregulates macrophage microbicidal activity. Curr. Biol. 11:2001;1870-1873.
    • (2001) Curr. Biol. , vol.11 , pp. 1870-1873
    • De Freitas Balanco, J.M.1
  • 18
    • 0034642522 scopus 로고    scopus 로고
    • Uptake of apoptotic cells drives the growth of a pathogenic trypanosome in macrophages
    • Freire-de-Lima C.G., et al. Uptake of apoptotic cells drives the growth of a pathogenic trypanosome in macrophages. Nature. 403:2000;199-203.
    • (2000) Nature , vol.403 , pp. 199-203
    • Freire-De-Lima, C.G.1
  • 19
    • 0033566932 scopus 로고    scopus 로고
    • Cutting edge: Differential effect of apoptotic versus necrotic tumor cells on macrophage antitumor activities
    • Reiter I., et al. Cutting edge: differential effect of apoptotic versus necrotic tumor cells on macrophage antitumor activities. J. Immunol. 163:1999;1730-1732.
    • (1999) J. Immunol. , vol.163 , pp. 1730-1732
    • Reiter, I.1
  • 20
    • 0037062989 scopus 로고    scopus 로고
    • Apoptosis disables CD31-mediated cell detachment from phagocytes promoting binding and engulfment
    • Brown S., et al. Apoptosis disables CD31-mediated cell detachment from phagocytes promoting binding and engulfment. Nature. 418:2002;200-203.
    • (2002) Nature , vol.418 , pp. 200-203
    • Brown, S.1
  • 21
    • 0033152776 scopus 로고    scopus 로고
    • Macrophage recognition of ICAM-3 on apoptotic leukocytes
    • Moffatt O.D., et al. Macrophage recognition of ICAM-3 on apoptotic leukocytes. J. Immunol. 162:1999;6800-6810.
    • (1999) J. Immunol. , vol.162 , pp. 6800-6810
    • Moffatt, O.D.1
  • 22
    • 0037046580 scopus 로고    scopus 로고
    • Identification of a factor that links apoptotic cells to phagocytes
    • Hanayama R., et al. Identification of a factor that links apoptotic cells to phagocytes. Nature. 417:2002;182-187.
    • (2002) Nature , vol.417 , pp. 182-187
    • Hanayama, R.1
  • 23
    • 0029910706 scopus 로고    scopus 로고
    • Identification of the product of growth arrest-specific gene 6 as a common ligand for Axl, Sky, and Mer receptor tyrosine kinases
    • Nagata K., et al. Identification of the product of growth arrest-specific gene 6 as a common ligand for Axl, Sky, and Mer receptor tyrosine kinases. J. Biol. Chem. 271:1996;30022-30027.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30022-30027
    • Nagata, K.1
  • 24
    • 0035903289 scopus 로고    scopus 로고
    • C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells
    • Ogden C.A., et al. C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells. J. Exp. Med. 194:2001;781-795.
    • (2001) J. Exp. Med. , vol.194 , pp. 781-795
    • Ogden, C.A.1
  • 25
    • 0036785571 scopus 로고    scopus 로고
    • Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: Calreticulin and CD91 as a common collectin receptor complex
    • Vandivier R.W., et al. Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: calreticulin and CD91 as a common collectin receptor complex. J. Immunol. 169:2002;3978-3986.
    • (2002) J. Immunol. , vol.169 , pp. 3978-3986
    • Vandivier, R.W.1
  • 26
    • 0345237926 scopus 로고    scopus 로고
    • Macrophage recognition and phagocytosis of apoptotic fibroblasts is critically dependent on fibroblast-derived thrombospondin 1 and CD36
    • Moodley Y., et al. Macrophage recognition and phagocytosis of apoptotic fibroblasts is critically dependent on fibroblast-derived thrombospondin 1 and CD36. Am. J. Pathol. 162:2003;771-779.
    • (2003) Am. J. Pathol. , vol.162 , pp. 771-779
    • Moodley, Y.1
  • 27
    • 0032400966 scopus 로고    scopus 로고
    • CD36 is required for phagocytosis of apoptotic cells by human macrophages that use either a phosphatidylserine receptor or the vitronectin receptor (alpha v beta 3)
    • Fadok V.A., et al. CD36 is required for phagocytosis of apoptotic cells by human macrophages that use either a phosphatidylserine receptor or the vitronectin receptor (alpha v beta 3). J. Immunol. 161:1998;6250-6257.
    • (1998) J. Immunol. , vol.161 , pp. 6250-6257
    • Fadok, V.A.1
  • 28
    • 0033950998 scopus 로고    scopus 로고
    • CD14-dependent clearance of apoptotic cells: Relevance to the immune system
    • Gregory C.D. CD14-dependent clearance of apoptotic cells: relevance to the immune system. Curr. Opin. Immunol. 12:2000;27-34.
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 27-34
    • Gregory, C.D.1
  • 30
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok V.A., et al. Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J. Immunol. 148:1992;2207-2216.
    • (1992) J. Immunol. , vol.148 , pp. 2207-2216
    • Fadok, V.A.1
  • 31
    • 0031849291 scopus 로고    scopus 로고
    • The role of phosphatidylserine in recognition of apoptotic cells by phagocytes
    • Fadok V.A., et al. The role of phosphatidylserine in recognition of apoptotic cells by phagocytes. Cell Death Differ. 5:1998;551-562.
    • (1998) Cell Death Differ. , vol.5 , pp. 551-562
    • Fadok, V.A.1
  • 32
    • 0035846941 scopus 로고    scopus 로고
    • Loss of phospholipid asymmetry and surface exposure of phosphatidylserine is required for phagocytosis of apoptotic cells by macrophages and fibroblasts
    • Fadok V.A., et al. Loss of phospholipid asymmetry and surface exposure of phosphatidylserine is required for phagocytosis of apoptotic cells by macrophages and fibroblasts. J. Biol. Chem. 276:2001;1071-1077.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1071-1077
    • Fadok, V.A.1
  • 33
    • 0035969234 scopus 로고    scopus 로고
    • Phosphatidylserine (PS) induces PS receptor-mediated macropinocytosis and promotes clearance of apoptotic cells
    • Hoffmann P.R., et al. Phosphatidylserine (PS) induces PS receptor-mediated macropinocytosis and promotes clearance of apoptotic cells. J. Cell Biol. 155:2001;649-660.
    • (2001) J. Cell Biol. , vol.155 , pp. 649-660
    • Hoffmann, P.R.1
  • 34
    • 0037203341 scopus 로고    scopus 로고
    • Transbilayer phospholipid movement and the clearance of apoptotic cells
    • Williamson P., Schlegel R.A. Transbilayer phospholipid movement and the clearance of apoptotic cells. Biochim Biophys Acta. 1585:2002;53-63.
    • (2002) Biochim Biophys Acta , vol.1585 , pp. 53-63
    • Williamson, P.1    Schlegel, R.A.2
  • 35
    • 0034604029 scopus 로고    scopus 로고
    • A receptor for phosphatidylserine-specific clearance of apoptotic cells
    • Fadok V.A., et al. A receptor for phosphatidylserine-specific clearance of apoptotic cells. Nature. 405:2000;85-90.
    • (2000) Nature , vol.405 , pp. 85-90
    • Fadok, V.A.1
  • 36
    • 0035846941 scopus 로고    scopus 로고
    • Loss of phospholipid asymmetry and surface exposure of phosphatidylserine is required for phagocytosis of apoptotic cells by macrophages and fibroblasts
    • Fadok V.A., et al. Loss of phospholipid asymmetry and surface exposure of phosphatidylserine is required for phagocytosis of apoptotic cells by macrophages and fibroblasts. J Biol Chem. 276:2001;1071-1077.
    • (2001) J Biol Chem , vol.276 , pp. 1071-1077
    • Fadok, V.A.1
  • 37
    • 0035434662 scopus 로고    scopus 로고
    • The phosphatidylserine receptor: A crucial molecular switch?
    • Henson P.M., et al. The phosphatidylserine receptor: a crucial molecular switch? Nat. Rev. Mol. Cell Biol. 2:2001;627-633.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 627-633
    • Henson, P.M.1
  • 38
    • 0034949428 scopus 로고    scopus 로고
    • If phosphatidylserine is the death knell, a new phosphatidylserine- specific receptor is the bellringer
    • Fadok V.A., et al. If phosphatidylserine is the death knell, a new phosphatidylserine- specific receptor is the bellringer. Cell Death Differ. 8:2001;582-587.
    • (2001) Cell Death Differ. , vol.8 , pp. 582-587
    • Fadok, V.A.1
  • 39
    • 0037390598 scopus 로고    scopus 로고
    • Annexin I is an endogenous ligand that mediates apoptotic cell engulfment
    • Arur S., et al. Annexin I is an endogenous ligand that mediates apoptotic cell engulfment. Dev. Cell. 4:2003;587-598.
    • (2003) Dev. Cell , vol.4 , pp. 587-598
    • Arur, S.1
  • 40
    • 0030013412 scopus 로고    scopus 로고
    • Evidence for specific annexin I-binding proteins on human monocytes
    • Goulding N.J., et al. Evidence for specific annexin I-binding proteins on human monocytes. Biochem. J. 316:1996;593-597.
    • (1996) Biochem. J. , vol.316 , pp. 593-597
    • Goulding, N.J.1
  • 41
    • 0033634942 scopus 로고    scopus 로고
    • A novel ligand of the formyl peptide receptor: Annexin I regulates neutrophil extravasation by interacting with the FPR
    • Walther A., et al. A novel ligand of the formyl peptide receptor: annexin I regulates neutrophil extravasation by interacting with the FPR. Mol. Cell. 5:2000;831-840.
    • (2000) Mol. Cell , vol.5 , pp. 831-840
    • Walther, A.1
  • 42
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Gerke V., Moss S.E. Annexins: from structure to function. Physiol. Rev. 82:2002;331-371.
    • (2002) Physiol. Rev. , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 43
    • 0035793710 scopus 로고    scopus 로고
    • Folding energetics of ligand binding proteins II. Cooperative binding of Ca2+ to annexin I
    • Rosengarth A., et al. Folding energetics of ligand binding proteins II. Cooperative binding of Ca2+ to annexin I. J. Mol. Biol. 306:2001;825-835.
    • (2001) J. Mol. Biol. , vol.306 , pp. 825-835
    • Rosengarth, A.1
  • 44
    • 0034619577 scopus 로고    scopus 로고
    • Mechanism of annexin I-mediated membrane aggregation
    • Bitto E., et al. Mechanism of annexin I-mediated membrane aggregation. Biochemistry. 39:2000;13469-13477.
    • (2000) Biochemistry , vol.39 , pp. 13469-13477
    • Bitto, E.1
  • 45
    • 0037424618 scopus 로고    scopus 로고
    • A calcium-driven conformational switch of the N-terminal and core domains of annexin A1
    • Rosengarth A., Luecke H. A calcium-driven conformational switch of the N-terminal and core domains of annexin A1. J. Mol. Biol. 326:2003;1317-1325.
    • (2003) J. Mol. Biol. , vol.326 , pp. 1317-1325
    • Rosengarth, A.1    Luecke, H.2
  • 46
    • 0034674421 scopus 로고    scopus 로고
    • Role of CD47 as a marker of self on red blood cells
    • Oldenborg P.A., et al. Role of CD47 as a marker of self on red blood cells. Science. 288:2000;2051-2054.
    • (2000) Science , vol.288 , pp. 2051-2054
    • Oldenborg, P.A.1
  • 47
    • 0038820117 scopus 로고    scopus 로고
    • Apoptotic cells induce migration of phagocytes via caspase-3-mediated release of a lipid attraction signal
    • Lauber K., et al. Apoptotic cells induce migration of phagocytes via caspase-3-mediated release of a lipid attraction signal. Cell. 113:2003;717-730.
    • (2003) Cell , vol.113 , pp. 717-730
    • Lauber, K.1
  • 48
    • 0025753458 scopus 로고
    • Analysis of the monocyte chemotactic response to lysophosphatidylcholine: Role of lysophospholipase C
    • Quinn M.T., et al. Analysis of the monocyte chemotactic response to lysophosphatidylcholine: role of lysophospholipase C. Biochim. Biophys. Acta. 1082:1991;293-302.
    • (1991) Biochim. Biophys. Acta , vol.1082 , pp. 293-302
    • Quinn, M.T.1
  • 49
    • 0027306764 scopus 로고
    • Oxidatively modified low density lipoprotein is a chemoattractant for human T lymphocytes
    • McMurray H.F., et al. Oxidatively modified low density lipoprotein is a chemoattractant for human T lymphocytes. J. Clin. Invest. 92:1993;1004-1008.
    • (1993) J. Clin. Invest. , vol.92 , pp. 1004-1008
    • Mcmurray, H.F.1
  • 50
    • 0028044102 scopus 로고
    • Lysophosphatidylcholine: A chemoattractant to human T lymphocytes
    • Ryborg A.K., et al. Lysophosphatidylcholine: a chemoattractant to human T lymphocytes. Arch. Dermatol. Res. 286:1994;462-465.
    • (1994) Arch. Dermatol. Res. , vol.286 , pp. 462-465
    • Ryborg, A.K.1
  • 51
    • 0037099201 scopus 로고    scopus 로고
    • Lysophosphatidylcholine as a ligand for immunoregulation
    • Kabarowski J.H., et al. Lysophosphatidylcholine as a ligand for immunoregulation. Biochem. Pharmacol. 64:2002;161-167.
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 161-167
    • Kabarowski, J.H.1
  • 52
    • 0020956808 scopus 로고
    • Serum proteins neutralize the toxic effect of lysophosphatidyl choline
    • Mochizuki M., et al. Serum proteins neutralize the toxic effect of lysophosphatidyl choline. Curr. Eye Res. 2:1982;621-624.
    • (1982) Curr. Eye Res. , vol.2 , pp. 621-624
    • Mochizuki, M.1
  • 53
    • 0033983832 scopus 로고    scopus 로고
    • Characterization of plasma unsaturated lysophosphatidylcholines in human and rat
    • Croset M., et al. Characterization of plasma unsaturated lysophosphatidylcholines in human and rat. Biochem. J. 345:2000;61-67.
    • (2000) Biochem. J. , vol.345 , pp. 61-67
    • Croset, M.1
  • 54
    • 0027301185 scopus 로고
    • Vitamin D-binding protein (group-specific component) is the sole serum protein required for macrophage activation after treatment of peritoneal cells with lysophosphatidylcholine
    • Homma S., et al. Vitamin D-binding protein (group-specific component) is the sole serum protein required for macrophage activation after treatment of peritoneal cells with lysophosphatidylcholine. Immunol. Cell Biol. 71:1993;249-257.
    • (1993) Immunol. Cell Biol. , vol.71 , pp. 249-257
    • Homma, S.1
  • 55
    • 0036719167 scopus 로고    scopus 로고
    • I-PLA(2) activation during apoptosis promotes the exposure of membrane lysophosphatidylcholine leading to binding by natural immunoglobulin M antibodies and complement activation
    • Kim S.J., et al. I-PLA(2) activation during apoptosis promotes the exposure of membrane lysophosphatidylcholine leading to binding by natural immunoglobulin M antibodies and complement activation. J. Exp. Med. 196:2002;655-665.
    • (2002) J. Exp. Med. , vol.196 , pp. 655-665
    • Kim, S.J.1
  • 56
    • 0035958728 scopus 로고    scopus 로고
    • Lysophosphatidylcholine as a ligand for the immunoregulatory receptor G2A
    • Kabarowski J.H., et al. Lysophosphatidylcholine as a ligand for the immunoregulatory receptor G2A. Science. 293:2001;702-705.
    • (2001) Science , vol.293 , pp. 702-705
    • Kabarowski, J.H.1
  • 57
    • 0035798686 scopus 로고    scopus 로고
    • Sphingosylphosphorylcholine and lysophosphatidylcholine are ligands for the G protein-coupled receptor GPR4
    • Zhu K., et al. Sphingosylphosphorylcholine and lysophosphatidylcholine are ligands for the G protein-coupled receptor GPR4. J. Biol. Chem. 276:2001;41325-41335.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41325-41335
    • Zhu, K.1
  • 58
    • 0032514679 scopus 로고    scopus 로고
    • A DNA damage and stress inducible G protein-coupled receptor blocks cells in G2/M
    • Weng Z., et al. A DNA damage and stress inducible G protein-coupled receptor blocks cells in G2/M. Proc. Natl. Acad. Sci. U. S. A. 95:1998;12334-12339.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12334-12339
    • Weng, Z.1
  • 59
    • 0034173212 scopus 로고    scopus 로고
    • Defective macrophage recruitment and clearance of apoptotic cells in the uterus of osteopetrotic mutant mice lacking macrophage colony-stimulating factor (M-CSF)
    • Shimada-Hiratsuka M., et al. Defective macrophage recruitment and clearance of apoptotic cells in the uterus of osteopetrotic mutant mice lacking macrophage colony-stimulating factor (M-CSF). J. Submicrosc. Cytol. Pathol. 32:2000;297-307.
    • (2000) J. Submicrosc. Cytol. Pathol. , vol.32 , pp. 297-307
    • Shimada-Hiratsuka, M.1
  • 60
    • 0032511234 scopus 로고    scopus 로고
    • Candidate adaptor protein CED-6 promotes the engulfment of apoptotic cells in C. elegans
    • Liu Q.A., Hengartner M.O. Candidate adaptor protein CED-6 promotes the engulfment of apoptotic cells in C. elegans. Cell. 93:1998;961-972.
    • (1998) Cell , vol.93 , pp. 961-972
    • Liu, Q.A.1    Hengartner, M.O.2
  • 61
    • 0033581828 scopus 로고    scopus 로고
    • Human CED-6 encodes a functional homologue of the Caenorhabditis elegans engulfment protein CED-6
    • Liu Q.A., Hengartner M.O. Human CED-6 encodes a functional homologue of the Caenorhabditis elegans engulfment protein CED-6. Curr. Biol. 9:1999;1347-1350.
    • (1999) Curr. Biol. , vol.9 , pp. 1347-1350
    • Liu, Q.A.1    Hengartner, M.O.2
  • 62
    • 0032511145 scopus 로고    scopus 로고
    • The C. elegans cell corpse engulfment gene ced-7 encodes a protein similar to ABC transporters
    • Wu Y.C., Horvitz H.R. The C. elegans cell corpse engulfment gene ced-7 encodes a protein similar to ABC transporters. Cell. 93:1998;951-960.
    • (1998) Cell , vol.93 , pp. 951-960
    • Wu, Y.C.1    Horvitz, H.R.2
  • 63
    • 0035846903 scopus 로고    scopus 로고
    • CED-1 Is a transmembrane receptor that mediates cell corpse engulfment in c. elegans
    • Zhou Z., et al. CED-1 Is a transmembrane receptor that mediates cell corpse engulfment in c. elegans. cell. 104:2001;43-56.
    • (2001) Cell , vol.104 , pp. 43-56
    • Zhou, Z.1
  • 64
    • 0037023693 scopus 로고    scopus 로고
    • Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP)
    • Su H.P., et al. Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP). J. Biol. Chem. 277:2002;11772-11779.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11772-11779
    • Su, H.P.1
  • 65
    • 0033776534 scopus 로고    scopus 로고
    • ABC1 promotes engulfment of apoptotic cells and transbilayer redistribution of phosphatidylserine
    • Hamon Y., et al. ABC1 promotes engulfment of apoptotic cells and transbilayer redistribution of phosphatidylserine. Nat. Cell Biol. 2:2000;399-406.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 399-406
    • Hamon, Y.1
  • 66
    • 0035487807 scopus 로고    scopus 로고
    • C. elegans CED-12 acts in the conserved crkII/DOCK180/Rac pathway to control cell migration and cell corpse engulfment
    • Wu Y.C., et al. C. elegans CED-12 acts in the conserved crkII/DOCK180/ Rac pathway to control cell migration and cell corpse engulfment. Dev. Cell. 1:2001;491-502.
    • (2001) Dev. Cell , vol.1 , pp. 491-502
    • Wu, Y.C.1
  • 67
    • 0032473981 scopus 로고    scopus 로고
    • C. elegans phagocytosis and cell-migration protein CED-5 is similar to human DOCK180
    • Wu Y.C., Horvitz H.R. C. elegans phagocytosis and cell-migration protein CED-5 is similar to human DOCK180. Nature. 392:1998;501-504.
    • (1998) Nature , vol.392 , pp. 501-504
    • Wu, Y.C.1    Horvitz, H.R.2
  • 68
    • 0035487646 scopus 로고    scopus 로고
    • The C. elegans PH domain protein CED-12 regulates cytoskeletal reorganization via a Rho/Rac GTPase signaling pathway
    • Zhou Z., et al. The C. elegans PH domain protein CED-12 regulates cytoskeletal reorganization via a Rho/Rac GTPase signaling pathway. Dev. Cell. 1:2001;477-489.
    • (2001) Dev. Cell , vol.1 , pp. 477-489
    • Zhou, Z.1
  • 69
    • 0033771902 scopus 로고    scopus 로고
    • CED-2/CrkII and CED-10/Rac control phagocytosis and cell migration in Caenorhabditis elegans
    • Reddien P.W., Horvitz H.R. CED-2/CrkII and CED-10/Rac control phagocytosis and cell migration in Caenorhabditis elegans. Nat. Cell Biol. 2:2000;131-136.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 131-136
    • Reddien, P.W.1    Horvitz, H.R.2
  • 70
    • 17944376439 scopus 로고    scopus 로고
    • CED-12/ELMO, a novel member of the crkII/Dock180/Rac pathway, is required for phagocytosis and cell migration
    • Gumienny T.L., et al. CED-12/ELMO, a novel member of the crkII/Dock180/Rac pathway, is required for phagocytosis and cell migration. Cell. 107:2001;27-41.
    • (2001) Cell , vol.107 , pp. 27-41
    • Gumienny, T.L.1
  • 71
    • 0036045768 scopus 로고    scopus 로고
    • Unconventional Rac-GEF activity is mediated through the Dock180-ELMO complex
    • Brugnera E., et al. Unconventional Rac-GEF activity is mediated through the Dock180-ELMO complex. Nat. Cell Biol. 4:2002;574-582.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 574-582
    • Brugnera, E.1
  • 72
    • 0033625871 scopus 로고    scopus 로고
    • αvβ5 integrin recruits the CrkII-Dock180-Rac1 complex for phagocytosis of apoptotic cells
    • Albert M., et al. αvβ5 integrin recruits the CrkII-Dock180-Rac1 complex for phagocytosis of apoptotic cells. Nat. Cell Biol. 2:2000;899-905.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 899-905
    • Albert, M.1
  • 73
    • 0042674398 scopus 로고    scopus 로고
    • RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo
    • Katoh H., Negishi M. RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo. Nature. 424:2003;461-464.
    • (2003) Nature , vol.424 , pp. 461-464
    • Katoh, H.1    Negishi, M.2
  • 74
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville S., Hall A. Rho GTPases in cell biology. Nature. 420:2002;629-635.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 75
    • 0032825266 scopus 로고    scopus 로고
    • Regulation of cell contraction and membrane ruffling by distinct signals in migratory cells
    • Cheresh D.A., et al. Regulation of cell contraction and membrane ruffling by distinct signals in migratory cells. J. Cell Biol. 146:1999;1107-1116.
    • (1999) J. Cell Biol. , vol.146 , pp. 1107-1116
    • Cheresh, D.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.