메뉴 건너뛰기




Volumn 5, Issue 11, 2011, Pages

Entamoeba lysyl-tRNA synthetase contains a cytokine-like domain with chemokine activity towards human endothelial cells

Author keywords

[No Author keywords available]

Indexed keywords

ENDOTHELIAL MONOCYTE ACTIVATING POLYPEPTIDE II; GENOMIC DNA; LYSINE TRANSFER RNA LIGASE; CYTOKINE; RNA BINDING PROTEIN; SMALL INDUCIBLE CYTOKINE SUBFAMILY E, MEMBER 1; TUMOR PROTEIN;

EID: 82555174606     PISSN: 19352727     EISSN: 19352735     Source Type: Journal    
DOI: 10.1371/journal.pntd.0001398     Document Type: Article
Times cited : (13)

References (59)
  • 1
    • 60449117752 scopus 로고    scopus 로고
    • Using differential gene expression to study Entamoeba histolytica pathogenesis
    • Gilchrist CA, Petri WA Jr, (2009) Using differential gene expression to study Entamoeba histolytica pathogenesis. Trends Parasitol 25: 124-131.
    • (2009) Trends Parasitol , vol.25 , pp. 124-131
    • Gilchrist, C.A.1    Petri Jr., W.A.2
  • 2
    • 73449102823 scopus 로고    scopus 로고
    • An ex-vivo Human Intestinal Model to Study Entamoeba histolytica Pathogenesis
    • Bansal D, Ave P, Kerneis S, Frileux P, Boché O, et al. (2009) An ex-vivo Human Intestinal Model to Study Entamoeba histolytica Pathogenesis. PLoS Negl Trop Dis 3: e551.
    • (2009) PLoS Negl Trop Dis , vol.3
    • Bansal, D.1    Ave, P.2    Kerneis, S.3    Frileux, P.4    Boché, O.5
  • 3
    • 77749273670 scopus 로고    scopus 로고
    • Epithelial Cell Apoptosis Facilitates Entamoeba histolytica Infection in the Gut
    • Becker SM, Cho K-N, Guo X, Fendig K, Oosman MN, et al. (2010) Epithelial Cell Apoptosis Facilitates Entamoeba histolytica Infection in the Gut. Am J Pathol 176: 1316-1322.
    • (2010) Am J Pathol , vol.176 , pp. 1316-1322
    • Becker, S.M.1    Cho, K.-N.2    Guo, X.3    Fendig, K.4    Oosman, M.N.5
  • 4
    • 34548017167 scopus 로고    scopus 로고
    • Crosstalk at the initial encounter: interplay between host defense and ameba survival strategies
    • Guo X, Houpt E, Petri WA Jr, (2007) Crosstalk at the initial encounter: interplay between host defense and ameba survival strategies. Curr Opin Immunol 19: 376-384.
    • (2007) Curr Opin Immunol , vol.19 , pp. 376-384
    • Guo, X.1    Houpt, E.2    Petri Jr., W.A.3
  • 5
    • 33746303014 scopus 로고    scopus 로고
    • Progress in research on Entamoeba histolytica pathogenesis
    • Ackers JP, Mirelman D, (2006) Progress in research on Entamoeba histolytica pathogenesis. Curr Opin Microbiol 9: 367-373.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 367-373
    • Ackers, J.P.1    Mirelman, D.2
  • 6
    • 0030965793 scopus 로고    scopus 로고
    • In vitro Entamoeba histolytica adhesion to human endothelium: a comparison using two strains of different virulence
    • Flores-Romo L, Estrada-Garcia T, Shibayama-Salas M, Campos-Rodriguez R, Bacon K, et al. (1997) In vitro Entamoeba histolytica adhesion to human endothelium: a comparison using two strains of different virulence. Parasitol Res 83: 397-400.
    • (1997) Parasitol Res , vol.83 , pp. 397-400
    • Flores-Romo, L.1    Estrada-Garcia, T.2    Shibayama-Salas, M.3    Campos-Rodriguez, R.4    Bacon, K.5
  • 7
  • 8
    • 0036208849 scopus 로고    scopus 로고
    • Early interactions of Entamoeba histolytica trophozoites with parenchymal and inflammatory cells in the hamster liver: an immunocytochemical study
    • Ventura-Juarez J, Campos-Rodriguez R, Tsutsumi V, (2002) Early interactions of Entamoeba histolytica trophozoites with parenchymal and inflammatory cells in the hamster liver: an immunocytochemical study. Can J Microbiol 48: 123-131.
    • (2002) Can J Microbiol , vol.48 , pp. 123-131
    • Ventura-Juarez, J.1    Campos-Rodriguez, R.2    Tsutsumi, V.3
  • 10
    • 59649120679 scopus 로고    scopus 로고
    • Host-microbe interactions and defense mechanisms in the development of amoebic liver abscesses
    • Santi-Rocca J, Rigothier MC, Guillen N, (2009) Host-microbe interactions and defense mechanisms in the development of amoebic liver abscesses. Clin Microbiol Rev 22: 65-75.
    • (2009) Clin Microbiol Rev , vol.22 , pp. 65-75
    • Santi-Rocca, J.1    Rigothier, M.C.2    Guillen, N.3
  • 11
    • 34548428327 scopus 로고    scopus 로고
    • Epigenetic silencing of Plasmodium falciparum genes linked to erythrocyte invasion
    • Cortes A, Carret C, Kaneko O, Yim Lim BY, Ivens A, et al. (2007) Epigenetic silencing of Plasmodium falciparum genes linked to erythrocyte invasion. PLoS Pathog 3: e107.
    • (2007) PLoS Pathog , vol.3
    • Cortes, A.1    Carret, C.2    Kaneko, O.3    Yim Lim, B.Y.4    Ivens, A.5
  • 12
    • 0036853070 scopus 로고    scopus 로고
    • Evasion of innate immunity by parasitic protozoa
    • Sacks D, Sher A, (2002) Evasion of innate immunity by parasitic protozoa. Nat Immunol 3: 1041-1047.
    • (2002) Nat Immunol , vol.3 , pp. 1041-1047
    • Sacks, D.1    Sher, A.2
  • 14
    • 52949118056 scopus 로고    scopus 로고
    • The role of aminoacyl-tRNA synthetases in genetic diseases
    • Antonellis A, Green ED, (2008) The role of aminoacyl-tRNA synthetases in genetic diseases. Annu Rev Genomics Hum Genet 9: 87-107.
    • (2008) Annu Rev Genomics Hum Genet , vol.9 , pp. 87-107
    • Antonellis, A.1    Green, E.D.2
  • 15
    • 77956095201 scopus 로고    scopus 로고
    • New functions of aminoacyl-tRNA synthetases beyond translation
    • Guo M, Yang XL, Schimmel P, (2010) New functions of aminoacyl-tRNA synthetases beyond translation. Nat Rev Mol Cell Biol 11: 668-674.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 668-674
    • Guo, M.1    Yang, X.L.2    Schimmel, P.3
  • 16
    • 49649110170 scopus 로고    scopus 로고
    • Aminoacyl tRNA synthetases and their connections to disease
    • Park SG, Schimmel P, Kim S, (2008) Aminoacyl tRNA synthetases and their connections to disease. Proc Natl Acad Sci USA 105: 11043-11049.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11043-11049
    • Park, S.G.1    Schimmel, P.2    Kim, S.3
  • 17
    • 41549107654 scopus 로고    scopus 로고
    • Not Just Because It Is There: Aminoacyl-tRNA Synthetases Gain Control of the Cell
    • Ribas de Pouplana L, Geslain R, (2008) Not Just Because It Is There: Aminoacyl-tRNA Synthetases Gain Control of the Cell. Mol Cell 30: 3-4.
    • (2008) Mol Cell , vol.30 , pp. 3-4
    • Ribas de Pouplana, L.1    Geslain, R.2
  • 18
    • 67651095905 scopus 로고    scopus 로고
    • Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity
    • Arif A, Jia J, Mukhopadhyay R, Willard B, Kinter M, et al. (2009) Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity. Mol Cell 35: 164-180.
    • (2009) Mol Cell , vol.35 , pp. 164-180
    • Arif, A.1    Jia, J.2    Mukhopadhyay, R.3    Willard, B.4    Kinter, M.5
  • 19
    • 40849118528 scopus 로고    scopus 로고
    • WHEP domains direct noncanonical function of glutamyl-Prolyl tRNA synthetase in translational control of gene expression
    • Jia J, Arif A, Ray PS, Fox PL, (2008) WHEP domains direct noncanonical function of glutamyl-Prolyl tRNA synthetase in translational control of gene expression. Mol Cell 29: 679-690.
    • (2008) Mol Cell , vol.29 , pp. 679-690
    • Jia, J.1    Arif, A.2    Ray, P.S.3    Fox, P.L.4
  • 20
    • 5444271940 scopus 로고    scopus 로고
    • Noncanonical Function of Glutamyl-Prolyl-tRNA Synthetase: Gene-Specific Silencing of Translation
    • Sampath P, Mazumder B, Seshadri V, Gerber CA, Chavatte L, et al. (2004) Noncanonical Function of Glutamyl-Prolyl-tRNA Synthetase: Gene-Specific Silencing of Translation. Cell 119: 195-208.
    • (2004) Cell , vol.119 , pp. 195-208
    • Sampath, P.1    Mazumder, B.2    Seshadri, V.3    Gerber, C.A.4    Chavatte, L.5
  • 21
    • 43249106267 scopus 로고    scopus 로고
    • The novel fragment of tyrosyl tRNA synthetase, mini-TyrRS, is secreted to induce an angiogenic response in endothelial cells
    • Greenberg Y, King M, Kiosses WB, Ewalt K, Yang X, et al. (2008) The novel fragment of tyrosyl tRNA synthetase, mini-TyrRS, is secreted to induce an angiogenic response in endothelial cells. FASEB J 22: 1597-1605.
    • (2008) FASEB J , vol.22 , pp. 1597-1605
    • Greenberg, Y.1    King, M.2    Kiosses, W.B.3    Ewalt, K.4    Yang, X.5
  • 22
    • 0033515887 scopus 로고    scopus 로고
    • Two distinct cytokines released from a human aminoacyl-tRNA synthetase
    • Wakasugi K, Schimmel P, (1999) Two distinct cytokines released from a human aminoacyl-tRNA synthetase. Science 284: 147-151.
    • (1999) Science , vol.284 , pp. 147-151
    • Wakasugi, K.1    Schimmel, P.2
  • 23
    • 2342581552 scopus 로고    scopus 로고
    • Relationship of two human tRNA synthetases used in cell signaling
    • Yang XL, Schimmel P, Ewalt KL, (2004) Relationship of two human tRNA synthetases used in cell signaling. Trends Biochem Sci 29: 250-256.
    • (2004) Trends Biochem Sci , vol.29 , pp. 250-256
    • Yang, X.L.1    Schimmel, P.2    Ewalt, K.L.3
  • 24
    • 33645783942 scopus 로고    scopus 로고
    • Brugia malayi Asparaginyl-Transfer RNA Synthetase Induces Chemotaxis of Human Leukocytes and Activates G-Protein-Coupled Receptors CXCR1 and CXCR2
    • Ramirez BL, Howard OM, Dong HF, Edamatsu T, Gao P, et al. (2006) Brugia malayi Asparaginyl-Transfer RNA Synthetase Induces Chemotaxis of Human Leukocytes and Activates G-Protein-Coupled Receptors CXCR1 and CXCR2. J infect Dis 193: 1164-1171.
    • (2006) J Infect Dis , vol.193 , pp. 1164-1171
    • Ramirez, B.L.1    Howard, O.M.2    Dong, H.F.3    Edamatsu, T.4    Gao, P.5
  • 25
    • 4444369924 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetase complexes: beyond translation
    • Lee SW, Cho BH, Park SG, Kim S, (2004) Aminoacyl-tRNA synthetase complexes: beyond translation. J Cell Sci 117: 3725-3734.
    • (2004) J Cell Sci , vol.117 , pp. 3725-3734
    • Lee, S.W.1    Cho, B.H.2    Park, S.G.3    Kim, S.4
  • 26
    • 32644460680 scopus 로고    scopus 로고
    • Structural separation of different extracellular activities in aminoacyl-tRNA synthetase-interacting multi-functional protein, p43/AIMP1
    • Han JM, Park SG, Lee Y, Kim S, (2006) Structural separation of different extracellular activities in aminoacyl-tRNA synthetase-interacting multi-functional protein, p43/AIMP1. Biochem Biophys Res Commun 342: 113-118.
    • (2006) Biochem Biophys Res Commun , vol.342 , pp. 113-118
    • Han, J.M.1    Park, S.G.2    Lee, Y.3    Kim, S.4
  • 27
    • 48749115388 scopus 로고    scopus 로고
    • AIMP1/p43 Protein Induces the Maturation of Bone Marrow-Derived Dendritic Cells with T Helper Type 1-Polarizing Ability
    • Kim E, Kim SH, Kim S, Cho D, Kim TS, (2008) AIMP1/p43 Protein Induces the Maturation of Bone Marrow-Derived Dendritic Cells with T Helper Type 1-Polarizing Ability. J Immunol 180: 2894-2902.
    • (2008) J Immunol , vol.180 , pp. 2894-2902
    • Kim, E.1    Kim, S.H.2    Kim, S.3    Cho, D.4    Kim, T.S.5
  • 28
    • 0035933792 scopus 로고    scopus 로고
    • A cofactor of tRNA synthetase, p43, is secreted to up-regulate proinflammatory genes
    • Ko YG, Park H, Kim T, Lee JW, Park SG, et al. (2001) A cofactor of tRNA synthetase, p43, is secreted to up-regulate proinflammatory genes. J Biol Chem 276: 23028-23033.
    • (2001) J Biol Chem , vol.276 , pp. 23028-23033
    • Ko, Y.G.1    Park, H.2    Kim, T.3    Lee, J.W.4    Park, S.G.5
  • 29
    • 0035968226 scopus 로고    scopus 로고
    • The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component
    • Shalak V, Kaminska M, Mitnacht-Kraus R, Vandenabeele P, Clauss M, et al. (2001) The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component. J Biol Chem 276: 23769-23776.
    • (2001) J Biol Chem , vol.276 , pp. 23769-23776
    • Shalak, V.1    Kaminska, M.2    Mitnacht-Kraus, R.3    Vandenabeele, P.4    Clauss, M.5
  • 30
    • 33749995841 scopus 로고    scopus 로고
    • Endothelial monocyte-activating polypeptide-II and its functions in (patho)physiological processes
    • van Horssen R, Eggermont AM, ten Hagen TL, (2006) Endothelial monocyte-activating polypeptide-II and its functions in (patho)physiological processes. Cytokine Growth Factor Rev 17: 339-348.
    • (2006) Cytokine Growth Factor Rev , vol.17 , pp. 339-348
    • van Horssen, R.1    Eggermont, A.M.2    ten Hagen, T.L.3
  • 31
    • 0034671820 scopus 로고    scopus 로고
    • A recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylation
    • Kaminska M, Deniziak M, Kerjan P, Barciszewski J, Mirande M, (2000) A recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylation. EMBO J 19: 6908-6917.
    • (2000) EMBO J , vol.19 , pp. 6908-6917
    • Kaminska, M.1    Deniziak, M.2    Kerjan, P.3    Barciszewski, J.4    Mirande, M.5
  • 32
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani G, Delarue M, Poch O, Gangloff J, Moras D, (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347: 203-206.
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 33
    • 0017846267 scopus 로고
    • A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba
    • Diamond LS, Harlow DR, Cunnick CC, (1978) A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba. Trans R Soc Trop Med Hyg 72: 431-432.
    • (1978) Trans R Soc Trop Med Hyg , vol.72 , pp. 431-432
    • Diamond, L.S.1    Harlow, D.R.2    Cunnick, C.C.3
  • 34
    • 0030882663 scopus 로고    scopus 로고
    • Removal of endotoxin from recombinant protein preparations
    • Liu S, Tobias R, McClure S, Styba G, Shi Q, et al. (1997) Removal of endotoxin from recombinant protein preparations. Clin Biochem 30: 455-463.
    • (1997) Clin Biochem , vol.30 , pp. 455-463
    • Liu, S.1    Tobias, R.2    McClure, S.3    Styba, G.4    Shi, Q.5
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (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
  • 36
    • 0016432066 scopus 로고
    • Demonstration of two active sites on a monomeric aminoacyl-tRNA synthetase. Possible roles of negative cooperativity and half-of-the-site reactivity in oligomeric enzymes
    • Fersht AR, (1975) Demonstration of two active sites on a monomeric aminoacyl-tRNA synthetase. Possible roles of negative cooperativity and half-of-the-site reactivity in oligomeric enzymes. Biochemistry 14: 5-12.
    • (1975) Biochemistry , vol.14 , pp. 5-12
    • Fersht, A.R.1
  • 37
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
    • Sampson JR, Uhlenbeck OC, (1988) Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc Natl Acad Sci USA 85: 1033-1037.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1033-1037
    • Sampson, J.R.1    Uhlenbeck, O.C.2
  • 39
  • 40
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ, (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 41
    • 0024152983 scopus 로고
    • Phylogenies from molecular sequences: inference and reliability
    • Felsenstein J, (1988) Phylogenies from molecular sequences: inference and reliability. Annu Rev Genet 22: 521-565.
    • (1988) Annu Rev Genet , vol.22 , pp. 521-565
    • Felsenstein, J.1
  • 43
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • Guindon S, Gascuel O, (2003) A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst Biol 52: 696-704.
    • (2003) Syst Biol , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 44
    • 0034849408 scopus 로고    scopus 로고
    • MRBAYES: Bayesian inference of phylogenetic trees
    • Huelsenbeck JP, Ronquist F, (2001) MRBAYES: Bayesian inference of phylogenetic trees. Bioinformatics 17: 754-755.
    • (2001) Bioinformatics , vol.17 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 45
    • 0021866533 scopus 로고
    • Amino acid replacements that compensate for a large polypeptide deletion in an enzyme
    • Ho C, Jasin M, Schimmel P, (1985) Amino acid replacements that compensate for a large polypeptide deletion in an enzyme. Science 229: 389-393.
    • (1985) Science , vol.229 , pp. 389-393
    • Ho, C.1    Jasin, M.2    Schimmel, P.3
  • 46
    • 0021088768 scopus 로고
    • Molecular arangement of functional domains along the sequence of an aminoacyl-tRNA synthetase
    • Jasin M, Regan L, Schimmel P, (1983) Molecular arangement of functional domains along the sequence of an aminoacyl-tRNA synthetase. Nature 306: 441-447.
    • (1983) Nature , vol.306 , pp. 441-447
    • Jasin, M.1    Regan, L.2    Schimmel, P.3
  • 47
    • 0021287190 scopus 로고
    • Dispensable pieces of an aminoacyl-tRNA synthetase which activate the catalytic site
    • Jasin M, Regan L, Schimmel P, (1984) Dispensable pieces of an aminoacyl-tRNA synthetase which activate the catalytic site. Cell 36: 1089-1095.
    • (1984) Cell , vol.36 , pp. 1089-1095
    • Jasin, M.1    Regan, L.2    Schimmel, P.3
  • 48
    • 0028985260 scopus 로고
    • Transcriptional Regulation of the Interferon-inducible Tryptophanyl-tRNA Synthetase Includes Alternative Splicing
    • Tolstrup AB, Bejder A, Fleckner J, Justesen J, (1995) Transcriptional Regulation of the Interferon-inducible Tryptophanyl-tRNA Synthetase Includes Alternative Splicing. J Biol Chem 270: 397-403.
    • (1995) J Biol Chem , vol.270 , pp. 397-403
    • Tolstrup, A.B.1    Bejder, A.2    Fleckner, J.3    Justesen, J.4
  • 49
    • 18144400079 scopus 로고    scopus 로고
    • Human lysyl-tRNA synthetase is secreted to trigger proinflammatory response
    • Park SG, Kim HJ, Min YH, Choi E-C, Shin YK, et al. (2005) Human lysyl-tRNA synthetase is secreted to trigger proinflammatory response. Proc Natl Acad Sci USA 102: 6356-6361.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6356-6361
    • Park, S.G.1    Kim, H.J.2    Min, Y.H.3    Choi, E.-C.4    Shin, Y.K.5
  • 50
    • 0028361971 scopus 로고
    • A peptide derived from the amino terminus of endothelial-monocyte-activating polypeptide II modulates mononuclear and polymorphonuclear leukocyte functions, defines an apparently novel cellular interaction site, and induces an acute inflammatory response
    • Kao J, Fan YG, Haehnel I, Brett J, Greenberg S, et al. (1994) A peptide derived from the amino terminus of endothelial-monocyte-activating polypeptide II modulates mononuclear and polymorphonuclear leukocyte functions, defines an apparently novel cellular interaction site, and induces an acute inflammatory response. J Biol Chem 269: 9774-9782.
    • (1994) J Biol Chem , vol.269 , pp. 9774-9782
    • Kao, J.1    Fan, Y.G.2    Haehnel, I.3    Brett, J.4    Greenberg, S.5
  • 51
    • 0033551781 scopus 로고    scopus 로고
    • Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase
    • Wakasugi K, Schimmel P, (1999) Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase. J Biol Chem 274: 23155-23159.
    • (1999) J Biol Chem , vol.274 , pp. 23155-23159
    • Wakasugi, K.1    Schimmel, P.2
  • 52
    • 0343618479 scopus 로고    scopus 로고
    • Footprints of aminoacyl-tRNA synthetases are everywhere
    • Schimmel P, Ribas De Pouplana L, (2000) Footprints of aminoacyl-tRNA synthetases are everywhere. Trends Biochem Sci 25: 207-209.
    • (2000) Trends Biochem Sci , vol.25 , pp. 207-209
    • Schimmel, P.1    Ribas de Pouplana, L.2
  • 53
    • 55749083195 scopus 로고    scopus 로고
    • The impact of Meth A fibrosarcoma derived EMAP II on dendritic cell migration
    • Haridas S, Bowers M, Tusano J, Mehojah J, Kirkpatrick M, et al. (2008) The impact of Meth A fibrosarcoma derived EMAP II on dendritic cell migration. Cytokine 44: 304-309.
    • (2008) Cytokine , vol.44 , pp. 304-309
    • Haridas, S.1    Bowers, M.2    Tusano, J.3    Mehojah, J.4    Kirkpatrick, M.5
  • 54
    • 33746031420 scopus 로고    scopus 로고
    • Endothelial-monocyte-activating polypeptide II induces migration of endothelial progenitor cells via the chemokine receptor CXCR3
    • Hou Y, Plett PA, Ingram DA, Rajashekhar G, Orschell CM, et al. (2006) Endothelial-monocyte-activating polypeptide II induces migration of endothelial progenitor cells via the chemokine receptor CXCR3. Exp Hematol 34: 1125-1132.
    • (2006) Exp Hematol , vol.34 , pp. 1125-1132
    • Hou, Y.1    Plett, P.A.2    Ingram, D.A.3    Rajashekhar, G.4    Orschell, C.M.5
  • 55
    • 0023387480 scopus 로고
    • Entamoeba histolytica: chemoattractant activity for gerbil neutrophils in vivo and in vitro
    • Chadee K, Moreau F, Meerovitch E, (1987) Entamoeba histolytica: chemoattractant activity for gerbil neutrophils in vivo and in vitro. Exp Parasitol 64: 12-23.
    • (1987) Exp Parasitol , vol.64 , pp. 12-23
    • Chadee, K.1    Moreau, F.2    Meerovitch, E.3
  • 56
    • 0024309034 scopus 로고
    • Chemoattractant activity of Entamoeba histolytica for human polymorphonuclear neutrophils
    • Salata RA, Ahmed P, Ravdin JI, (1989) Chemoattractant activity of Entamoeba histolytica for human polymorphonuclear neutrophils. J Parasitol 75: 644-646.
    • (1989) J Parasitol , vol.75 , pp. 644-646
    • Salata, R.A.1    Ahmed, P.2    Ravdin, J.I.3
  • 57
    • 47649101100 scopus 로고    scopus 로고
    • Chemotaxis of Entamoeba histolytica towards the pro-inflammatory cytokine TNF is based on PI3K signalling, cytoskeleton reorganization and the Galactose/N-acetylgalactosamine lectin activity
    • Blazquez S, Guigon G, Weber C, Syan S, Sismeiro O, et al. (2008) Chemotaxis of Entamoeba histolytica towards the pro-inflammatory cytokine TNF is based on PI3K signalling, cytoskeleton reorganization and the Galactose/N-acetylgalactosamine lectin activity. Cell Microbiol 10: 1676-1686.
    • (2008) Cell Microbiol , vol.10 , pp. 1676-1686
    • Blazquez, S.1    Guigon, G.2    Weber, C.3    Syan, S.4    Sismeiro, O.5
  • 58
    • 58649108302 scopus 로고    scopus 로고
    • IL-6 and Stat3 are required for survival of intestinal epithelial cells and development of colitis-associated cancer
    • Grivennikov S, Karin E, Terzic J, Mucida D, Yu GY, et al. (2009) IL-6 and Stat3 are required for survival of intestinal epithelial cells and development of colitis-associated cancer. Cancer Cell 15: 103-113.
    • (2009) Cancer Cell , vol.15 , pp. 103-113
    • Grivennikov, S.1    Karin, E.2    Terzic, J.3    Mucida, D.4    Yu, G.Y.5
  • 59
    • 77149154668 scopus 로고    scopus 로고
    • STAT3 and its activators in intestinal defense and mucosal homeostasis
    • Hruz P, Dann SM, Eckmann L, (2010) STAT3 and its activators in intestinal defense and mucosal homeostasis. Curr Opin Gastroenterol 26: 109-115.
    • (2010) Curr Opin Gastroenterol , vol.26 , pp. 109-115
    • Hruz, P.1    Dann, S.M.2    Eckmann, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.