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Volumn 86, Issue 3, 2005, Pages 365-377

Modulation of NB4 promyelocytic leukemic cell machinery by Anaplasma phagocytophilum

Author keywords

2D DIGE; Anaplasma phagocytophilum; Ehrlichia spp.; Microarray; NB4

Indexed keywords

CELL ADHESION MOLECULE; CYTOKINE; FERRITIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON REGULATORY FACTOR 3; MYELOID DIFFERENTIATION FACTOR 88; POLYPEPTIDE; TOLL LIKE RECEPTOR; TRANSCRIPTION FACTOR; TRANSFERRIN; TRANSFERRIN RECEPTOR;

EID: 23344451806     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ygeno.2005.05.008     Document Type: Article
Times cited : (32)

References (44)
  • 1
    • 0035192367 scopus 로고    scopus 로고
    • Reorganization of genera in the families Rickettsiaceae and Anaplasmataceae in the order Rickettsiales: Unification of some species of Ehrlichia with Anaplasma, Cowdria with Ehrlichia and Ehrlichia with Neorickettsia, descriptions of six new species combinations and designation of Ehrlichia equi and 'HGE agent' as subjective synonyms of Ehrlichia phagocytophila
    • J.S. Dumler, A.F. Barbet, C.P.J. Bekker, G.A. Dasch, G.H. Palmer, and S.C. Ray Reorganization of genera in the families Rickettsiaceae and Anaplasmataceae in the order Rickettsiales: unification of some species of Ehrlichia with Anaplasma, Cowdria with Ehrlichia and Ehrlichia with Neorickettsia, descriptions of six new species combinations and designation of Ehrlichia equi and 'HGE agent' as subjective synonyms of Ehrlichia phagocytophila Int. J. Syst. Evol. Microbiol. 51 2001 2145 2165
    • (2001) Int. J. Syst. Evol. Microbiol. , vol.51 , pp. 2145-2165
    • Dumler, J.S.1    Barbet, A.F.2    Bekker, C.P.J.3    Dasch, G.A.4    Palmer, G.H.5    Ray, S.C.6
  • 2
    • 0030829324 scopus 로고    scopus 로고
    • Human monocytic and granulocytic ehrlichioses: Discovery and diagnosis of emerging tick-borne infections and the critical role of the pathologist
    • D.H. Walker, and J.S. Dumler Human monocytic and granulocytic ehrlichioses: discovery and diagnosis of emerging tick-borne infections and the critical role of the pathologist Arch. Pathol. Lab. Med 121 1997 785 791
    • (1997) Arch. Pathol. Lab. Med , vol.121 , pp. 785-791
    • Walker, D.H.1    Dumler, J.S.2
  • 3
    • 3543147269 scopus 로고    scopus 로고
    • Ecology of Anaplasma phagocytophilum and Borrelia burgdorferi in the western United States
    • J.E. Foley, P. Foley, R.N. Brown, R.S. Lane, J.S. Dumler, and J.E. Madigan Ecology of Anaplasma phagocytophilum and Borrelia burgdorferi in the western United States J. Vector Ecol. 2004 (June) 41 50
    • (2004) J. Vector Ecol. , pp. 41-50
    • Foley, J.E.1    Foley, P.2    Brown, R.N.3    Lane, R.S.4    Dumler, J.S.5    Madigan, J.E.6
  • 4
  • 5
    • 0036150092 scopus 로고    scopus 로고
    • Rapid activation of protein tyrosine kinase and phospholipase C-γ2 and increase in cytosolic free calcium are required by Ehrlichia chaffeensis for internalization and growth in THP-1 cells
    • M. Lin, M.X. Zhu, and Y. Rikihisa Rapid activation of protein tyrosine kinase and phospholipase C-γ2 and increase in cytosolic free calcium are required by Ehrlichia chaffeensis for internalization and growth in THP-1 cells Infect. Immun. 70 2002 889 898
    • (2002) Infect. Immun. , vol.70 , pp. 889-898
    • Lin, M.1    Zhu, M.X.2    Rikihisa, Y.3
  • 6
    • 0030959591 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis are early endosomes, which selectively accumulate transferrin receptor
    • R.E. Barnewall, Y. Rikihisa, and E.H. Lee Ehrlichia chaffeensis are early endosomes, which selectively accumulate transferrin receptor Infect. Immun. 65 1997 1455 1461
    • (1997) Infect. Immun. , vol.65 , pp. 1455-1461
    • Barnewall, R.E.1    Rikihisa, Y.2    Lee, E.H.3
  • 7
    • 0033916679 scopus 로고    scopus 로고
    • Granulocytic ehrlichiosis in mice deficient in phagocyte oxidase or inducible nitric oxide synthase
    • R. Banerjee, J. Anguita, and E. Fikrig Granulocytic ehrlichiosis in mice deficient in phagocyte oxidase or inducible nitric oxide synthase Infect. Immun. 68 2000 4361 4362
    • (2000) Infect. Immun. , vol.68 , pp. 4361-4362
    • Banerjee, R.1    Anguita, J.2    Fikrig, E.3
  • 8
    • 0033914787 scopus 로고    scopus 로고
    • The agent of human granulocytic ehrlichiosis induces the production of myelosuppressing chemokines without induction of proinflammatory cytokines
    • M.B. Klein, S. Hu, C.C. Chao, and J.L. Goodman The agent of human granulocytic ehrlichiosis induces the production of myelosuppressing chemokines without induction of proinflammatory cytokines J. Infect. Dis. 182 2000 200 205
    • (2000) J. Infect. Dis. , vol.182 , pp. 200-205
    • Klein, M.B.1    Hu, S.2    Chao, C.C.3    Goodman, J.L.4
  • 9
    • 0034100619 scopus 로고    scopus 로고
    • Gamma interferon dominates the murine cytokine response to the agent of human granulocytic ehrlichiosis and helps to control the degree of early rickettsemia
    • M. Akkoyunlu, and E. Fikrig Gamma interferon dominates the murine cytokine response to the agent of human granulocytic ehrlichiosis and helps to control the degree of early rickettsemia Infect. Immun. 68 2000 1827 1833
    • (2000) Infect. Immun. , vol.68 , pp. 1827-1833
    • Akkoyunlu, M.1    Fikrig, E.2
  • 11
    • 0041764407 scopus 로고    scopus 로고
    • Diminished adhesion of Anaplasma phagocytophilum-infected neutrophils to endothelial cells is associated with reduced expression of leukocyte surface selectin
    • K.S. Choi, J. Garyu, J. Park, and J.S. Dumler Diminished adhesion of Anaplasma phagocytophilum-infected neutrophils to endothelial cells is associated with reduced expression of leukocyte surface selectin Infect. Immun. 71 2003 4586 4594
    • (2003) Infect. Immun. , vol.71 , pp. 4586-4594
    • Choi, K.S.1    Garyu, J.2    Park, J.3    Dumler, J.S.4
  • 13
    • 0025109079 scopus 로고
    • Failure of f-Met-Leu-Phe to induce chemotaxis in differentiated promyelocytic (HL-60) leukemia cells
    • A.A. Sirak, J.D. Laskin, F.M. Robertson, and D.L. Laskin Failure of f-Met-Leu-Phe to induce chemotaxis in differentiated promyelocytic (HL-60) leukemia cells J. Leukoc. Biol. 48 1990 333 342
    • (1990) J. Leukoc. Biol. , vol.48 , pp. 333-342
    • Sirak, A.A.1    Laskin, J.D.2    Robertson, F.M.3    Laskin, D.L.4
  • 14
    • 0034861225 scopus 로고    scopus 로고
    • Exploitation of interleukin-8-induced neutrophil chemotaxis by the agent of human granulocytic anaplasmosis
    • M. Akkoyunlu, S.E. Malawista, J. Anguita, and E. Fikrig Exploitation of interleukin-8-induced neutrophil chemotaxis by the agent of human granulocytic anaplasmosis Infect. Immun. 69 2001 5577 5588
    • (2001) Infect. Immun. , vol.69 , pp. 5577-5588
    • Akkoyunlu, M.1    Malawista, S.E.2    Anguita, J.3    Fikrig, E.4
  • 15
    • 0026013478 scopus 로고
    • NB4, a maturation inducible cell line with the t(15;17) marker isolated from a human acute promyelocytic leukemia (M3)
    • M. Lanotte, V. Martin-Thouvenin, S. Najman, P. Balerini, F. Valensi, and R. Berger NB4, a maturation inducible cell line with the t(15;17) marker isolated from a human acute promyelocytic leukemia (M3) Blood 77 1991 1080 1086
    • (1991) Blood , vol.77 , pp. 1080-1086
    • Lanotte, M.1    Martin-Thouvenin, V.2    Najman, S.3    Balerini, P.4    Valensi, F.5    Berger, R.6
  • 16
    • 18244397924 scopus 로고    scopus 로고
    • Heterogeneity of functional responses in differentiated myeloid cell lines reveals EPRO cells as a valid model of murine neutrophil functional activation
    • P. Gaines, J. Chi, and N. Berliner Heterogeneity of functional responses in differentiated myeloid cell lines reveals EPRO cells as a valid model of murine neutrophil functional activation J. Leukoc. Biol. 77 2005 1 11
    • (2005) J. Leukoc. Biol. , vol.77 , pp. 1-11
    • Gaines, P.1    Chi, J.2    Berliner, N.3
  • 17
    • 0037114184 scopus 로고    scopus 로고
    • Repression of rac2 mRNA expression by Anaplasma phagocytophilum is essential to the inhibition of superoxide production and bacterial proliferation
    • J.A. Carlyon, W.-T. Chan, J. Galan, D. Roos, and E. Fikrig Repression of rac2 mRNA expression by Anaplasma phagocytophilum is essential to the inhibition of superoxide production and bacterial proliferation J. Immunol. 169 2002 7009 7018
    • (2002) J. Immunol. , vol.169 , pp. 7009-7018
    • Carlyon, J.A.1    Chan, W.-T.2    Galan, J.3    Roos, D.4    Fikrig, E.5
  • 18
    • 15944425755 scopus 로고    scopus 로고
    • Gene expression profiling of human promyelocytic cells in response to infection with Anaplasma phagocytophilum
    • J. De la Fuente, P. Ayobi, E.F. Blouin, C. Almazan, V. Naranjo, and K.M. Kocan Gene expression profiling of human promyelocytic cells in response to infection with Anaplasma phagocytophilum Cell Microbiol. 7 2005 549 559
    • (2005) Cell Microbiol. , vol.7 , pp. 549-559
    • De La Fuente, J.1    Ayobi, P.2    Blouin, E.F.3    Almazan, C.4    Naranjo, V.5    Kocan, K.M.6
  • 19
    • 18744367006 scopus 로고    scopus 로고
    • Insights into pathogen immune evasion mechanisms: Anaplasma phagocytophilum fails to induce an apoptosis differentiation program in human neutrophils
    • D.L. Borjesson, S.D. Kobayashi, A.R. Whitney, J.M. Voyich, C.M. Argue, and F.R. DeLeo Insights into pathogen immune evasion mechanisms: Anaplasma phagocytophilum fails to induce an apoptosis differentiation program in human neutrophils J. Immunol. 174 2005 6364 6372
    • (2005) J. Immunol. , vol.174 , pp. 6364-6372
    • Borjesson, D.L.1    Kobayashi, S.D.2    Whitney, A.R.3    Voyich, J.M.4    Argue, C.M.5    Deleo, F.R.6
  • 20
    • 4544382411 scopus 로고    scopus 로고
    • Neutrophil NADPH oxidase is reduced at the Anaplasma phagocytophilum phagosome
    • J.W. Ijdo, and A.C. Mueller Neutrophil NADPH oxidase is reduced at the Anaplasma phagocytophilum phagosome Infect. Immun. 72 2004 5392 5401
    • (2004) Infect. Immun. , vol.72 , pp. 5392-5401
    • Ijdo, J.W.1    Mueller, A.C.2
  • 21
    • 0036071945 scopus 로고    scopus 로고
    • Roles of p38 mitogen-activated protein kinase, NF-κB, and protein kinase C in proinflammatory cytokine mRNA expression by human peripheral blood leukocytes, monocytes, and neutrophils in response to Anaplasma phagocytophilum
    • H.-Y. Kim, and Y. Rikihisa Roles of p38 mitogen-activated protein kinase, NF-κB, and protein kinase C in proinflammatory cytokine mRNA expression by human peripheral blood leukocytes, monocytes, and neutrophils in response to Anaplasma phagocytophilum Infect. Immun. 70 2002 4132 4141
    • (2002) Infect. Immun. , vol.70 , pp. 4132-4141
    • Kim, H.-Y.1    Rikihisa, Y.2
  • 22
    • 0142217168 scopus 로고    scopus 로고
    • Obligately intracellular parasitism by Ehrlichia chaffeensis and Anaplasma phagocytophilum involves caveolae and glycosylphosphatidylinositol- anchored proteins
    • M. Lin, and Y. Rikihisa Obligately intracellular parasitism by Ehrlichia chaffeensis and Anaplasma phagocytophilum involves caveolae and glycosylphosphatidylinositol-anchored proteins Cell Microbiol. 5 2003 809 820
    • (2003) Cell Microbiol. , vol.5 , pp. 809-820
    • Lin, M.1    Rikihisa, Y.2
  • 23
    • 0347511899 scopus 로고    scopus 로고
    • Survival strategy of obligately intracellular Ehrlichia chaffeensis: Novel modulation of immune response and host cell cycles
    • J.-Z. Zhang, M. Sinha, B.A. Luxon, and X.-J. Yu Survival strategy of obligately intracellular Ehrlichia chaffeensis: novel modulation of immune response and host cell cycles Infect. Immun. 72 2004 498 507
    • (2004) Infect. Immun. , vol.72 , pp. 498-507
    • Zhang, J.-Z.1    Sinha, M.2    Luxon, B.A.3    Yu, X.-J.4
  • 24
    • 3442897088 scopus 로고    scopus 로고
    • Control of Anaplasma phagocytophilum, an obligate intracellular pathogen, in the absence o inducible nitric oxide synthase, phagocyte NADPH oxidase, tumor necrosis factor, Toll-like receptor (TLR) 2 and TLR4, or the TLR adaptor molecule MyD88
    • F.D. von Loewenich, D.G. Scorpio, U. Reischl, J.S. Dumler, and C. Bogdan Control of Anaplasma phagocytophilum, an obligate intracellular pathogen, in the absence o inducible nitric oxide synthase, phagocyte NADPH oxidase, tumor necrosis factor, Toll-like receptor (TLR) 2 and TLR4, or the TLR adaptor molecule MyD88 Eur. J. Immunol. 34 2004 1789 1797
    • (2004) Eur. J. Immunol. , vol.34 , pp. 1789-1797
    • Von Loewenich, F.D.1    Scorpio, D.G.2    Reischl, U.3    Dumler, J.S.4    Bogdan, C.5
  • 25
    • 0032910502 scopus 로고    scopus 로고
    • Leukocyte infection by the granulocytic ehrlichiosis agent is linked to expression of a selectin ligand
    • J.L. Goodman, C.M. Nelson, M.B. Klein, S.F. Hayes, and B.W. Weston Leukocyte infection by the granulocytic ehrlichiosis agent is linked to expression of a selectin ligand J. Clin. Invest. 103 1999 407 412
    • (1999) J. Clin. Invest. , vol.103 , pp. 407-412
    • Goodman, J.L.1    Nelson, C.M.2    Klein, M.B.3    Hayes, S.F.4    Weston, B.W.5
  • 26
    • 0034595997 scopus 로고    scopus 로고
    • Intracellular parasitism by the human granulocytic ehrlichiosis bacterium through the P-Selectin ligand, PSGL-1
    • M.J. Herron, C.M. Nelson, J. Larson, K.R. Snapp, G.S. Kansas, and J.L. Goodman Intracellular parasitism by the human granulocytic ehrlichiosis bacterium through the P-Selectin ligand, PSGL-1 Science 288 2000 1653 1656
    • (2000) Science , vol.288 , pp. 1653-1656
    • Herron, M.J.1    Nelson, C.M.2    Larson, J.3    Snapp, K.R.4    Kansas, G.S.5    Goodman, J.L.6
  • 27
    • 0033969660 scopus 로고    scopus 로고
    • Intracellular infection by the human granulocytic ehrlichiosis agent inhibits human neutrophil apoptosis
    • K. Yoshiie, H.Y. Kim, J. Mott, and Y. Rikihisa Intracellular infection by the human granulocytic ehrlichiosis agent inhibits human neutrophil apoptosis Infect. Immun. 68 2000 1125 1133
    • (2000) Infect. Immun. , vol.68 , pp. 1125-1133
    • Yoshiie, K.1    Kim, H.Y.2    Mott, J.3    Rikihisa, Y.4
  • 28
    • 0344405661 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum reduces neutrophil apoptosis in vivo
    • H. Scaiffe, Z. Woldehiwet, C.A. Hart, and S.W. Edwards Anaplasma phagocytophilum reduces neutrophil apoptosis in vivo Infect. Immun. 71 2003 1995 2001
    • (2003) Infect. Immun. , vol.71 , pp. 1995-2001
    • Scaiffe, H.1    Woldehiwet, Z.2    Hart, C.A.3    Edwards, S.W.4
  • 29
    • 12444278282 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum inhibits human neutrophil apoptosis via up-regulation of bfl-1, maintenance of mitochondrial membrane potential and prevention of caspase 3 activation
    • Y. Ge, K. Yoshiie, F. Kuribayashi, M. Lin, and Y. Rikihisa Anaplasma phagocytophilum inhibits human neutrophil apoptosis via up-regulation of bfl-1, maintenance of mitochondrial membrane potential and prevention of caspase 3 activation Cell Microbiol. 7 2005 29 38
    • (2005) Cell Microbiol. , vol.7 , pp. 29-38
    • Ge, Y.1    Yoshiie, K.2    Kuribayashi, F.3    Lin, M.4    Rikihisa, Y.5
  • 30
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: Regulators of the cellular life-or-death switch
    • S. Cory, and J.M. Adams The Bcl2 family: regulators of the cellular life-or-death switch Nat. Rev. Cancer 2 2002 647 656
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 32
    • 0027938009 scopus 로고
    • Abrogation of gamma interferon-induced inhibition of Ehrlichia chaffeensis infection in human monocytes with iron transferrin
    • R.E. Barnewall, and Y. Rikihisa Abrogation of gamma interferon-induced inhibition of Ehrlichia chaffeensis infection in human monocytes with iron transferrin Infect. Immun. 62 1994 4804 4810
    • (1994) Infect. Immun. , vol.62 , pp. 4804-4810
    • Barnewall, R.E.1    Rikihisa, Y.2
  • 33
    • 0032900986 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis and E. sennetsu, but not the human granulocytic ehrlichiosis agent, co-localize with transferrin receptor and up-regulate transferrin mRNA by activating iron-responsive protein 1
    • R.E. Barnewall, N. Ohashi, and Y. Rikihisa Ehrlichia chaffeensis and E. sennetsu, but not the human granulocytic ehrlichiosis agent, co-localize with transferrin receptor and up-regulate transferrin mRNA by activating iron-responsive protein 1 Infect. Immun. 67 1999 2258 2265
    • (1999) Infect. Immun. , vol.67 , pp. 2258-2265
    • Barnewall, R.E.1    Ohashi, N.2    Rikihisa, Y.3
  • 34
    • 11144254408 scopus 로고    scopus 로고
    • An immunoreactive 38-kilodalton protein of Ehrlichia canis shares structural homology and iron-binding capacity with the ferric-ion binding protein family
    • C.K. Doyle, X. Zhang, V. Popov, and J.W. McBride An immunoreactive 38-kilodalton protein of Ehrlichia canis shares structural homology and iron-binding capacity with the ferric-ion binding protein family Infect. Immun. 73 2005 62 69
    • (2005) Infect. Immun. , vol.73 , pp. 62-69
    • Doyle, C.K.1    Zhang, X.2    Popov, V.3    McBride, J.W.4
  • 35
    • 0029679613 scopus 로고    scopus 로고
    • Emergence of the ehrlichioses as human health problems
    • D.H. Walker, and J.S. Dumler Emergence of the ehrlichioses as human health problems Emerg. Infect. Dis. 2 1996 18 29
    • (1996) Emerg. Infect. Dis. , vol.2 , pp. 18-29
    • Walker, D.H.1    Dumler, J.S.2
  • 36
    • 0142217173 scopus 로고    scopus 로고
    • Invasion and survival strategies of Anaplasma phagocytophilum
    • J.A. Carlyon, and E. Fikrig Invasion and survival strategies of Anaplasma phagocytophilum Cell Microbiol. 5 2003 743 754
    • (2003) Cell Microbiol. , vol.5 , pp. 743-754
    • Carlyon, J.A.1    Fikrig, E.2
  • 37
    • 20144389877 scopus 로고    scopus 로고
    • Exogenous and endogenous glycolipid antigens activate NKT cells during microbial infections
    • J. Mattner, K.L. DeBord, N. Ismail, R.D. Goff, C. Cantu III, and D. Zhou Exogenous and endogenous glycolipid antigens activate NKT cells during microbial infections Nature 434 2005 525 529
    • (2005) Nature , vol.434 , pp. 525-529
    • Mattner, J.1    Debord, K.L.2    Ismail, N.3    Goff, R.D.4    Cantu III, C.5    Zhou, D.6
  • 38
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • M. Unlu, M.E. Morgan, and J.S. Minden Difference gel electrophoresis: a single gel method for detecting changes in protein extracts Electrophoresis 18 1997 2071 2077
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 39
    • 0036463947 scopus 로고    scopus 로고
    • Evaluation of two-dimensional differential gel electrophoresis for proteomic expression analysis of a model breast cancer cell system
    • S. Gharbi, P. Gaffney, A. Yang, M.J. Zvelebil, R. Cramer, M.D. Waterfield, and J.F. Timms Evaluation of two-dimensional differential gel electrophoresis for proteomic expression analysis of a model breast cancer cell system Mol. Cell. Proteomics 1 2002 91 98
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 91-98
    • Gharbi, S.1    Gaffney, P.2    Yang, A.3    Zvelebil, M.J.4    Cramer, R.5    Waterfield, M.D.6    Timms, J.F.7
  • 40
    • 0034595617 scopus 로고    scopus 로고
    • Lack of a role of iron in the Lyme disease pathogen
    • J.E. Posey, and F.C. Gherardini Lack of a role of iron in the Lyme disease pathogen Science 288 2000 1651 1653
    • (2000) Science , vol.288 , pp. 1651-1653
    • Posey, J.E.1    Gherardini, F.C.2
  • 42
    • 0033844429 scopus 로고    scopus 로고
    • Expression of genes involved in initiation, regulation, and execution of apoptosis in human neutrophils and during neutrophil differentiation of HL-60 cells
    • A.M. Santos-Beneit, and F. Mollinedo Expression of genes involved in initiation, regulation, and execution of apoptosis in human neutrophils and during neutrophil differentiation of HL-60 cells J. Leukoc. Biol 67 2000 712 724
    • (2000) J. Leukoc. Biol , vol.67 , pp. 712-724
    • Santos-Beneit, A.M.1    Mollinedo, F.2
  • 43
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • M.W. Pfaffl, G.W. Horgan, and L. Dempfle Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR Nucleic Acids Res. 30 2002 e36
    • (2002) Nucleic Acids Res. , vol.30 , pp. 36
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 44
    • 4444326879 scopus 로고    scopus 로고
    • Proteome and transcriptome analysis of retinoic acid-induced differentiation of human promyelocytic leukemia cells, NB4
    • D. Wang, R. Jensen, G. Gendeh, K. Williams, and M.G. Pallavicini Proteome and transcriptome analysis of retinoic acid-induced differentiation of human promyelocytic leukemia cells, NB4 J. Protein Res. 3 2004 627 635
    • (2004) J. Protein Res. , vol.3 , pp. 627-635
    • Wang, D.1    Jensen, R.2    Gendeh, G.3    Williams, K.4    Pallavicini, M.G.5


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