메뉴 건너뛰기




Volumn 11, Issue 7, 2010, Pages 823-833

The potential and limitations of p38MAPK as a drug target for the treatment of hematological malignancies

Author keywords

Apoptosis; Bone marrow stroma; Chemotherapy; Hematological malignancy; p38MAPK; Proliferation

Indexed keywords

2 CYANO 3,12 DIOXOOLEANA 1,9 DIEN 28 OIC ACID; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; ARSENIC DERIVATIVE; ARSENIC SULFIDE; ARSENIC TRIOXIDE; BCR ABL PROTEIN; BORTEZOMIB; CLADRIBINE; CYTARABINE; DEXAMETHASONE; ETOPOSIDE; GENISTEIN; GW 856553; HISTONE DEACETYLASE INHIBITOR; IMATINIB; METHOTREXATE; MITOGEN ACTIVATED PROTEIN KINASE P38; NONSTEROID ANTIINFLAMMATORY AGENT; PAMAPIMOD; RESVERATROL; RITUXIMAB; RO 4402257; SB 681323; SCIO 469; SEMAPIMOD; SULINDAC; UNCLASSIFIED DRUG; VINBLASTINE; VX 702;

EID: 77954726295     PISSN: 13894501     EISSN: None     Source Type: Journal    
DOI: 10.2174/138945010791320854     Document Type: Article
Times cited : (26)

References (164)
  • 1
    • 0033965158 scopus 로고    scopus 로고
    • The p38 signal transduction pathway: Activation and function
    • Ono K, Han J. The p38 signal transduction pathway: activation and function. Cell Signal 2000; 12: 1-13.
    • (2000) Cell Signal , vol.12 , pp. 1-13
    • Ono, K.1    Han, J.2
  • 2
    • 0037040869 scopus 로고    scopus 로고
    • Activation of the p38 mitogen-activated protein kinase mediates the suppressive effects of type I interferons and transforming growth factor-beta on normal hematopoiesis
    • Verma A, Deb DK, Sassano A, et al. Activation of the p38 mitogen-activated protein kinase mediates the suppressive effects of type I interferons and transforming growth factor-beta on normal hematopoiesis. J Biol Chem 2002; 277: 7726-35.
    • (2002) J Biol Chem , vol.277 , pp. 7726-7735
    • Verma, A.1    Deb, D.K.2    Sassano, A.3
  • 3
    • 0030828701 scopus 로고    scopus 로고
    • Characterization of the structure and function of the fourth member of p38 group mitogen-activated protein kinases, p38delta
    • Jiang Y, Gram H, Zhao M, et al. Characterization of the structure and function of the fourth member of p38 group mitogen-activated protein kinases, p38delta. J Biol Chem 1997; 272: 30122-8.
    • (1997) J Biol Chem , vol.272 , pp. 30122-30128
    • Jiang, Y.1    Gram, H.2    Zhao, M.3
  • 4
    • 0033622470 scopus 로고    scopus 로고
    • Essential role of p38alpha MAP kinase in placental but not embryonic cardiovascular development
    • Adams RH, Porras A, Alonso G, et al. Essential role of p38alpha MAP kinase in placental but not embryonic cardiovascular development. Mol Cell 2000; 6: 109-16.
    • (2000) Mol Cell , vol.6 , pp. 109-116
    • Adams, R.H.1    Porras, A.2    Alonso, G.3
  • 5
    • 0034641614 scopus 로고    scopus 로고
    • Essential role for p38alpha mitogen-activated protein kinase in placental angiogenesis
    • Mudgett J, Ding J, Guh-Siesel L, et al. Essential role for p38alpha mitogen-activated protein kinase in placental angiogenesis. Proc Natl Acad Sci USA 2000; 97: 10454-9.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10454-10459
    • Mudgett, J.1    Ding, J.2    Guh-Siesel, L.3
  • 6
    • 27944461325 scopus 로고    scopus 로고
    • Generation and characterization of p38beta (MAPK11) gene-targeted mice
    • Beardmore VA, Hinton HJ, Eftychi C, et al. Generation and characterization of p38beta (MAPK11) gene-targeted mice. Mol Cell Biol 2005; 25: 10454-64.
    • (2005) Mol Cell Biol , vol.25 , pp. 10454-10464
    • Beardmore, V.A.1    Hinton, H.J.2    Eftychi, C.3
  • 7
    • 20244365497 scopus 로고    scopus 로고
    • p38gamma regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP
    • Sabio G, Arthur JS, Kuma Y, et al. p38gamma regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP. EMBO J 2005; 24: 1134-45.
    • (2005) EMBO J , vol.24 , pp. 1134-1145
    • Sabio, G.1    Arthur, J.S.2    Kuma, Y.3
  • 9
    • 0030756286 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel p38 mitogen-activated protein kinase
    • Wang XS, Diener K, Manthey CL, et al. Molecular cloning and characterization of a novel p38 mitogen-activated protein kinase. J Biol Chem 1997; 272: 23668-74.
    • (1997) J Biol Chem , vol.272 , pp. 23668-23674
    • Wang, X.S.1    Diener, K.2    Manthey, C.L.3
  • 10
    • 0030805915 scopus 로고    scopus 로고
    • p38-2, a novel mitogen- activated protein kinase with distinct properties
    • Stein B, Yang MX, Young DB, et al. p38-2, a novel mitogen- activated protein kinase with distinct properties. J Biol Chem 1997; 272: 19509-17.
    • (1997) J Biol Chem , vol.272 , pp. 19509-19517
    • Stein, B.1    Yang, M.X.2    Young, D.B.3
  • 11
    • 0029982565 scopus 로고    scopus 로고
    • Characterization of the structure and function of a new mitogen-activated protein kinase (p38beta)
    • Jiang Y, Chen C, Li Z, et al. Characterization of the structure and function of a new mitogen-activated protein kinase (p38beta). J Biol Chem 1996; 271: 17920-6.
    • (1996) J Biol Chem , vol.271 , pp. 17920-17926
    • Jiang, Y.1    Chen, C.2    Li, Z.3
  • 12
    • 0033773187 scopus 로고    scopus 로고
    • Haloperidol-induced neuronal apoptosis: Role of p38 and c-Jun-NH(2)-terminal protein kinase
    • Noh JS, Kang HJ, Kim EY, et al. Haloperidol-induced neuronal apoptosis: role of p38 and c-Jun-NH(2)-terminal protein kinase. J Neurochem 2000; 75: 2327-34.
    • (2000) J Neurochem , vol.75 , pp. 2327-2334
    • Noh, J.S.1    Kang, H.J.2    Kim, E.Y.3
  • 13
    • 0032212557 scopus 로고    scopus 로고
    • Purification and activation of recombinant p38 isoforms alpha, beta, gamma, and delta
    • Keesler GA, Bray J, Hunt J, et al. Purification and activation of recombinant p38 isoforms alpha, beta, gamma, and delta. Protein Expr Purif 1998; 14: 221-8.
    • (1998) Protein Expr Purif , vol.14 , pp. 221-228
    • Keesler, G.A.1    Bray, J.2    Hunt, J.3
  • 14
    • 0031916832 scopus 로고    scopus 로고
    • Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6
    • Enslen H, Raingeaud J, Davis RJ. Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6. J Biol Chem 1998; 273: 1741-8.
    • (1998) J Biol Chem , vol.273 , pp. 1741-1748
    • Enslen, H.1    Raingeaud, J.2    Davis, R.J.3
  • 15
    • 0037083375 scopus 로고    scopus 로고
    • MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha
    • Ge B, Gram H, Di Padova F, et al. MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha. Science 2002; 295: 1291-4.
    • (2002) Science , vol.295 , pp. 1291-1294
    • Ge, B.1    Gram, H.2    Di Padova, F.3
  • 16
    • 16844367955 scopus 로고    scopus 로고
    • Alternative p38 activation pathway mediated by T cell receptor-proximal tyrosine kinases
    • Salvador JM, Mittelstadt PR, Guszczynski T, et al. Alternative p38 activation pathway mediated by T cell receptor-proximal tyrosine kinases. Nat Immunol 2005; 6: 390-5.
    • (2005) Nat Immunol , vol.6 , pp. 390-395
    • Salvador, J.M.1    Mittelstadt, P.R.2    Guszczynski, T.3
  • 17
    • 20444437586 scopus 로고    scopus 로고
    • Casein kinase 2- and protein kinase A-regulated adenomatous polyposis coli and beta-catenin cellular localization is dependent on p38 MAPK
    • Hildesheim J, Salvador JM, Hollander MC, Fornace AJ Jr. Casein kinase 2- and protein kinase A-regulated adenomatous polyposis coli and beta-catenin cellular localization is dependent on p38 MAPK. J Biol Chem 2005; 280: 17221-6.
    • (2005) J Biol Chem , vol.280 , pp. 17221-17226
    • Hildesheim, J.1    Salvador, J.M.2    Hollander, M.C.3    Fornace Jr., A.J.4
  • 18
    • 2342540450 scopus 로고    scopus 로고
    • Nuclear export inhibitors and kinase inhibitors identified using a MAPK-activated protein kinase 2 redistribution screen
    • Almholt DL, Loechel F, Nielsen SJ, et al. Nuclear export inhibitors and kinase inhibitors identified using a MAPK-activated protein kinase 2 redistribution screen. Assay Drug Dev Technol 2004; 2: 7- 20.
    • (2004) Assay Drug Dev Technol , vol.2 , Issue.7 , pp. 20
    • Almholt, D.L.1    Loechel, F.2    Nielsen, S.J.3
  • 19
    • 0030977270 scopus 로고    scopus 로고
    • MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates
    • Fukunaga R, Hunter T. MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. EMBO J 1997; 16: 1921-33.
    • (1997) EMBO J , vol.16 , pp. 1921-1933
    • Fukunaga, R.1    Hunter, T.2
  • 20
    • 0035163198 scopus 로고    scopus 로고
    • Multiple signaling pathways regulate NF-kappaB-dependent transcription of the monocyte chemoattractant protein-1 gene in primary endothelial cells
    • Goebeler M, Gillitzer R, Kilian K, et al. Multiple signaling pathways regulate NF-kappaB-dependent transcription of the monocyte chemoattractant protein-1 gene in primary endothelial cells. Blood 2001; 97: 46-55.
    • (2001) Blood , vol.97 , pp. 46-55
    • Goebeler, M.1    Gillitzer, R.2    Kilian, K.3
  • 21
    • 0035799557 scopus 로고    scopus 로고
    • Initiation of a G2/M checkpoint after ultraviolet radiation requires p38 kinase
    • Bulavin D, Higashimoto Y, Popoff I, et al. Initiation of a G2/M checkpoint after ultraviolet radiation requires p38 kinase. Nature 2001; 411: 102-7.
    • (2001) Nature , vol.411 , pp. 102-107
    • Bulavin, D.1    Higashimoto, Y.2    Popoff, I.3
  • 22
    • 13244260955 scopus 로고    scopus 로고
    • Essential role of p53 phosphorylation by p38 MAPK in apoptosis induction by the HIV-1 envelope
    • Perfettini J-L, Castedo M, Nardacci R, et al. Essential role of p53 phosphorylation by p38 MAPK in apoptosis induction by the HIV-1 envelope. J Exp Med 2005; 201: 279-89.
    • (2005) J Exp Med , vol.201 , pp. 279-289
    • Perfettini, J.-L.1    Castedo, M.2    Nardacci, R.3
  • 23
    • 0035854673 scopus 로고    scopus 로고
    • A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs
    • Tanoue T, Yamamoto T, Maeda R, Nishida E. A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs. J Biol Chem 2001; 276: 26629-39.
    • (2001) J Biol Chem , vol.276 , pp. 26629-26639
    • Tanoue, T.1    Yamamoto, T.2    Maeda, R.3    Nishida, E.4
  • 24
    • 0034697904 scopus 로고    scopus 로고
    • Requirement for p38alpha in erythropoietin expression: A role for stress kinases in erythropoiesis
    • Tamura K, Sudo T, Senftleben U, Dadak AM, Johnson R, Karin M. Requirement for p38alpha in erythropoietin expression: a role for stress kinases in erythropoiesis. Cell 2000; 102: 221-31.
    • (2000) Cell , vol.102 , pp. 221-231
    • Tamura, K.1    Sudo, T.2    Senftleben, U.3    Dadak, A.M.4    Johnson, R.5    Karin, M.6
  • 25
    • 0030788708 scopus 로고    scopus 로고
    • Activation of p38 MAP kinase pathway by erythropoietin and interleukin-3
    • Nagata Y, Moriguchi T, Nishida E, Todokoro K. Activation of p38 MAP kinase pathway by erythropoietin and interleukin-3. Blood 1997; 90: 929-34.
    • (1997) Blood , vol.90 , pp. 929-934
    • Nagata, Y.1    Moriguchi, T.2    Nishida, E.3    Todokoro, K.4
  • 26
    • 0032530921 scopus 로고    scopus 로고
    • Activation of p38 MAP kinase and JNK but not ERK is required for erythropoietin- induced erythroid differentiation
    • Nagata Y, Takahashi N, Davis RJ, Todokoro K. Activation of p38 MAP kinase and JNK but not ERK is required for erythropoietin- induced erythroid differentiation. Blood 1998; 92: 1859-69.
    • (1998) Blood , vol.92 , pp. 1859-1869
    • Nagata, Y.1    Takahashi, N.2    Davis, R.J.3    Todokoro, K.4
  • 27
    • 0034254515 scopus 로고    scopus 로고
    • JNK and p38 are activated by erythropoietin (EPO) but are not induced in apoptosis following EPO withdrawal in EPO-dependent HCD57 cells
    • Jacobs-Helber SM, Ryan JJ, Sawyer ST. JNK and p38 are activated by erythropoietin (EPO) but are not induced in apoptosis following EPO withdrawal in EPO-dependent HCD57 cells. Blood 2000; 96: 933-40.
    • (2000) Blood , vol.96 , pp. 933-940
    • Jacobs-Helber, S.M.1    Ryan, J.J.2    Sawyer, S.T.3
  • 28
    • 0034176006 scopus 로고    scopus 로고
    • Butyrate-induced erythroid differentiation of human K562 leukemia cells involves inhibition of ERK and activation of p38 MAP kinase pathways
    • Witt O, Sand K, Pekrun A. Butyrate-induced erythroid differentiation of human K562 leukemia cells involves inhibition of ERK and activation of p38 MAP kinase pathways. Blood 2000; 95: 2391-6.
    • (2000) Blood , vol.95 , pp. 2391-2396
    • Witt, O.1    Sand, K.2    Pekrun, A.3
  • 29
    • 0037337444 scopus 로고    scopus 로고
    • Different levels of p38 MAP kinase activity mediate distinct biological effects in primary human erythroid progenitors
    • Somervaille TC, Linch DC, Khwaja A. Different levels of p38 MAP kinase activity mediate distinct biological effects in primary human erythroid progenitors. Br J Haematol 2003; 120: 876-86.
    • (2003) Br J Haematol , vol.120 , pp. 876-886
    • Somervaille, T.C.1    Linch, D.C.2    Khwaja, A.3
  • 30
    • 3142517825 scopus 로고    scopus 로고
    • Functions of MAP kinases: Insights from gene-targeting studies
    • Kuida K, Boucher DM. Functions of MAP kinases: insights from gene-targeting studies. J Biochem 2004; 135: 653-6.
    • (2004) J Biochem , vol.135 , pp. 653-656
    • Kuida, K.1    Boucher, D.M.2
  • 31
    • 68149166871 scopus 로고    scopus 로고
    • Effects of p38 MAP kinase inhibitors on the differentiation and maturation of erythroid progenitors
    • Dalmas DA, Tierney LA, Zhang C, et al. Effects of p38 MAP kinase inhibitors on the differentiation and maturation of erythroid progenitors. Toxicol Pathol 2008; 36: 958-71.
    • (2008) Toxicol Pathol , vol.36 , pp. 958-971
    • Dalmas, D.A.1    Tierney, L.A.2    Zhang, C.3
  • 32
    • 0347719362 scopus 로고    scopus 로고
    • Differentiation stage-specific activation of p38 mitogen-activated protein kinase isoforms in primary human erythroid cells
    • Uddin S, Ah-Kang J, Ulaszek J, Mahmud D, Wickrema A. Differentiation stage-specific activation of p38 mitogen-activated protein kinase isoforms in primary human erythroid cells. Proc Natl Acad Sci USA 2004; 101: 147-52.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 147-152
    • Uddin, S.1    Ah-Kang, J.2    Ulaszek, J.3    Mahmud, D.4    Wickrema, A.5
  • 33
    • 0033569766 scopus 로고    scopus 로고
    • Activation of the p38 mitogen-activated protein kinase by type I interferons
    • Uddin S, Majchrzak B, Woodson J, et al. Activation of the p38 mitogen-activated protein kinase by type I interferons. J Biol Chem 1999; 274: 30127-31.
    • (1999) J Biol Chem , vol.274 , pp. 30127-30131
    • Uddin, S.1    Majchrzak, B.2    Woodson, J.3
  • 34
    • 25444513364 scopus 로고    scopus 로고
    • Role of the p38 mitogen- activated protein kinase pathway in cytokine-mediated hematopoietic suppression in myelodysplastic syndromes
    • Katsoulidis E, Li Y, Yoon P, et al. Role of the p38 mitogen- activated protein kinase pathway in cytokine-mediated hematopoietic suppression in myelodysplastic syndromes. Cancer Res 2005; 65: 9029-37.
    • (2005) Cancer Res , vol.65 , pp. 9029-9037
    • Katsoulidis, E.1    Li, Y.2    Yoon, P.3
  • 35
    • 0037097528 scopus 로고    scopus 로고
    • Cutting edge: Activation of the p38 mitogen-activated protein kinase signaling pathway mediates cytokine-induced hemopoietic suppression in aplastic anemia
    • Verma A, Deb DK, Sassano A, et al. Cutting edge: activation of the p38 mitogen-activated protein kinase signaling pathway mediates cytokine-induced hemopoietic suppression in aplastic anemia. J Immunol 2002; 168: 5984-8.
    • (2002) J Immunol , vol.168 , pp. 5984-5988
    • Verma, A.1    Deb, D.K.2    Sassano, A.3
  • 36
    • 0031013368 scopus 로고    scopus 로고
    • Hemopoietic growth factors with the exception of interleukin-4 activate the p38 mitogen- activated protein kinase pathway
    • Foltz I, Lee J, Young P, Schrader J. Hemopoietic growth factors with the exception of interleukin-4 activate the p38 mitogen- activated protein kinase pathway. J Biol Chem 1997; 272: 3296- 301.
    • (1997) J Biol Chem , vol.272 , pp. 3296-3301
    • Foltz, I.1    Lee, J.2    Young, P.3    Schrader, J.4
  • 37
    • 0033548164 scopus 로고    scopus 로고
    • Cooperation of p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways during granulocyte colony-stimulating factor-induced hemopoietic cell proliferation
    • Rausch O, Marshall CJ. Cooperation of p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways during granulocyte colony-stimulating factor-induced hemopoietic cell proliferation. J Biol Chem 1999; 274: 4096-105.
    • (1999) J Biol Chem , vol.274 , pp. 4096-4105
    • Rausch, O.1    Marshall, C.J.2
  • 39
    • 0033559703 scopus 로고    scopus 로고
    • Regulation of Rb and E2F by signal transduction cascades: Divergent effects of JNK1 and p38 kinases
    • Wang S, Nath N, Minden A, Chellappan S. Regulation of Rb and E2F by signal transduction cascades: divergent effects of JNK1 and p38 kinases. EMBO J 1999; 18: 1559-70.
    • (1999) EMBO J , vol.18 , pp. 1559-1570
    • Wang, S.1    Nath, N.2    Minden, A.3    Chellappan, S.4
  • 40
    • 0141841682 scopus 로고    scopus 로고
    • Apoptotic and mitogenic stimuli inactivate Rb by differential utilization of p38 and cyclin-dependent kinases
    • Nath N, Wang S, Betts V, Knudsen E, Chellappan S. Apoptotic and mitogenic stimuli inactivate Rb by differential utilization of p38 and cyclin-dependent kinases. Oncogene 2003; 22: 5986-94.
    • (2003) Oncogene , vol.22 , pp. 5986-5994
    • Nath, N.1    Wang, S.2    Betts, V.3    Knudsen, E.4    Chellappan, S.5
  • 41
    • 0037073753 scopus 로고    scopus 로고
    • Activation of the Rb/E2F1 pathway by the nonproliferative p38 MAPK during Fas (APO1/CD95)-mediated neuronal apoptosis
    • Hou ST, Xie X, Baggley A, Park DS, Chen G, Walker T. Activation of the Rb/E2F1 pathway by the nonproliferative p38 MAPK during Fas (APO1/CD95)-mediated neuronal apoptosis. J Biol Chem 2002; 277: 48764-70.
    • (2002) J Biol Chem , vol.277 , pp. 48764-48770
    • Hou, S.T.1    Xie, X.2    Baggley, A.3    Park, D.S.4    Chen, G.5    Walker, T.6
  • 42
    • 33644515316 scopus 로고    scopus 로고
    • Activation of p38 MAP kinase by DNA double-strand breaks in V(D)J recombination induces a G2/M cell cycle checkpoint
    • Pedraza-Alva G, Koulnis M, Charland C, et al. Activation of p38 MAP kinase by DNA double-strand breaks in V(D)J recombination induces a G2/M cell cycle checkpoint. EMBO J 2006; 25: 763-73.
    • (2006) EMBO J , vol.25 , pp. 763-773
    • Pedraza-Alva, G.1    Koulnis, M.2    Charland, C.3
  • 44
    • 43249106330 scopus 로고    scopus 로고
    • Phosphorylation by p38 MAPK as an alternative pathway for GSK3beta inactivation
    • Thornton TM, Pedraza-Alva G, Deng B, et al. Phosphorylation by p38 MAPK as an alternative pathway for GSK3beta inactivation. Science 2008; 320: 667-70.
    • (2008) Science , vol.320 , pp. 667-670
    • Thornton, T.M.1    Pedraza-Alva, G.2    Deng, B.3
  • 45
    • 11144268038 scopus 로고    scopus 로고
    • Constitutive activation of the MAPkinase p38 is critical for MMP-9 production and survival of B-CLL cells on bone marrow stromal cells
    • Ringshausen I, Dechow T, Schneller F, et al. Constitutive activation of the MAPkinase p38 is critical for MMP-9 production and survival of B-CLL cells on bone marrow stromal cells. Leukemia 2004; 18: 1964-70.
    • (2004) Leukemia , vol.18 , pp. 1964-1970
    • Ringshausen, I.1    Dechow, T.2    Schneller, F.3
  • 46
    • 0038471347 scopus 로고    scopus 로고
    • Involvement of multiple signaling pathways in follicular lymphoma transformation: P38-mitogen-activated protein kinase as a target for therapy
    • Elenitoba-Johnson K, Jenson S, Abbott R, et al. Involvement of multiple signaling pathways in follicular lymphoma transformation: p38-mitogen-activated protein kinase as a target for therapy. Proc Natl Acad Sci USA 2003; 100: 7259-64.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7259-7264
    • Elenitoba-Johnson, K.1    Jenson, S.2    Abbott, R.3
  • 47
    • 33845976332 scopus 로고    scopus 로고
    • BIRB 796 enhances cytotoxicity triggered by bortezomib, heat shock protein (Hsp) 90 inhibitor, and dexamethasone via inhibition of p38 mitogen- activated protein kinase/Hsp27 pathway in multiple myeloma cell lines and inhibits paracrine tumour growth
    • Yasui H, Hideshima T, Ikeda H, et al. BIRB 796 enhances cytotoxicity triggered by bortezomib, heat shock protein (Hsp) 90 inhibitor, and dexamethasone via inhibition of p38 mitogen- activated protein kinase/Hsp27 pathway in multiple myeloma cell lines and inhibits paracrine tumour growth. Br J Haematol 2007; 136: 414-23.
    • (2007) Br J Haematol , vol.136 , pp. 414-423
    • Yasui, H.1    Hideshima, T.2    Ikeda, H.3
  • 48
    • 0037657499 scopus 로고    scopus 로고
    • Regulation of hairy-cell survival through constitutive activation of mitogen-activated protein kinase pathways
    • Kamiguti A, Harris R, Slupsky J, Baker P, Cawley J, Zuzel M. Regulation of hairy-cell survival through constitutive activation of mitogen-activated protein kinase pathways. Oncogene 2003; 22: 2272-84.
    • (2003) Oncogene , vol.22 , pp. 2272-2284
    • Kamiguti, A.1    Harris, R.2    Slupsky, J.3    Baker, P.4    Cawley, J.5    Zuzel, M.6
  • 49
    • 17144384436 scopus 로고    scopus 로고
    • Defective p38 mitogen-activated protein kinase signaling impairs chemotaxic but not proliferative responses to stromal-derived factor-1alpha in acute lymphoblastic leukemia
    • Bendall LJ, Baraz R, Juarez J, Shen W, Bradstock KF. Defective p38 mitogen-activated protein kinase signaling impairs chemotaxic but not proliferative responses to stromal-derived factor-1alpha in acute lymphoblastic leukemia. Cancer Res 2005; 65: 3290-8.
    • (2005) Cancer Res , vol.65 , pp. 3290-3298
    • Bendall, L.J.1    Baraz, R.2    Juarez, J.3    Shen, W.4    Bradstock, K.F.5
  • 50
    • 0037728227 scopus 로고    scopus 로고
    • Constitutive activation of extracellular signal-regulated kinase and p38 mitogen-activated protein kinase in B-cell lymphoproliferative disorders
    • Ogasawara T, Yasuyama M, Kawauchi K. Constitutive activation of extracellular signal-regulated kinase and p38 mitogen-activated protein kinase in B-cell lymphoproliferative disorders. Int J Hematol 2003; 77: 364-70.
    • (2003) Int J Hematol , vol.77 , pp. 364-370
    • Ogasawara, T.1    Yasuyama, M.2    Kawauchi, K.3
  • 51
    • 64149111380 scopus 로고    scopus 로고
    • Colocalization of the VEGF-R2 and the common IL-3/GM-CSF receptor beta chain to lipid rafts leads to enhanced p38 activation
    • Saulle E, Riccioni R, Coppola S, et al. Colocalization of the VEGF-R2 and the common IL-3/GM-CSF receptor beta chain to lipid rafts leads to enhanced p38 activation. Br J Haematol 2009; 145: 399-411.
    • (2009) Br J Haematol , vol.145 , pp. 399-411
    • Saulle, E.1    Riccioni, R.2    Coppola, S.3
  • 52
    • 0037715079 scopus 로고    scopus 로고
    • Involvement of Akt kinase in the action of STI571 on chronic myelogenous leukemia cells
    • Kawauchi K, Ogasawara T, Yasuyama M, Ohkawa S. Involvement of Akt kinase in the action of STI571 on chronic myelogenous leukemia cells. Blood Cells Mol Dis 2003; 31: 11-7.
    • (2003) Blood Cells Mol Dis , vol.31 , pp. 11-17
    • Kawauchi, K.1    Ogasawara, T.2    Yasuyama, M.3    Ohkawa, S.4
  • 53
    • 20244370529 scopus 로고    scopus 로고
    • Modulation of the p38 MAPK (mitogen-activated protein kinase) pathway through Bcr/Abl: Implications in the cellular response to Ara-C
    • Sanchez-Arevalo Lobo VJ, Aceves Luquero CI, Alvarez-Vallina L, et al. Modulation of the p38 MAPK (mitogen-activated protein kinase) pathway through Bcr/Abl: implications in the cellular response to Ara-C. Biochem J 2005; 387: 231-8.
    • (2005) Biochem J , vol.387 , pp. 231-238
    • Sanchez-Arevalo lobo, V.J.1    Aceves Luquero, C.I.2    Alvarez-Vallina, L.3
  • 54
    • 0037063166 scopus 로고    scopus 로고
    • p38 MAPK- mediated activation of NF-kappaB by the RhoGEF domain of Bcr
    • Korus M, Mahon GM, Cheng L, Whitehead IP. p38 MAPK- mediated activation of NF-kappaB by the RhoGEF domain of Bcr. Oncogene 2002; 21: 4601-12.
    • (2002) Oncogene , vol.21 , pp. 4601-4612
    • Korus, M.1    Mahon, G.M.2    Cheng, L.3    Whitehead, I.P.4
  • 55
    • 2942558439 scopus 로고    scopus 로고
    • Role of the p38 mitogen- activated protein kinase pathway in the generation of the effects of imatinib mesylate (STI571) in BCR-ABL-expressing cells
    • Parmar S, Katsoulidis E, Verma A, et al. Role of the p38 mitogen- activated protein kinase pathway in the generation of the effects of imatinib mesylate (STI571) in BCR-ABL-expressing cells. J Biol Chem 2004; 279: 25345-52.
    • (2004) J Biol Chem , vol.279 , pp. 25345-25352
    • Parmar, S.1    Katsoulidis, E.2    Verma, A.3
  • 56
    • 33748923798 scopus 로고    scopus 로고
    • Opposing roles of mitogenic and stress signaling pathways in the induction of cancer dormancy
    • Ranganathan A, Adam A, Aguirre-Ghiso J. Opposing roles of mitogenic and stress signaling pathways in the induction of cancer dormancy. Cell Cycle 2006; 5: 1799-807.
    • (2006) Cell Cycle , vol.5 , pp. 1799-1807
    • Ranganathan, A.1    Adam, A.2    Aguirre-Ghiso, J.3
  • 57
    • 61449219879 scopus 로고    scopus 로고
    • The p38 pathway inhibitor SB202190 activates MEK/MAPK to stimulate the growth of leukemia cells
    • Hirosawa M, Nakahara M, Otosaka R, Imoto A, Okazaki T, Takahashi S. The p38 pathway inhibitor SB202190 activates MEK/MAPK to stimulate the growth of leukemia cells. Leuk Res 2009; 33: 693-9.
    • (2009) Leuk Res , vol.33 , pp. 693-699
    • Hirosawa, M.1    Nakahara, M.2    Otosaka, R.3    Imoto, A.4    Okazaki, T.5    Takahashi, S.6
  • 58
    • 0036167084 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase and p38 mitogen-activated protein kinase pathways cooperate in mediating cytokine-induced proliferation of a leukemic cell line
    • Srinivasa S, Doshi P. Extracellular signal-regulated kinase and p38 mitogen-activated protein kinase pathways cooperate in mediating cytokine-induced proliferation of a leukemic cell line. Leukemia 2002; 16: 244-53.
    • (2002) Leukemia , vol.16 , pp. 244-253
    • Srinivasa, S.1    Doshi, P.2
  • 59
    • 38949098302 scopus 로고    scopus 로고
    • JNK2 and p38 MAPK over-expressions do not represent key events in chronic myeloid leukemia transformation
    • Merkerova M, Bruchova H, Brdicka R. JNK2 and p38 MAPK over-expressions do not represent key events in chronic myeloid leukemia transformation. Neoplasma 2007; 54: 503-10.
    • (2007) Neoplasma , vol.54 , pp. 503-510
    • Merkerova, M.1    Bruchova, H.2    Brdicka, R.3
  • 60
    • 70349283058 scopus 로고    scopus 로고
    • Bendall LJ. p38MAPK inhibitors attenuate cytokine production by bone marrow stromal cells and reduce stroma-mediated proliferation of acute lymphoblastic leukemia cells
    • Gaundar SS, Bradstock KF, Bendall LJ. p38MAPK inhibitors attenuate cytokine production by bone marrow stromal cells and reduce stroma-mediated proliferation of acute lymphoblastic leukemia cells. Cell Cycle 2009; 8: 2975-83.
    • (2009) Cell Cycle , vol.8 , pp. 2975-2983
    • Gaundar, S.S.1    Bradstock, K.F.2
  • 61
    • 34347334539 scopus 로고    scopus 로고
    • Depsipeptide (FK228) preferentially induces apoptosis in BCR/ABL-expressing cell lines and cells from patients with chronic myelogenous leukemia in blast crisis
    • Okabe S, Tauchi T, Nakajima A, et al. Depsipeptide (FK228) preferentially induces apoptosis in BCR/ABL-expressing cell lines and cells from patients with chronic myelogenous leukemia in blast crisis. Stem Cells Dev 2007; 16: 503-14.
    • (2007) Stem Cells Dev , vol.16 , pp. 503-514
    • Okabe, S.1    Tauchi, T.2    Nakajima, A.3
  • 62
    • 24644467226 scopus 로고    scopus 로고
    • p38 MAP kinase plays a role in G2 checkpoint activation and inhibits apoptosis of human B cell lymphoma cells treated with etoposide
    • Kurosu T, Takahashi Y, Fukuda T, Koyama T, Miki T, Miura O. p38 MAP kinase plays a role in G2 checkpoint activation and inhibits apoptosis of human B cell lymphoma cells treated with etoposide. Apoptosis 2005; 10: 1111-20.
    • (2005) Apoptosis , vol.10 , pp. 1111-1120
    • Kurosu, T.1    Takahashi, Y.2    Fukuda, T.3    Koyama, T.4    Miki, T.5    Miura, O.6
  • 63
    • 22344458207 scopus 로고    scopus 로고
    • p38 Mitogen-activated protein kinase (MAPK) is a key mediator in glucocorticoid-induced apoptosis of lymphoid cells: Correlation between p38 MAPK activation and site-specific phosphorylation of the human glucocorticoid receptor at serine 211
    • Miller A, Webb M, Copik A, et al. p38 Mitogen-activated protein kinase (MAPK) is a key mediator in glucocorticoid-induced apoptosis of lymphoid cells: correlation between p38 MAPK activation and site-specific phosphorylation of the human glucocorticoid receptor at serine 211. Mol Endocrinol 2005; 19: 1569-83.
    • (2005) Mol Endocrinol , vol.19 , pp. 1569-1583
    • Miller, A.1    Webb, M.2    Copik, A.3
  • 64
    • 0035866406 scopus 로고    scopus 로고
    • Inhibition of extracellular signal-regulated kinase (ERK) mediates cell cycle phase independent apoptosis in vinblastine-treated ML-1 cells
    • Stadheim TA, Xiao H, Eastman A. Inhibition of extracellular signal-regulated kinase (ERK) mediates cell cycle phase independent apoptosis in vinblastine-treated ML-1 cells. Cancer Res 2001; 61: 1533-40.
    • (2001) Cancer Res , vol.61 , pp. 1533-1540
    • Stadheim, T.A.1    Xiao, H.2    Eastman, A.3
  • 65
    • 0037082469 scopus 로고    scopus 로고
    • The chimeric anti-CD20 antibody rituximab induces apoptosis in B-cell chronic lymphocytic leukemia cells through a p38 mitogen activated protein-kinase-dependent mechanism
    • Pedersen IM, Buhl AM, Klausen P, Geisler CH, Jurlander J. The chimeric anti-CD20 antibody rituximab induces apoptosis in B-cell chronic lymphocytic leukemia cells through a p38 mitogen activated protein-kinase-dependent mechanism. Blood 2002; 99: 1314-9.
    • (2002) Blood , vol.99 , pp. 1314-1319
    • Pedersen, I.M.1    Buhl, A.M.2    Klausen, P.3    Geisler, C.H.4    Jurlander, J.5
  • 66
    • 33746391136 scopus 로고    scopus 로고
    • p38-MAP kinase activation followed by BIM induction is essential for glucocorticoid-induced apoptosis in lymphoblastic leukemia cells
    • Lu J, Quearry B, Harada H. p38-MAP kinase activation followed by BIM induction is essential for glucocorticoid-induced apoptosis in lymphoblastic leukemia cells. FEBS Lett 2006; 580: 3539-44.
    • (2006) FEBS Lett , vol.580 , pp. 3539-3544
    • Lu, J.1    Quearry, B.2    Harada, H.3
  • 67
    • 34249899143 scopus 로고    scopus 로고
    • Balance of NF-kappaB and p38 MAPK is a determinant of radiosensitivity of the AML-2 and its doxorubicin-resistant cell lines
    • Choi CH, Xu H, Bark H, et al. Balance of NF-kappaB and p38 MAPK is a determinant of radiosensitivity of the AML-2 and its doxorubicin-resistant cell lines. Leuk Res 2007; 31: 1267-76.
    • (2007) Leuk Res , vol.31 , pp. 1267-1276
    • Choi, C.H.1    Xu, H.2    Bark, H.3
  • 68
    • 33746178172 scopus 로고    scopus 로고
    • Role of the p38 mitogen- activated protein kinase pathway in the generation of arsenic trioxide-dependent cellular responses
    • Giafis N, Katsoulidis E, Sassano A, et al. Role of the p38 mitogen- activated protein kinase pathway in the generation of arsenic trioxide-dependent cellular responses. Cancer Res 2006; 66: 6763- 71.
    • (2006) Cancer Res , vol.66 , pp. 6763-6771
    • Giafis, N.1    Katsoulidis, E.2    Sassano, A.3
  • 69
    • 48149085154 scopus 로고    scopus 로고
    • 2-Chloro-2'- deoxyadenosine-induced apoptosis in T leukemia cells is mediated via a caspase-3-dependent mitochondrial feedback amplification loop
    • Conrad DM, Robichaud MR, Mader JS, et al. 2-Chloro-2'- deoxyadenosine-induced apoptosis in T leukemia cells is mediated via a caspase-3-dependent mitochondrial feedback amplification loop. Int J Oncol 2008; 32: 1325-33.
    • (2008) Int J Oncol , vol.32 , pp. 1325-1333
    • Conrad, D.M.1    Robichaud, M.R.2    Mader, J.S.3
  • 70
    • 49749140733 scopus 로고    scopus 로고
    • Suppression of p38-stress kinase sensitizes quiescent leukemic cells to anti-mitotic drugs by inducing proliferative responses in them
    • Vaidya AA, Sharma MB, Kale VP. Suppression of p38-stress kinase sensitizes quiescent leukemic cells to anti-mitotic drugs by inducing proliferative responses in them. Cancer Biol Ther 2008; 7: 1232-40.
    • (2008) Cancer Biol Ther , vol.7 , pp. 1232-1240
    • Vaidya, A.A.1    Sharma, M.B.2    Kale, V.P.3
  • 71
    • 41549160315 scopus 로고    scopus 로고
    • Phosphatase-mediated crosstalk between MAPK signaling pathways in the regulation of cell survival
    • Junttila M, Li S, Westermarck J. Phosphatase-mediated crosstalk between MAPK signaling pathways in the regulation of cell survival. FASEB J 2008; 22: 954-65.
    • (2008) FASEB J , vol.22 , pp. 954-965
    • Junttila, M.1    Li, S.2    Westermarck, J.3
  • 72
    • 33747884339 scopus 로고    scopus 로고
    • DNA damage-induced cell death by apoptosis
    • Roos W, Kaina B. DNA damage-induced cell death by apoptosis. Trends Mol Med 2006; 12: 440-50.
    • (2006) Trends Mol Med , vol.12 , pp. 440-450
    • Roos, W.1    Kaina, B.2
  • 73
    • 0034944612 scopus 로고    scopus 로고
    • SB203580, a specific inhibitor of p38-MAPK pathway, is a new reversal agent of P-glycoprotein-mediated multidrug resistance
    • Barancik M, Bohacova V, Kvackajova J, Hudecova S, Krizanova O, Breier A. SB203580, a specific inhibitor of p38-MAPK pathway, is a new reversal agent of P-glycoprotein-mediated multidrug resistance. Eur J Pharm Sci 2001; 14: 29-36.
    • (2001) Eur J Pharm Sci , vol.14 , pp. 29-36
    • Barancik, M.1    Bohacova, V.2    Kvackajova, J.3    Hudecova, S.4    Krizanova, O.5    Breier, A.6
  • 74
    • 37249084060 scopus 로고    scopus 로고
    • P38 MAPK inhibition enhancing ATO-induced cytotoxicity against multiple myeloma cells
    • Wen J, Cheng HY, Feng Y, et al. P38 MAPK inhibition enhancing ATO-induced cytotoxicity against multiple myeloma cells. Br J Haematol 2008; 140: 169-80.
    • (2008) Br J Haematol , vol.140 , pp. 169-180
    • Wen, J.1    Cheng, H.Y.2    Feng, Y.3
  • 75
    • 9944242716 scopus 로고    scopus 로고
    • p38 MAPK inhibition enhances PS-341 (bortezomib)-induced cytotoxicity against multiple myeloma cells
    • Hideshima T, Podar K, Chauhan D, et al. p38 MAPK inhibition enhances PS-341 (bortezomib)-induced cytotoxicity against multiple myeloma cells. Oncogene 2004; 23: 8766-76.
    • (2004) Oncogene , vol.23 , pp. 8766-8776
    • Hideshima, T.1    Podar, K.2    Chauhan, D.3
  • 76
    • 73249129928 scopus 로고    scopus 로고
    • Enhanced antimyeloma cytotoxicity by the combination of arsenic trioxide and bortezomib is further potentiated by p38 MAPK inhibition
    • Wen J, Feng Y, Huang W, et al. Enhanced antimyeloma cytotoxicity by the combination of arsenic trioxide and bortezomib is further potentiated by p38 MAPK inhibition. Leuk Res 2010; 34: 85-92.
    • (2010) Leuk Res , vol.34 , pp. 85-92
    • Wen, J.1    Feng, Y.2    Huang, W.3
  • 77
    • 33845474265 scopus 로고    scopus 로고
    • Inhibition of overactivated p38 MAPK can restore hematopoiesis in myelodysplastic syndrome progenitors
    • Navas T, Mohindru M, Estes M, et al. Inhibition of overactivated p38 MAPK can restore hematopoiesis in myelodysplastic syndrome progenitors. Blood 2006; 108: 4170-7.
    • (2006) Blood , vol.108 , pp. 4170-4177
    • Navas, T.1    Mohindru, M.2    Estes, M.3
  • 78
    • 0031056783 scopus 로고    scopus 로고
    • Regulation of actin filament dynamics by p38 map kinase- mediated phosphorylation of heat shock protein 27
    • Guay J, Lambert H, Gingras-Breton G, Lavoie JN, Huot J, Landry J. Regulation of actin filament dynamics by p38 map kinase- mediated phosphorylation of heat shock protein 27. J Cell Sci 1997; 110: 357-68.
    • (1997) J Cell Sci , vol.110 , pp. 357-368
    • Guay, J.1    Lambert, H.2    Gingras-Breton, G.3    Lavoie, J.N.4    Huot, J.5    Landry, J.6
  • 79
    • 0028817419 scopus 로고
    • Constitutive expression of human hsp27, Drosophila hsp27, or human alpha B-crystallin confers resistance to TNF- and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts
    • Mehlen P, Preville X, Chareyron P, Briolay J, Klemenz R, Arrigo AP. Constitutive expression of human hsp27, Drosophila hsp27, or human alpha B-crystallin confers resistance to TNF- and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts. J Immunol 1995; 154: 363-74.
    • (1995) J Immunol , vol.154 , pp. 363-374
    • Mehlen, P.1    Preville, X.2    Chareyron, P.3    Briolay, J.4    Klemenz, R.5    Arrigo, A.P.6
  • 80
    • 0034282104 scopus 로고    scopus 로고
    • Hsp27 negatively regulates cell death by interacting with cytochrome c
    • Bruey JM, Ducasse C, Bonniaud P, et al. Hsp27 negatively regulates cell death by interacting with cytochrome c. Nat Cell Biol 2000; 2: 645-52.
    • (2000) Nat Cell Biol , vol.2 , pp. 645-652
    • Bruey, J.M.1    Ducasse, C.2    Bonniaud, P.3
  • 81
    • 63749131243 scopus 로고    scopus 로고
    • Kinases that control the cell cycle in response to DNA damage: Chk1, Chk2, and MK2
    • Reinhardt H, Yaffe M. Kinases that control the cell cycle in response to DNA damage: Chk1, Chk2, and MK2. Curr Opin Cell Biol 2009; 21: 245-55.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 245-255
    • Reinhardt, H.1    Yaffe, M.2
  • 82
    • 0032562716 scopus 로고    scopus 로고
    • Activation of the protein kinase p38 in the spindle assembly checkpoint and mitotic arrest
    • Takenaka K, Moriguchi T, Nishida E. Activation of the protein kinase p38 in the spindle assembly checkpoint and mitotic arrest. Science 1998; 280: 599-602.
    • (1998) Science , vol.280 , pp. 599-602
    • Takenaka, K.1    Moriguchi, T.2    Nishida, E.3
  • 83
    • 34247269029 scopus 로고    scopus 로고
    • TAO kinases mediate activation of p38 in response to DNA damage
    • Raman M, Earnest S, Zhang K, Zhao Y, Cobb M. TAO kinases mediate activation of p38 in response to DNA damage. EMBO J 2007; 26: 2005-14.
    • (2007) EMBO J , vol.26 , pp. 2005-2014
    • Raman, M.1    Earnest, S.2    Zhang, K.3    Zhao, Y.4    Cobb, M.5
  • 84
    • 33846821915 scopus 로고    scopus 로고
    • p53-deficient cells rely on ATM- and ATR-mediated checkpoint signaling through the p38MAPK/MK2 pathway for survival after DNA damage
    • Reinhardt HC, Aslanian AS, Lees JA, Yaffe MB. p53-deficient cells rely on ATM- and ATR-mediated checkpoint signaling through the p38MAPK/MK2 pathway for survival after DNA damage. Cancer Cell 2007; 11: 175-89.
    • (2007) Cancer Cell , vol.11 , pp. 175-189
    • Reinhardt, H.C.1    Aslanian, A.S.2    Lees, J.A.3    Yaffe, M.B.4
  • 85
    • 4143057046 scopus 로고    scopus 로고
    • Topoisomerase II and histone deacetylase inhibitors delay the G2/M transition by triggering the p38 MAPK checkpoint pathway
    • Mikhailov A, Shinohara M, Rieder C. Topoisomerase II and histone deacetylase inhibitors delay the G2/M transition by triggering the p38 MAPK checkpoint pathway. J Cell Biol 2004; 166: 517-26.
    • (2004) J Cell Biol , vol.166 , pp. 517-526
    • Mikhailov, A.1    Shinohara, M.2    Rieder, C.3
  • 86
    • 4143140977 scopus 로고    scopus 로고
    • Chfr acts with the p38 stress kinases to block entry to mitosis in mammalian cells
    • Matsusaka T, Pines J. Chfr acts with the p38 stress kinases to block entry to mitosis in mammalian cells. J Cell Biol 2004; 166: 507-16.
    • (2004) J Cell Biol , vol.166 , pp. 507-516
    • Matsusaka, T.1    Pines, J.2
  • 87
    • 0033485261 scopus 로고    scopus 로고
    • Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation
    • Bulavin D, Saito S, Hollander M, et al. Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation. EMBO J 1999; 18: 6845-54.
    • (1999) EMBO J , vol.18 , pp. 6845-6854
    • Bulavin, D.1    Saito, S.2    Hollander, M.3
  • 88
    • 33751299346 scopus 로고    scopus 로고
    • DNA damage checkpoints and cancer
    • Shimada M, Nakanishi M. DNA damage checkpoints and cancer. J Mol Histol 2006; 37: 253-60.
    • (2006) J Mol Histol , vol.37 , pp. 253-260
    • Shimada, M.1    Nakanishi, M.2
  • 89
    • 0033616501 scopus 로고    scopus 로고
    • GADD45 induction of a G2/M cell cycle checkpoint
    • Wang XW, Zhan Q, Coursen JD, et al. GADD45 induction of a G2/M cell cycle checkpoint. Proc Natl Acad Sci USA 1999; 96: 3706-11.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3706-3711
    • Wang, X.W.1    Zhan, Q.2    Coursen, J.D.3
  • 90
    • 0034711210 scopus 로고    scopus 로고
    • Identification of a functional domain in a GADD45-mediated G2/M checkpoint
    • Yang Q, Manicone A, Coursen JD, et al. Identification of a functional domain in a GADD45-mediated G2/M checkpoint. J Biol Chem 2000; 275: 36892-8.
    • (2000) J Biol Chem , vol.275 , pp. 36892-36898
    • Yang, Q.1    Manicone, A.2    Coursen, J.D.3
  • 91
    • 0035914446 scopus 로고    scopus 로고
    • Osmotic shock induces G1 arrest through p53 phosphorylation at Ser33 by activated p38MAPK without phosphorylation at Ser15 and Ser20
    • Kishi H, Nakagawa K, Matsumoto M, et al. Osmotic shock induces G1 arrest through p53 phosphorylation at Ser33 by activated p38MAPK without phosphorylation at Ser15 and Ser20. J Biol Chem 2001; 276: 39115-22.
    • (2001) J Biol Chem , vol.276 , pp. 39115-39122
    • Kishi, H.1    Nakagawa, K.2    Matsumoto, M.3
  • 92
    • 33747855844 scopus 로고    scopus 로고
    • CDC25B phosphorylation by p38 and MK-2
    • Lemaire M, Froment C, Boutros R, et al. CDC25B phosphorylation by p38 and MK-2. Cell Cycle 2006; 5: 1649-53.
    • (2006) Cell Cycle , vol.5 , pp. 1649-1653
    • Lemaire, M.1    Froment, C.2    Boutros, R.3
  • 93
    • 0142084976 scopus 로고    scopus 로고
    • Regulation of human Cdc25A stability by Serine 75 phosphorylation is not sufficient to activate a S phase checkpoint
    • Goloudina A, Yamaguchi H, Chervyakova D, Appella E, Fornace AJ, Bulavin D. Regulation of human Cdc25A stability by Serine 75 phosphorylation is not sufficient to activate a S phase checkpoint. Cell Cycle 2003; 2: 473-8.
    • (2003) Cell Cycle , vol.2 , pp. 473-478
    • Goloudina, A.1    Yamaguchi, H.2    Chervyakova, D.3    Appella, E.4    Fornace, A.J.5    Bulavin, D.6
  • 94
    • 22344438505 scopus 로고    scopus 로고
    • Cytokine-driven cell cycling is mediated through Cdc25A
    • Khaled A, Bulavin D, Kittipatarin C, et al. Cytokine-driven cell cycling is mediated through Cdc25A. J Cell Biol 2005; 169: 755- 63.
    • (2005) J Cell Biol , vol.169 , pp. 755-763
    • Khaled, A.1    Bulavin, D.2    Kittipatarin, C.3
  • 95
    • 0029786329 scopus 로고    scopus 로고
    • Cyclin D1 expression is regulated positively by the p42/p44MAPK and negatively by the p38/HOGMAPK pathway
    • Lavoie J, L'Allemain G, Brunet A, Müller R, Pouysségur J. Cyclin D1 expression is regulated positively by the p42/p44MAPK and negatively by the p38/HOGMAPK pathway. J Biol Chem 1996; 271: 20608-16.
    • (1996) J Biol Chem , vol.271 , pp. 20608-20616
    • Lavoie, J.1    L'Allemain, G.2    Brunet, A.3    Müller, R.4    Pouysségur, J.5
  • 96
    • 3242772188 scopus 로고    scopus 로고
    • The HBP1 transcriptional repressor and the p38 MAP kinase: Unlikely partners in G1 regulation and tumor suppression
    • Yee A, Paulson E, McDevitt M, et al. The HBP1 transcriptional repressor and the p38 MAP kinase: unlikely partners in G1 regulation and tumor suppression. Gene 2004; 336: 1-13.
    • (2004) Gene , vol.336 , pp. 1-13
    • Yee, A.1    Paulson, E.2    McDevitt, M.3
  • 97
    • 0034634574 scopus 로고    scopus 로고
    • Osmotic stress regulates the stability of cyclin D1 in a p38SAPK2- dependent manner
    • Casanovas O, Miro F, Estanyol J, Itarte E, Agell N, Bachs O. Osmotic stress regulates the stability of cyclin D1 in a p38SAPK2- dependent manner. J Biol Chem 2000; 275: 35091-7.
    • (2000) J Biol Chem , vol.275 , pp. 35091-35097
    • Casanovas, O.1    Miro, F.2    Estanyol, J.3    Itarte, E.4    Agell, N.5    Bachs, O.6
  • 98
    • 6344240450 scopus 로고    scopus 로고
    • P38SAPK2 phosphorylates cyclin D3 at Thr-283 and targets it for proteasomal degradation
    • Casanovas O, Jaumot M, Paules AB, Agell N, Bachs O. P38SAPK2 phosphorylates cyclin D3 at Thr-283 and targets it for proteasomal degradation. Oncogene 2004; 23: 7537-44.
    • (2004) Oncogene , vol.23 , pp. 7537-7544
    • Casanovas, O.1    Jaumot, M.2    Paules, A.B.3    Agell, N.4    Bachs, O.5
  • 99
    • 1842483852 scopus 로고    scopus 로고
    • Inactivation of the Wip1 phosphatase inhibits mammary tumorigenesis through p38 MAPK- mediated activation of the p16(Ink4a)-p19(Arf) pathway
    • Bulavin D, Phillips C, Nannenga B, et al. Inactivation of the Wip1 phosphatase inhibits mammary tumorigenesis through p38 MAPK- mediated activation of the p16(Ink4a)-p19(Arf) pathway. Nat Genet 2004; 36: 343-50.
    • (2004) Nat Genet , vol.36 , pp. 343-350
    • Bulavin, D.1    Phillips, C.2    Nannenga, B.3
  • 100
    • 33645730667 scopus 로고    scopus 로고
    • Reactive oxygen species act through p38 MAPK to limit the lifespan of hematopoietic stem cells
    • Ito K, Hirao A, Arai F, et al. Reactive oxygen species act through p38 MAPK to limit the lifespan of hematopoietic stem cells. Nat Med 2006; 12: 446-51.
    • (2006) Nat Med , vol.12 , pp. 446-451
    • Ito, K.1    Hirao, A.2    Arai, F.3
  • 101
    • 0037119470 scopus 로고    scopus 로고
    • The stress-activated protein kinases p38 alpha and JNK1 stabilize p21(Cip1) by phosphorylation
    • Kim GY, Mercer SE, Ewton DZ, Yan Z, Jin K, Friedman E. The stress-activated protein kinases p38 alpha and JNK1 stabilize p21(Cip1) by phosphorylation. J Biol Chem 2002; 277: 29792-802.
    • (2002) J Biol Chem , vol.277 , pp. 29792-29802
    • Kim, G.Y.1    Mercer, S.E.2    Ewton, D.Z.3    Yan, Z.4    Jin, K.5    Friedman, E.6
  • 102
    • 26444603774 scopus 로고    scopus 로고
    • Inhibition of the ATR/Chk1 pathway induces a p38-dependent S-phase delay in mouse embryonic stem cells
    • Jirmanova L, Bulavin DV, Fornace AJ Jr. Inhibition of the ATR/Chk1 pathway induces a p38-dependent S-phase delay in mouse embryonic stem cells. Cell Cycle 2005; 4: 1428-34.
    • (2005) Cell Cycle , vol.4 , pp. 1428-1434
    • Jirmanova, L.1    Bulavin, D.V.2    Fornace Jr., A.J.3
  • 103
    • 11344286593 scopus 로고    scopus 로고
    • MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates the G2/M transition and S phase progression in response to UV irradiation
    • Manke I, Nguyen A, Lim D, Stewart M, Elia A, Yaffe M. MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates the G2/M transition and S phase progression in response to UV irradiation. Mol Cell 2005; 17: 37-48.
    • (2005) Mol Cell , vol.17 , pp. 37-48
    • Manke, I.1    Nguyen, A.2    Lim, D.3    Stewart, M.4    Elia, A.5    Yaffe, M.6
  • 104
    • 41949135035 scopus 로고    scopus 로고
    • Role of p38 in regulation of hematopoiesis: Effect of p38 inhibition on cytokine production and transcription factor activity in human bone marrow stromal cells
    • Scicchitano M, McFarland D, Tierney L, et al. Role of p38 in regulation of hematopoiesis: effect of p38 inhibition on cytokine production and transcription factor activity in human bone marrow stromal cells. Blood Cells Mol Dis 2008; 40: 370-80.
    • (2008) Blood Cells Mol Dis , vol.40 , pp. 370-380
    • Scicchitano, M.1    McFarland, D.2    Tierney, L.3
  • 105
    • 0024336941 scopus 로고
    • Participation of the cytokines interleukin 6, tumor necrosis factor-alpha, and interleukin 1-beta secreted by acute myelogenous leukemia blasts in autocrine and paracrine leukemia growth control
    • Oster W, Cicco NA, Klein H, et al. Participation of the cytokines interleukin 6, tumor necrosis factor-alpha, and interleukin 1-beta secreted by acute myelogenous leukemia blasts in autocrine and paracrine leukemia growth control. J Clin Invest 1989; 84: 451-7.
    • (1989) J Clin Invest , vol.84 , pp. 451-457
    • Oster, W.1    Cicco, N.A.2    Klein, H.3
  • 106
    • 0027359386 scopus 로고
    • Constitutive expression of interleukin-8 and its receptor in human myeloid and lymphoid leukemia
    • Tobler A, Moser B, Dewald B, et al. Constitutive expression of interleukin-8 and its receptor in human myeloid and lymphoid leukemia. Blood 1993; 82: 2517-25.
    • (1993) Blood , vol.82 , pp. 2517-2525
    • Tobler, A.1    Moser, B.2    Dewald, B.3
  • 107
    • 0037097818 scopus 로고    scopus 로고
    • The role of cytokines in classical Hodgkin's lymphoma
    • Skinnider B, Mak T. The role of cytokines in classical Hodgkin's lymphoma. Blood 2002; 99: 4283-97.
    • (2002) Blood , vol.99 , pp. 4283-4297
    • Skinnider, B.1    Mak, T.2
  • 108
    • 33846238425 scopus 로고    scopus 로고
    • Hodgkin lymphoma cells express TACI and BCMA receptors and generate survival and proliferation signals in response to BAFF and APRIL
    • Chiu A, Xu W, He B, et al. Hodgkin lymphoma cells express TACI and BCMA receptors and generate survival and proliferation signals in response to BAFF and APRIL. Blood 2007; 109: 729-39.
    • (2007) Blood , vol.109 , pp. 729-739
    • Chiu, A.1    Xu, W.2    He, B.3
  • 109
    • 0028179142 scopus 로고
    • Interleukin-1 alpha as an autocrine growth factor for acute lymphoblastic leukaemia cells
    • Mori N, Shirakawa F, Murakami S, Oda S, Eto S. Interleukin-1 alpha as an autocrine growth factor for acute lymphoblastic leukaemia cells. Br J Haematol 1994; 86: 386-8.
    • (1994) Br J Haematol , vol.86 , pp. 386-388
    • Mori, N.1    Shirakawa, F.2    Murakami, S.3    Oda, S.4    Eto, S.5
  • 110
    • 0027216062 scopus 로고
    • Autocrine and paracrine growth control by granulocyte- monocyte colony-stimulating factor of acute lymphoblastic leukemia cells
    • Freedman MH, Grunberger T, Correa P, Axelrad AA, Dube ID, Cohen A. Autocrine and paracrine growth control by granulocyte- monocyte colony-stimulating factor of acute lymphoblastic leukemia cells. Blood 1993; 81: 3068-75.
    • (1993) Blood , vol.81 , pp. 3068-3075
    • Freedman, M.H.1    Grunberger, T.2    Correa, P.3    Axelrad, A.A.4    Dube, I.D.5    Cohen, A.6
  • 111
    • 0035819238 scopus 로고    scopus 로고
    • Characterization of cytokine, growth factor receptor, costimulatory and adhesion molecule expression patterns of bone marrow blasts in relapsed childhood B cell precursor all
    • Kebelmann-Betzing C, Korner G, Badiali L, et al. Characterization of cytokine, growth factor receptor, costimulatory and adhesion molecule expression patterns of bone marrow blasts in relapsed childhood B cell precursor all. Cytokine 2001; 13: 39-50.
    • (2001) Cytokine , vol.13 , pp. 39-50
    • Kebelmann-Betzing, C.1    Korner, G.2    Badiali, L.3
  • 112
    • 0035863942 scopus 로고    scopus 로고
    • Autocrine interleukin-6 production and highly malignant multiple myeloma: Relation with resistance to drug-induced apoptosis
    • Frassanito MA, Cusmai A, Iodice G, Dammacco F. Autocrine interleukin-6 production and highly malignant multiple myeloma: relation with resistance to drug-induced apoptosis. Blood 2001; 97: 483-9.
    • (2001) Blood , vol.97 , pp. 483-489
    • Frassanito, M.A.1    Cusmai, A.2    Iodice, G.3    Dammacco, F.4
  • 113
    • 0028605318 scopus 로고
    • A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
    • Lee JC, Laydon JT, McDonnell PC, et al. A protein kinase involved in the regulation of inflammatory cytokine biosynthesis. Nature 1994; 372: 739-46.
    • (1994) Nature , vol.372 , pp. 739-746
    • Lee, J.C.1    Laydon, J.T.2    McDonnell, P.C.3
  • 114
    • 0029983730 scopus 로고    scopus 로고
    • The p38/RK mitogen-activated protein kinase pathway regulates interleukin-6 synthesis response to tumor necrosis factor
    • Beyaert R, Cuenda A, Vanden Berghe W, et al. The p38/RK mitogen-activated protein kinase pathway regulates interleukin-6 synthesis response to tumor necrosis factor. EMBO J 1996; 15: 1914-23.
    • (1996) EMBO J , vol.15 , pp. 1914-1923
    • Beyaert, R.1    Cuenda, A.2    Vanden Berghe, W.3
  • 115
    • 0033953399 scopus 로고    scopus 로고
    • p38 MAP kinase regulates TNF alpha-, IL-1 alpha- and PAF-induced RANTES and GM-CSF production by human bronchial epithelial cells
    • Hashimoto S, Matsumoto K, Gon Y, et al. p38 MAP kinase regulates TNF alpha-, IL-1 alpha- and PAF-induced RANTES and GM-CSF production by human bronchial epithelial cells. Clin Exp Allergy 2000; 30: 48-55.
    • (2000) Clin Exp Allergy , vol.30 , pp. 48-55
    • Hashimoto, S.1    Matsumoto, K.2    Gon, Y.3
  • 116
    • 0034327287 scopus 로고    scopus 로고
    • Role of p38 mitogen-activated protein kinase in rhinovirus-induced cytokine production by bronchial epithelial cells
    • Griego SD, Weston CB, Adams JL, Tal-Singer R, Dillon SB. Role of p38 mitogen-activated protein kinase in rhinovirus-induced cytokine production by bronchial epithelial cells. J Immunol 2000; 165: 5211-20.
    • (2000) J Immunol , vol.165 , pp. 5211-5220
    • Griego, S.D.1    Weston, C.B.2    Adams, J.L.3    Tal-Singer, R.4    Dillon, S.B.5
  • 117
    • 33744494283 scopus 로고    scopus 로고
    • Inhibition of p38alpha MAPK enhances proteasome inhibitor-induced apoptosis of myeloma cells by modulating Hsp27, Bcl-X(L), Mcl-1 and p53 levels in vitro and inhibits tumor growth in vivo
    • Navas TA, Nguyen AN, Hideshima T, et al. Inhibition of p38alpha MAPK enhances proteasome inhibitor-induced apoptosis of myeloma cells by modulating Hsp27, Bcl-X(L), Mcl-1 and p53 levels in vitro and inhibits tumor growth in vivo. Leukemia 2006; 20: 1017-27.
    • (2006) Leukemia , vol.20 , pp. 1017-1027
    • Navas, T.A.1    Nguyen, A.N.2    Hideshima, T.3
  • 118
    • 0037438374 scopus 로고    scopus 로고
    • Targeting p38 MAPK inhibits multiple myeloma cell growth in the bone marrow milieu
    • Hideshima T, Akiyama M, Hayashi T, et al. Targeting p38 MAPK inhibits multiple myeloma cell growth in the bone marrow milieu. Blood 2003; 101: 703-5.
    • (2003) Blood , vol.101 , pp. 703-705
    • Hideshima, T.1    Akiyama, M.2    Hayashi, T.3
  • 119
    • 33646853556 scopus 로고    scopus 로고
    • Normalizing the bone marrow microenvironment with p38 inhibitor reduces multiple myeloma cell proliferation and adhesion and suppresses osteoclast formation
    • Nguyen A, Stebbins E, Henson M, et al. Normalizing the bone marrow microenvironment with p38 inhibitor reduces multiple myeloma cell proliferation and adhesion and suppresses osteoclast formation. Exp Cell Res 2006; 312: 1909-23.
    • (2006) Exp Cell Res , vol.312 , pp. 1909-1923
    • Nguyen, A.1    Stebbins, E.2    Henson, M.3
  • 120
    • 0038103869 scopus 로고    scopus 로고
    • Effects of inhibitors of the chemokine receptor CXCR4 on acute lymphoblastic leukemia cells in vitro
    • Juarez J, Bradstock K, Gottlieb D, Bendall L. Effects of inhibitors of the chemokine receptor CXCR4 on acute lymphoblastic leukemia cells in vitro. Leukemia 2003; 17: 1294-300.
    • (2003) Leukemia , vol.17 , pp. 1294-1300
    • Juarez, J.1    Bradstock, K.2    Gottlieb, D.3    Bendall, L.4
  • 121
    • 0026630954 scopus 로고
    • Bone marrow-derived stromal cells prevent apoptotic cell death in B-lineage acute lymphoblastic leukemia
    • Manabe A, Coustan-Smith E, Behm F, Raimondi S, Campana D. Bone marrow-derived stromal cells prevent apoptotic cell death in B-lineage acute lymphoblastic leukemia. Blood 1992; 79: 2370-7.
    • (1992) Blood , vol.79 , pp. 2370-2377
    • Manabe, A.1    Coustan-Smith, E.2    Behm, F.3    Raimondi, S.4    Campana, D.5
  • 122
    • 0022344945 scopus 로고
    • Stimulation of proliferation and differentiation of acute myeloid leukemia cells on a bone marrow stroma in culture
    • Scholzel C, Lowenberg B. Stimulation of proliferation and differentiation of acute myeloid leukemia cells on a bone marrow stroma in culture. Exp Hematol 1985; 13: 664-9.
    • (1985) Exp Hematol , vol.13 , pp. 664-669
    • Scholzel, C.1    Lowenberg, B.2
  • 123
    • 0030048565 scopus 로고    scopus 로고
    • Human bone marrow stromal cells prevent apoptosis and support the survival of chronic lymphocytic leukaemia cells in vitro
    • Panayiotidis P, Jones D, Ganeshaguru K, Foroni L, Hoffbrand AV. Human bone marrow stromal cells prevent apoptosis and support the survival of chronic lymphocytic leukaemia cells in vitro. Br J Haematol 1996; 92: 97-103.
    • (1996) Br J Haematol , vol.92 , pp. 97-103
    • Panayiotidis, P.1    Jones, D.2    Ganeshaguru, K.3    Foroni, L.4    Hoffbrand, A.V.5
  • 124
    • 0028007178 scopus 로고
    • Bone marrow adherent layers inhibit apoptosis of acute myeloid leukemia cells
    • Bendall LJ, Daniel A, Kortlepel K, Gottlieb DJ. Bone marrow adherent layers inhibit apoptosis of acute myeloid leukemia cells. Exp Hematol 1994; 22: 1252-60.
    • (1994) Exp Hematol , vol.22 , pp. 1252-1260
    • Bendall, L.J.1    Daniel, A.2    Kortlepel, K.3    Gottlieb, D.J.4
  • 125
    • 0027954624 scopus 로고
    • Adhesion-dependent survival of normal and leukemic human B lymphoblasts on bone marrow stromal cells
    • Manabe A, Murti KG, Coustan-Smith E, et al. Adhesion-dependent survival of normal and leukemic human B lymphoblasts on bone marrow stromal cells. Blood 1994; 83: 758-66.
    • (1994) Blood , vol.83 , pp. 758-766
    • Manabe, A.1    Murti, K.G.2    Coustan-Smith, E.3
  • 126
    • 0029665151 scopus 로고    scopus 로고
    • Activation- dependent alpha5beta1 integrin-mediated adhesion to fibronectin decreases proliferation of chronic myelogenous leukemia progenitors and K562 cells
    • Lundell BI, McCarthy JB, Kovach NL, Verfaillie CM. Activation- dependent alpha5beta1 integrin-mediated adhesion to fibronectin decreases proliferation of chronic myelogenous leukemia progenitors and K562 cells. Blood 1996; 87: 2450-8.
    • (1996) Blood , vol.87 , pp. 2450-2458
    • Lundell, B.I.1    McCarthy, J.B.2    Kovach, N.L.3    Verfaillie, C.M.4
  • 127
    • 0031990830 scopus 로고    scopus 로고
    • Rescue from apoptosis in early (CD34-selected) versus late (non-CD34-selected) human hematopoietic cells by very late antigen 4- and vascular cell adhesion molecule (VCAM) 1-dependent adhesion to bone marrow stromal cells
    • Wang M, Consoli U, Lane C, et al. Rescue from apoptosis in early (CD34-selected) versus late (non-CD34-selected) human hematopoietic cells by very late antigen 4- and vascular cell adhesion molecule (VCAM) 1-dependent adhesion to bone marrow stromal cells. Cell Growth Differ 1998; 9: 105-12.
    • (1998) Cell Growth Differ , vol.9 , pp. 105-112
    • Wang, M.1    Consoli, U.2    Lane, C.3
  • 128
    • 7844220599 scopus 로고    scopus 로고
    • Effect of the interaction between fibronectin and VLA-4 on the proliferation of human B cells, especially a novel human B-cell line, OPM-3
    • Yoshida H, Nishiura T, Karasuno T, et al. Effect of the interaction between fibronectin and VLA-4 on the proliferation of human B cells, especially a novel human B-cell line, OPM-3. Br J Haematol 1998; 103: 804-12.
    • (1998) Br J Haematol , vol.103 , pp. 804-812
    • Yoshida, H.1    Nishiura, T.2    Karasuno, T.3
  • 129
    • 0033580928 scopus 로고    scopus 로고
    • C-reactive protein inhibits chemotactic peptide-induced p38 mitogen-activated protein kinase activity and human neutrophil movement
    • Heuertz RM, Tricomi SM, Ezekiel UR, Webster RO. C-reactive protein inhibits chemotactic peptide-induced p38 mitogen-activated protein kinase activity and human neutrophil movement. J Biol Chem 1999; 274: 17968-74.
    • (1999) J Biol Chem , vol.274 , pp. 17968-17974
    • Heuertz, R.M.1    Tricomi, S.M.2    Ezekiel, U.R.3    Webster, R.O.4
  • 130
    • 0037078334 scopus 로고    scopus 로고
    • An intracellular signaling hierarchy determines direction of migration in opposing chemotactic gradients
    • Heit B, Tavener S, Raharjo E, Kubes P. An intracellular signaling hierarchy determines direction of migration in opposing chemotactic gradients. J Cell Biol 2002; 159: 91-102.
    • (2002) J Cell Biol , vol.159 , pp. 91-102
    • Heit, B.1    Tavener, S.2    Raharjo, E.3    Kubes, P.4
  • 131
    • 44649094127 scopus 로고    scopus 로고
    • Migration across the sinusoidal endothelium regulates neutrophil mobilization in response to ELR + CXC chemokines
    • Burdon PC, Martin C, Rankin SM. Migration across the sinusoidal endothelium regulates neutrophil mobilization in response to ELR + CXC chemokines. Br J Haematol 2008; 142: 100-8.
    • (2008) Br J Haematol , vol.142 , pp. 100-108
    • Burdon, P.C.1    Martin, C.2    Rankin, S.M.3
  • 132
    • 0035881679 scopus 로고    scopus 로고
    • Sensitized mast cells migrate toward the antigen: A response regulated by p38 mitogen- activated protein kinase and Rho-associated coiled-coil-forming protein kinase
    • Ishizuka T, Okajima F, Ishiwara M, et al. Sensitized mast cells migrate toward the antigen: a response regulated by p38 mitogen- activated protein kinase and Rho-associated coiled-coil-forming protein kinase. J Immunol 2001; 167: 2298-304.
    • (2001) J Immunol , vol.167 , pp. 2298-2304
    • Ishizuka, T.1    Okajima, F.2    Ishiwara, M.3
  • 133
    • 33749257848 scopus 로고    scopus 로고
    • CXCL12 and C5a trigger cell migration via a PAK1/2-p38alpha MAPK-MAPKAP- K2-HSP27 pathway
    • Rousseau S, Dolado I, Beardmore V, et al. CXCL12 and C5a trigger cell migration via a PAK1/2-p38alpha MAPK-MAPKAP- K2-HSP27 pathway. Cell Signal 2006; 18: 1897-905.
    • (2006) Cell Signal , vol.18 , pp. 1897-1905
    • Rousseau, S.1    Dolado, I.2    Beardmore, V.3
  • 134
    • 41949133387 scopus 로고    scopus 로고
    • BAFF enhances chemotaxis of primary human B cells: A particular synergy between BAFF and CXCL13 on memory B cells
    • Badr G, Borhis G, Lefevre EA, et al. BAFF enhances chemotaxis of primary human B cells: a particular synergy between BAFF and CXCL13 on memory B cells. Blood 2008; 111: 2744-54.
    • (2008) Blood , vol.111 , pp. 2744-2754
    • Badr, G.1    Borhis, G.2    Lefevre, E.A.3
  • 135
    • 65349111856 scopus 로고    scopus 로고
    • CXCR4 mediates the homing of B cell progenitor acute lymphoblastic leukaemia cells to the bone marrow via activation of p38MAPK
    • Juarez JG, Thien M, Dela Pena A, Baraz R, Bradstock KF, Bendall LJ. CXCR4 mediates the homing of B cell progenitor acute lymphoblastic leukaemia cells to the bone marrow via activation of p38MAPK. Br J Haematol 2009; 145: 491-9.
    • (2009) Br J Haematol , vol.145 , pp. 491-499
    • Juarez, J.G.1    Thien, M.2    Dela Pena, A.3    Baraz, R.4    Bradstock, K.F.5    Bendall, L.J.6
  • 136
    • 0025813543 scopus 로고
    • A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein
    • Miron T, Vancompernolle K, Vandekerckhove J, Wilchek M, Geiger B. A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein. J Cell Biol 1991; 114: 255-61.
    • (1991) J Cell Biol , vol.114 , pp. 255-261
    • Miron, T.1    Vancompernolle, K.2    Vandekerckhove, J.3    Wilchek, M.4    Geiger, B.5
  • 137
    • 22144462425 scopus 로고    scopus 로고
    • The phosphorylation of CapZ-interacting protein (CapZIP) by stress-activated protein kinases triggers its dissociation from CapZ
    • Eyers CE, McNeill H, Knebel A, et al. The phosphorylation of CapZ-interacting protein (CapZIP) by stress-activated protein kinases triggers its dissociation from CapZ. Biochem J 2005; 389: 127-35.
    • (2005) Biochem J , vol.389 , pp. 127-135
    • Eyers, C.E.1    McNeill, H.2    Knebel, A.3
  • 138
    • 33644508365 scopus 로고    scopus 로고
    • MAPKAPK-2-mediated LIM-kinase activation is critical for VEGF-induced actin remodeling and cell migration
    • Kobayashi M, Nishita M, Mishima T, Ohashi K, Mizuno K. MAPKAPK-2-mediated LIM-kinase activation is critical for VEGF-induced actin remodeling and cell migration. EMBO J 2006; 25: 713-26.
    • (2006) EMBO J , vol.25 , pp. 713-726
    • Kobayashi, M.1    Nishita, M.2    Mishima, T.3    Ohashi, K.4    Mizuno, K.5
  • 139
    • 1242307450 scopus 로고    scopus 로고
    • Phosphorylation of paxillin by p38MAPK is involved in the neurite extension of PC-12 cells
    • Huang C, Borchers CH, Schaller MD, Jacobson K. Phosphorylation of paxillin by p38MAPK is involved in the neurite extension of PC-12 cells. J Cell Biol 2004; 164: 593-602.
    • (2004) J Cell Biol , vol.164 , pp. 593-602
    • Huang, C.1    Borchers, C.H.2    Schaller, M.D.3    Jacobson, K.4
  • 140
    • 34247570008 scopus 로고    scopus 로고
    • p38 MAPK and ERK activation by 9-cis-retinoic acid induces chemokine receptors CCR1 and CCR2 expression in human monocytic THP-1 cells
    • Ko J, Yun CY, Lee JS, Kim JH, Kim IS. p38 MAPK and ERK activation by 9-cis-retinoic acid induces chemokine receptors CCR1 and CCR2 expression in human monocytic THP-1 cells. Exp Mol Med 2007; 39: 129-38.
    • (2007) Exp Mol Med , vol.39 , pp. 129-138
    • Ko, J.1    Yun, C.Y.2    Lee, J.S.3    Kim, J.H.4    Kim, I.S.5
  • 141
    • 9144234780 scopus 로고    scopus 로고
    • Lipopolysaccharide induces matrix metalloproteinase-9 expression via a mitochondrial reactive oxygen species-p38 kinase-activator protein-1 pathway in Raw 264.7 cells
    • Woo CH, Lim JH, Kim JH. Lipopolysaccharide induces matrix metalloproteinase-9 expression via a mitochondrial reactive oxygen species-p38 kinase-activator protein-1 pathway in Raw 264.7 cells. J Immunol 2004; 173: 6973-80.
    • (2004) J Immunol , vol.173 , pp. 6973-6980
    • Woo, C.H.1    Lim, J.H.2    Kim, J.H.3
  • 142
    • 33746225582 scopus 로고    scopus 로고
    • Protein tyrosine kinase and p38 MAP kinase pathways are involved in stimulation of matrix metalloproteinase-9 by TNF-alpha in human monocytes
    • Nguyen J, Gogusev J, Knapnougel P, Bauvois B. Protein tyrosine kinase and p38 MAP kinase pathways are involved in stimulation of matrix metalloproteinase-9 by TNF-alpha in human monocytes. Immunol Lett 2006; 106: 34-41.
    • (2006) Immunol Lett , vol.106 , pp. 34-41
    • Nguyen, J.1    Gogusev, J.2    Knapnougel, P.3    Bauvois, B.4
  • 143
    • 34447335316 scopus 로고    scopus 로고
    • Osteoblasts promote migration and invasion of myeloma cells through upregulation of matrix metalloproteinases, urokinase plasminogen activator, hepatocyte growth factor and activation of p38 MAPK
    • Hecht M, Heider U, Kaiser M, von Metzler I, Sterz J, Sezer O. Osteoblasts promote migration and invasion of myeloma cells through upregulation of matrix metalloproteinases, urokinase plasminogen activator, hepatocyte growth factor and activation of p38 MAPK. Br J Haematol 2007; 138: 446-58.
    • (2007) Br J Haematol , vol.138 , pp. 446-458
    • Hecht, M.1    Heider, U.2    Kaiser, M.3    von Metzler, I.4    Sterz, J.5    Sezer, O.6
  • 144
    • 60549114409 scopus 로고    scopus 로고
    • The role of MAPK in governing lymphocyte adhesion to and migration across the microvasculature in inflammatory bowel disease
    • Scaldaferri F, Sans M, Vetrano S, et al. The role of MAPK in governing lymphocyte adhesion to and migration across the microvasculature in inflammatory bowel disease. Eur J Immunol 2009; 39: 290-300.
    • (2009) Eur J Immunol , vol.39 , pp. 290-300
    • Scaldaferri, F.1    Sans, M.2    Vetrano, S.3
  • 145
    • 67650410440 scopus 로고    scopus 로고
    • Chemosensitization of acute myeloid leukemia (AML) following mobilization by the CXCR4 antagonist AMD3100
    • Nervi B, Ramirez P, Rettig MP, et al. Chemosensitization of acute myeloid leukemia (AML) following mobilization by the CXCR4 antagonist AMD3100. Blood 2009; 113: 6206-14.
    • (2009) Blood , vol.113 , pp. 6206-6214
    • Nervi, B.1    Ramirez, P.2    Rettig, M.P.3
  • 146
    • 58149154965 scopus 로고    scopus 로고
    • p38alpha-selective MAP kinase inhibitor reduces tumor growth in mouse xenograft models of multiple myeloma
    • Medicherla S, Reddy M, Ying J, et al. p38alpha-selective MAP kinase inhibitor reduces tumor growth in mouse xenograft models of multiple myeloma. Anticancer Res 2008; 28: 3827-33.
    • (2008) Anticancer Res , vol.28 , pp. 3827-3833
    • Medicherla, S.1    Reddy, M.2    Ying, J.3
  • 147
    • 34250328203 scopus 로고    scopus 로고
    • Inhibition of p38alpha mitogen-activated protein kinase prevents the development of osteolytic bone disease, reduces tumor burden, and increases survival in murine models of multiple myeloma
    • Vanderkerken K, Medicherla S, Coulton L, et al. Inhibition of p38alpha mitogen-activated protein kinase prevents the development of osteolytic bone disease, reduces tumor burden, and increases survival in murine models of multiple myeloma. Cancer Res 2007; 67: 4572-7.
    • (2007) Cancer Res , vol.67 , pp. 4572-4577
    • Vanderkerken, K.1    Medicherla, S.2    Coulton, L.3
  • 148
    • 43449140012 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase inhibitor LY2228820 enhances bortezomib-induced cytotoxicity and inhibits osteoclastogenesis in multiple myeloma; therapeutic implications
    • Ishitsuka K, Hideshima T, Neri P, et al. p38 mitogen-activated protein kinase inhibitor LY2228820 enhances bortezomib-induced cytotoxicity and inhibits osteoclastogenesis in multiple myeloma; therapeutic implications. Br J Haematol 2008; 141: 598-606.
    • (2008) Br J Haematol , vol.141 , pp. 598-606
    • Ishitsuka, K.1    Hideshima, T.2    Neri, P.3
  • 149
    • 27944503331 scopus 로고    scopus 로고
    • MAP kinase p38 inhibitors: Clinical results and an intimate look at their interactions with p38alpha protein
    • Lee MR, Dominguez C. MAP kinase p38 inhibitors: clinical results and an intimate look at their interactions with p38alpha protein. Curr Med Chem 2005; 12: 2979-94.
    • (2005) Curr Med Chem , vol.12 , pp. 2979-2994
    • Lee, M.R.1    Dominguez, C.2
  • 151
    • 72749121087 scopus 로고    scopus 로고
    • A randomized, placebo-controlled study of the effects of the p38 MAPK inhibitor SB-681323 on blood biomarkers of inflammation in COPD patients
    • Singh D, Smyth L, Borrill Z, Sweeney L, Tal-Singer R. A randomized, placebo-controlled study of the effects of the p38 MAPK inhibitor SB-681323 on blood biomarkers of inflammation in COPD patients. J Clin Pharmacol 2010; 50: 94-100.
    • (2010) J Clin Pharmacol , vol.50 , pp. 94-100
    • Singh, D.1    Smyth, L.2    Borrill, Z.3    Sweeney, L.4    Tal-Singer, R.5
  • 153
    • 59649114148 scopus 로고    scopus 로고
    • Evaluation of the efficacy and safety of pamapimod, a p38 MAP kinase inhibitor, in a double-blind, methotrexate-controlled study of patients with active rheumatoid arthritis
    • Cohen SB, Cheng TT, Chindalore V, et al. Evaluation of the efficacy and safety of pamapimod, a p38 MAP kinase inhibitor, in a double-blind, methotrexate-controlled study of patients with active rheumatoid arthritis. Arthritis Rheum 2009; 60: 335-44.
    • (2009) Arthritis Rheum , vol.60 , pp. 335-344
    • Cohen, S.B.1    Cheng, T.T.2    Chindalore, V.3
  • 154
    • 75749115980 scopus 로고    scopus 로고
    • Efficacy and safety of pamapimod in patients with active rheumatoid arthritis receiving stable methotrexate therapy
    • Alten RE, Zerbini C, Jeka S, et al. Efficacy and safety of pamapimod in patients with active rheumatoid arthritis receiving stable methotrexate therapy. Ann Rheum Dis 2010; 69: 364-7.
    • (2010) Ann Rheum Dis , vol.69 , pp. 364-367
    • Alten, R.E.1    Zerbini, C.2    Jeka, S.3
  • 155
    • 66049086274 scopus 로고    scopus 로고
    • Efficacy, pharmacodynamics, and safety of VX-702, a novel p38 MAPK inhibitor, in rheumatoid arthritis: Results of two randomized, double-blind, placebo-controlled clinical studies
    • Damjanov N, Kauffman RS, Spencer-Green GT. Efficacy, pharmacodynamics, and safety of VX-702, a novel p38 MAPK inhibitor, in rheumatoid arthritis: results of two randomized, double-blind, placebo-controlled clinical studies. Arthritis Rheum 2009; 60: 1232-41.
    • (2009) Arthritis Rheum , vol.60 , pp. 1232-1241
    • Damjanov, N.1    Kauffman, R.S.2    Spencer-Green, G.T.3
  • 156
    • 33644756429 scopus 로고    scopus 로고
    • Oral p38 mitogen- activated protein kinase inhibition with BIRB 796 for active Crohn's disease: A randomized, double-blind, placebo-controlled trial
    • Schreiber S, Feagan B, D'Haens G, et al. Oral p38 mitogen- activated protein kinase inhibition with BIRB 796 for active Crohn's disease: a randomized, double-blind, placebo-controlled trial. Clin Gastroenterol Hepatol 2006; 4: 325-34.
    • (2006) Clin Gastroenterol Hepatol , vol.4 , pp. 325-334
    • Schreiber, S.1    Feagan, B.2    D'Haens, G.3
  • 157
    • 0036142395 scopus 로고    scopus 로고
    • Inhibition of stress- activated MAP kinases induces clinical improvement in moderate to severe Crohn's disease
    • Hommes D, van den Blink B, Plasse T, et al. Inhibition of stress- activated MAP kinases induces clinical improvement in moderate to severe Crohn's disease. Gastroenterol 2002; 122: 7-14.
    • (2002) Gastroenterol , vol.122 , pp. 7-14
    • Hommes, D.1    van Den Blink, B.2    Plasse, T.3
  • 158
    • 34447131774 scopus 로고    scopus 로고
    • Interaction of interleukin-7 and interleukin-3 with the CXCL12-induced proliferation of B-cell progenitor acute lymphoblastic leukemia
    • Juarez J, Baraz R, Gaundar S, Bradstock K, Bendall L. Interaction of interleukin-7 and interleukin-3 with the CXCL12-induced proliferation of B-cell progenitor acute lymphoblastic leukemia. Haematologica 2007; 92: 450-9.
    • (2007) Haematologica , vol.92 , pp. 450-459
    • Juarez, J.1    Baraz, R.2    Gaundar, S.3    Bradstock, K.4    Bendall, L.5
  • 159
    • 0242663968 scopus 로고    scopus 로고
    • The p38 mitogen-activated protein kinase pathway links the DNA mismatch repair system to the G2 checkpoint and to resistance to chemotherapeutic DNA-methylating agents
    • Hirose Y, Katayama M, Stokoe D, Haas-Kogan DA, Berger MS, Pieper RO. The p38 mitogen-activated protein kinase pathway links the DNA mismatch repair system to the G2 checkpoint and to resistance to chemotherapeutic DNA-methylating agents. Mol Cell Biol 2003; 23: 8306-15.
    • (2003) Mol Cell Biol , vol.23 , pp. 8306-8315
    • Hirose, Y.1    Katayama, M.2    Stokoe, D.3    Haas-Kogan, D.A.4    Berger, M.S.5    Pieper, R.O.6
  • 160
    • 47249154397 scopus 로고    scopus 로고
    • Genistein selectively potentiates arsenic trioxide-induced apoptosis in human leukemia cells via reactive oxygen species generation and activation of reactive oxygen species-inducible protein kinases (p38-MAPK, AMPK)
    • Sanchez Y, Amran D, Fernandez C, de Blas E, Aller P. Genistein selectively potentiates arsenic trioxide-induced apoptosis in human leukemia cells via reactive oxygen species generation and activation of reactive oxygen species-inducible protein kinases (p38-MAPK, AMPK). Int J Cancer 2008; 123: 1205-14.
    • (2008) Int J Cancer , vol.123 , pp. 1205-1214
    • Sanchez, Y.1    Amran, D.2    Fernandez, C.3    de Blas, E.4    Aller, P.5
  • 161
    • 23744501131 scopus 로고    scopus 로고
    • The novel triterpenoid CDDO-Me suppresses MAPK pathways and promotes p38 activation in acute myeloid leukemia cells
    • Konopleva M, Contractor R, Kurinna SM, Chen W, Andreeff M, Ruvolo PP. The novel triterpenoid CDDO-Me suppresses MAPK pathways and promotes p38 activation in acute myeloid leukemia cells. Leukemia 2005; 19: 1350-4.
    • (2005) Leukemia , vol.19 , pp. 1350-1354
    • Konopleva, M.1    Contractor, R.2    Kurinna, S.M.3    Chen, W.4    Andreeff, M.5    Ruvolo, P.P.6
  • 162
    • 56149102360 scopus 로고    scopus 로고
    • Realgar- induced differentiation is associated with MAPK pathways in HL- 60 cells
    • Wang N, Wang LW, Gou BD, Zhang TL, Wang K. Realgar- induced differentiation is associated with MAPK pathways in HL- 60 cells. Cell Biol Int 2008; 32: 1497-505.
    • (2008) Cell Biol Int , vol.32 , pp. 1497-1505
    • Wang, N.1    Wang, L.W.2    Gou, B.D.3    Zhang, T.L.4    Wang, K.5
  • 163
    • 33845760859 scopus 로고    scopus 로고
    • Sulindac-derived reactive oxygen species induce apoptosis of human multiple myeloma cells via p38 mitogen activated protein kinase-induced mitochondrial dysfunc- tion
    • Seo SK, Lee HC, Woo SH, et al. Sulindac-derived reactive oxygen species induce apoptosis of human multiple myeloma cells via p38 mitogen activated protein kinase-induced mitochondrial dysfunc- tion. Apoptosis 2007; 12: 195-209.
    • (2007) Apoptosis , vol.12 , pp. 195-209
    • Seo, S.K.1    Lee, H.C.2    Woo, S.H.3
  • 164
    • 32144436448 scopus 로고    scopus 로고
    • Resveratrol induces apoptosis of human malignant B cells by activation of caspase-3 and p38 MAP kinase pathways
    • Shimizu T, Nakazato T, Xian MJ, Sagawa M, Ikeda Y, Kizaki M. Resveratrol induces apoptosis of human malignant B cells by activation of caspase-3 and p38 MAP kinase pathways. Biochem Pharmacol 2006; 71: 742-50.
    • (2006) Biochem Pharmacol , vol.71 , pp. 742-750
    • Shimizu, T.1    Nakazato, T.2    Xian, M.J.3    Sagawa, M.4    Ikeda, Y.5    Kizaki, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.