메뉴 건너뛰기




Volumn 77, Issue , 2012, Pages 406-422

Proteins implicated in the increase of adhesivity induced by suberoylanilide hydroxamic acid in leukemic cells

Author keywords

Adhesion; Cofilin; HDAC inhibitor; PAK; SAHA; Vimentin

Indexed keywords

BUTYRIC ACID; COFILIN; HISTONE DEACETYLASE INHIBITOR; PAXILLIN; PROTEIN 14 3 3; PROTEIN 14 3 3 EPSILON; SERINE; STATHMIN; UNCLASSIFIED DRUG; VIMENTIN; VORINOSTAT;

EID: 84870391600     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.09.014     Document Type: Article
Times cited : (7)

References (62)
  • 1
    • 4143128717 scopus 로고    scopus 로고
    • Acetylation of proteins as novel target for antitumor therapy: review article
    • Di Gennaro E., Bruzzese F., Caraglia M., Abruzzese A., Budillon A. Acetylation of proteins as novel target for antitumor therapy: review article. Amino Acids 2004, 26:435-441.
    • (2004) Amino Acids , vol.26 , pp. 435-441
    • Di Gennaro, E.1    Bruzzese, F.2    Caraglia, M.3    Abruzzese, A.4    Budillon, A.5
  • 2
    • 33144478290 scopus 로고    scopus 로고
    • Histone-deacetylases inhibitors: from TSA to SAHA
    • Peixoto P., Lansiaux A. Histone-deacetylases inhibitors: from TSA to SAHA. Bull Cancer 2006, 93:27-36.
    • (2006) Bull Cancer , vol.93 , pp. 27-36
    • Peixoto, P.1    Lansiaux, A.2
  • 3
    • 67650090545 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: potential in cancer therapy
    • Marks P.A., Xu W.S. Histone deacetylase inhibitors: potential in cancer therapy. J Cell Biochem 2009, 107:600-608.
    • (2009) J Cell Biochem , vol.107 , pp. 600-608
    • Marks, P.A.1    Xu, W.S.2
  • 4
    • 33751035378 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors as novel anti-inflammatory agents
    • Adcock I.M. Histone deacetylase inhibitors as novel anti-inflammatory agents. Curr Opin Investig Drugs 2006, 7:966-973.
    • (2006) Curr Opin Investig Drugs , vol.7 , pp. 966-973
    • Adcock, I.M.1
  • 5
    • 34547864236 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: molecular mechanisms of action
    • Xu W.S., Parmigiani R.B., Marks P.A. Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene 2007, 26:5541-5552.
    • (2007) Oncogene , vol.26 , pp. 5541-5552
    • Xu, W.S.1    Parmigiani, R.B.2    Marks, P.A.3
  • 6
    • 20444479514 scopus 로고    scopus 로고
    • Drug insight: histone deacetylase inhibitors-development of the new targeted anticancer agent suberoylanilide hydroxamic acid
    • Kelly W.K., Marks P.A. Drug insight: histone deacetylase inhibitors-development of the new targeted anticancer agent suberoylanilide hydroxamic acid. Nat Clin Pract Oncol 2005, 2:150-157.
    • (2005) Nat Clin Pract Oncol , vol.2 , pp. 150-157
    • Kelly, W.K.1    Marks, P.A.2
  • 7
    • 33748427812 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors (HDI) cause DNA damage in leukemia cells: a mechanism for leukemia-specific HDI-dependent apoptosis?
    • Gaymes T.J., Padua R.A., Pla M., Orr S., Omidvar N., Chomienne C., et al. Histone deacetylase inhibitors (HDI) cause DNA damage in leukemia cells: a mechanism for leukemia-specific HDI-dependent apoptosis?. Mol Cancer Res 2006, 4:563-573.
    • (2006) Mol Cancer Res , vol.4 , pp. 563-573
    • Gaymes, T.J.1    Padua, R.A.2    Pla, M.3    Orr, S.4    Omidvar, N.5    Chomienne, C.6
  • 8
    • 80053968084 scopus 로고    scopus 로고
    • SAHA Capture Compound-a novel tool for the profiling of histone deacetylases and the identification of additional vorinostat binders
    • Fischer J.J., Michaelis S., Schrey A.K., Diehl A., Graebner O.Y., Ungewiss J., et al. SAHA Capture Compound-a novel tool for the profiling of histone deacetylases and the identification of additional vorinostat binders. Proteomics 2011, 11:4096-4104.
    • (2011) Proteomics , vol.11 , pp. 4096-4104
    • Fischer, J.J.1    Michaelis, S.2    Schrey, A.K.3    Diehl, A.4    Graebner, O.Y.5    Ungewiss, J.6
  • 9
    • 39749116808 scopus 로고    scopus 로고
    • Proteomic analysis of liver cancer cells treated with suberonylanilide hydroxamic acid
    • Tong A., Zhang H., Li Z., Gou L., Wang Z., Wei H., et al. Proteomic analysis of liver cancer cells treated with suberonylanilide hydroxamic acid. Cancer Chemother Pharmacol 2008, 61:791-802.
    • (2008) Cancer Chemother Pharmacol , vol.61 , pp. 791-802
    • Tong, A.1    Zhang, H.2    Li, Z.3    Gou, L.4    Wang, Z.5    Wei, H.6
  • 10
    • 59449094854 scopus 로고    scopus 로고
    • Proteomic analysis of cervical cancer cells treated with suberonylanilide hydroxamic acid
    • He J., Huang C., Tong A., Chen B., Zeng Z., Zhang P., et al. Proteomic analysis of cervical cancer cells treated with suberonylanilide hydroxamic acid. J Biosci 2008, 33:715-721.
    • (2008) J Biosci , vol.33 , pp. 715-721
    • He, J.1    Huang, C.2    Tong, A.3    Chen, B.4    Zeng, Z.5    Zhang, P.6
  • 11
    • 77951727320 scopus 로고    scopus 로고
    • Proteomic profile of differentially expressed plasma proteins from dystrophic mice and following suberoylanilide hydroxamic acid treatment
    • Colussi C., Banfi C., Brioschi M., Tremoli E., Straino S., Spallotta F., et al. Proteomic profile of differentially expressed plasma proteins from dystrophic mice and following suberoylanilide hydroxamic acid treatment. Proteomics Clin Appl 2010, 4:71-83.
    • (2010) Proteomics Clin Appl , vol.4 , pp. 71-83
    • Colussi, C.1    Banfi, C.2    Brioschi, M.3    Tremoli, E.4    Straino, S.5    Spallotta, F.6
  • 12
    • 77955884095 scopus 로고    scopus 로고
    • Proteomic analysis revealed association of aberrant ROS signaling with suberoylanilide hydroxamic acid-induced autophagy in Jurkat T-leukemia cells
    • Li J., Liu R., Lei Y., Wang K., Lau Q.C., Xie N., et al. Proteomic analysis revealed association of aberrant ROS signaling with suberoylanilide hydroxamic acid-induced autophagy in Jurkat T-leukemia cells. Autophagy 2010, 6:711-724.
    • (2010) Autophagy , vol.6 , pp. 711-724
    • Li, J.1    Liu, R.2    Lei, Y.3    Wang, K.4    Lau, Q.C.5    Xie, N.6
  • 13
    • 73849101542 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid (SAHA) at subtoxic concentrations increases the adhesivity of human leukemic cells to fibronectin
    • Kuzelova K., Pluskalova M., Brodska B., Otevrelova P., Elknerova K., Grebenova D., et al. Suberoylanilide hydroxamic acid (SAHA) at subtoxic concentrations increases the adhesivity of human leukemic cells to fibronectin. J Cell Biochem 2010, 109:184-195.
    • (2010) J Cell Biochem , vol.109 , pp. 184-195
    • Kuzelova, K.1    Pluskalova, M.2    Brodska, B.3    Otevrelova, P.4    Elknerova, K.5    Grebenova, D.6
  • 14
    • 0043016178 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor LAQ824 both lowers expression and promotes proteasomal degradation of Bcr-Abl and induces apoptosis of imatinib mesylate-sensitive or -refractory chronic myelogenous leukemia-blast crisis cells
    • Nimmanapalli R., Fuino L., Bali P., Gasparetto M., Glozak M., Tao J., et al. Histone deacetylase inhibitor LAQ824 both lowers expression and promotes proteasomal degradation of Bcr-Abl and induces apoptosis of imatinib mesylate-sensitive or -refractory chronic myelogenous leukemia-blast crisis cells. Cancer Res 2003, 63:5126-5135.
    • (2003) Cancer Res , vol.63 , pp. 5126-5135
    • Nimmanapalli, R.1    Fuino, L.2    Bali, P.3    Gasparetto, M.4    Glozak, M.5    Tao, J.6
  • 15
    • 33750303818 scopus 로고    scopus 로고
    • Cotreatment with vorinostat (suberoylanilide hydroxamic acid) enhances activity of dasatinib (BMS-354825) against imatinib mesylate-sensitive or imatinib mesylate-resistant chronic myelogenous leukemia cells
    • Fiskus W., Pranpat M., Balasis M., Bali P., Estrella V., Kumaraswamy S., et al. Cotreatment with vorinostat (suberoylanilide hydroxamic acid) enhances activity of dasatinib (BMS-354825) against imatinib mesylate-sensitive or imatinib mesylate-resistant chronic myelogenous leukemia cells. Clin Cancer Res 2006, 12:5869-5878.
    • (2006) Clin Cancer Res , vol.12 , pp. 5869-5878
    • Fiskus, W.1    Pranpat, M.2    Balasis, M.3    Bali, P.4    Estrella, V.5    Kumaraswamy, S.6
  • 16
    • 84863011183 scopus 로고    scopus 로고
    • Activation of p53 by SIRT1 inhibition enhances elimination of CML leukemia stem cells in combination with imatinib
    • Li L., Wang L., Li L., Wang Z., Ho Y., McDonald T., et al. Activation of p53 by SIRT1 inhibition enhances elimination of CML leukemia stem cells in combination with imatinib. Cancer Cell 2012, 21:266-281.
    • (2012) Cancer Cell , vol.21 , pp. 266-281
    • Li, L.1    Wang, L.2    Li, L.3    Wang, Z.4    Ho, Y.5    McDonald, T.6
  • 17
    • 42349116071 scopus 로고    scopus 로고
    • Enhanced BCR-ABL kinase inhibition does not result in increased inhibition of downstream signaling pathways or increased growth suppression in CML progenitors
    • Konig H., Holtz M., Modi H., Manley P., Holyoake T.L., Forman S.J., et al. Enhanced BCR-ABL kinase inhibition does not result in increased inhibition of downstream signaling pathways or increased growth suppression in CML progenitors. Leukemia 2008, 22:748-755.
    • (2008) Leukemia , vol.22 , pp. 748-755
    • Konig, H.1    Holtz, M.2    Modi, H.3    Manley, P.4    Holyoake, T.L.5    Forman, S.J.6
  • 18
    • 49849092970 scopus 로고    scopus 로고
    • Stromal-mediated protection of tyrosine kinase inhibitor-treated BCR-ABL-expressing leukemia cells
    • Weisberg E., Wright R.D., McMillin D.W., Mitsiades C., Ray A., Barrett R., et al. Stromal-mediated protection of tyrosine kinase inhibitor-treated BCR-ABL-expressing leukemia cells. Mol Cancer Ther 2008, 7:1121-1129.
    • (2008) Mol Cancer Ther , vol.7 , pp. 1121-1129
    • Weisberg, E.1    Wright, R.D.2    McMillin, D.W.3    Mitsiades, C.4    Ray, A.5    Barrett, R.6
  • 19
    • 33750937577 scopus 로고    scopus 로고
    • Targeting multiple kinase pathways in leukemic progenitors and stem cells is essential for improved treatment of Ph+ leukemia in mice
    • Hu Y., Swerdlow S., Duffy T.M., Weinmann R., Lee F.Y., Li S. Targeting multiple kinase pathways in leukemic progenitors and stem cells is essential for improved treatment of Ph+ leukemia in mice. Proc Natl Acad Sci U S A 2006, 103:16870-16875.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 16870-16875
    • Hu, Y.1    Swerdlow, S.2    Duffy, T.M.3    Weinmann, R.4    Lee, F.Y.5    Li, S.6
  • 20
    • 16844380143 scopus 로고    scopus 로고
    • P210BCR-ABL inhibits SDF-1 chemotactic response via alteration of CXCR4 signaling and down-regulation of CXCR4 expression
    • Geay J.F., Buet D., Zhang Y., Foudi A., Jarrier P., Berthebaud M., et al. p210BCR-ABL inhibits SDF-1 chemotactic response via alteration of CXCR4 signaling and down-regulation of CXCR4 expression. Cancer Res 2005, 65:2676-2683.
    • (2005) Cancer Res , vol.65 , pp. 2676-2683
    • Geay, J.F.1    Buet, D.2    Zhang, Y.3    Foudi, A.4    Jarrier, P.5    Berthebaud, M.6
  • 21
    • 13044279495 scopus 로고    scopus 로고
    • The BCR/ABL oncogene alters the chemotactic response to stromal-derived factor-1alpha
    • Salgia R., Quackenbush E., Lin J., Souchkova N., Sattler M., Ewaniuk D.S., et al. The BCR/ABL oncogene alters the chemotactic response to stromal-derived factor-1alpha. Blood 1999, 94:4233-4246.
    • (1999) Blood , vol.94 , pp. 4233-4246
    • Salgia, R.1    Quackenbush, E.2    Lin, J.3    Souchkova, N.4    Sattler, M.5    Ewaniuk, D.S.6
  • 23
    • 66749172227 scopus 로고    scopus 로고
    • Bidirectional control of the inner dynamics of focal adhesions promotes cell migration
    • Goetz J.G. Bidirectional control of the inner dynamics of focal adhesions promotes cell migration. Cell Adh Migr 2009, 3:185-190.
    • (2009) Cell Adh Migr , vol.3 , pp. 185-190
    • Goetz, J.G.1
  • 24
    • 79955856806 scopus 로고    scopus 로고
    • Signaling networks regulating leukocyte podosome dynamics and function
    • Dovas A., Cox D. Signaling networks regulating leukocyte podosome dynamics and function. Cell Signal 2011, 23:1225-1234.
    • (2011) Cell Signal , vol.23 , pp. 1225-1234
    • Dovas, A.1    Cox, D.2
  • 25
    • 0346244001 scopus 로고    scopus 로고
    • Intracellular phospho-protein staining techniques for flow cytometry: monitoring single cell signaling events
    • Krutzik P.O., Nolan G.P. Intracellular phospho-protein staining techniques for flow cytometry: monitoring single cell signaling events. Cytometry A 2003, 55:61-70.
    • (2003) Cytometry A , vol.55 , pp. 61-70
    • Krutzik, P.O.1    Nolan, G.P.2
  • 26
    • 80054999734 scopus 로고    scopus 로고
    • Dose-dependent effects of the caspase inhibitor Q-VD-OPh on different apoptosis-related processes
    • Kuzelova K., Grebenova D., Brodska B. Dose-dependent effects of the caspase inhibitor Q-VD-OPh on different apoptosis-related processes. J Cell Biochem 2011, 112:3334-3342.
    • (2011) J Cell Biochem , vol.112 , pp. 3334-3342
    • Kuzelova, K.1    Grebenova, D.2    Brodska, B.3
  • 27
    • 78649779774 scopus 로고    scopus 로고
    • Changes in cell adhesivity and cytoskeleton-related proteins during imatinib-induced apoptosis of leukemic JURL-MK1 cells
    • Kuzelova K., Pluskalova M., Grebenova D., Pavlaskova K., Halada P., Hrkal Z. Changes in cell adhesivity and cytoskeleton-related proteins during imatinib-induced apoptosis of leukemic JURL-MK1 cells. J Cell Biochem 2010, 111:1413-1425.
    • (2010) J Cell Biochem , vol.111 , pp. 1413-1425
    • Kuzelova, K.1    Pluskalova, M.2    Grebenova, D.3    Pavlaskova, K.4    Halada, P.5    Hrkal, Z.6
  • 28
    • 0037270323 scopus 로고    scopus 로고
    • Identification of cofilin and LIM-domain-containing protein kinase 1 as novel interaction partners of 14-3-3 zeta
    • Birkenfeld J., Betz H., Roth D. Identification of cofilin and LIM-domain-containing protein kinase 1 as novel interaction partners of 14-3-3 zeta. Biochem J 2003, 369:45-54.
    • (2003) Biochem J , vol.369 , pp. 45-54
    • Birkenfeld, J.1    Betz, H.2    Roth, D.3
  • 29
    • 0036794093 scopus 로고    scopus 로고
    • 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin
    • Gohla A., Bokoch G.M. 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin. Curr Biol 2002, 12:1704-1710.
    • (2002) Curr Biol , vol.12 , pp. 1704-1710
    • Gohla, A.1    Bokoch, G.M.2
  • 30
    • 60449087924 scopus 로고    scopus 로고
    • Analysis of the protein complex associated with 14-3-3 epsilon by a deuterated-leucine labeling quantitative proteomics strategy
    • Liang S., Yu Y., Yang P., Gu S., Xue Y., Chen X. Analysis of the protein complex associated with 14-3-3 epsilon by a deuterated-leucine labeling quantitative proteomics strategy. J Chromatogr B Analyt Technol Biomed Life Sci 2009, 877:627-634.
    • (2009) J Chromatogr B Analyt Technol Biomed Life Sci , vol.877 , pp. 627-634
    • Liang, S.1    Yu, Y.2    Yang, P.3    Gu, S.4    Xue, Y.5    Chen, X.6
  • 31
    • 26444439216 scopus 로고    scopus 로고
    • Prospects: histone deacetylase inhibitors
    • Dokmanovic M., Marks P.A. Prospects: histone deacetylase inhibitors. J Cell Biochem 2005, 96:293-304.
    • (2005) J Cell Biochem , vol.96 , pp. 293-304
    • Dokmanovic, M.1    Marks, P.A.2
  • 32
    • 79961234301 scopus 로고    scopus 로고
    • Siva1 suppresses epithelial-mesenchymal transition and metastasis of tumor cells by inhibiting stathmin and stabilizing microtubules
    • Li N., Jiang P., Du W., Wu Z., Li C., Qiao M., et al. Siva1 suppresses epithelial-mesenchymal transition and metastasis of tumor cells by inhibiting stathmin and stabilizing microtubules. Proc Natl Acad Sci U S A 2011, 108:12851-12856.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 12851-12856
    • Li, N.1    Jiang, P.2    Du, W.3    Wu, Z.4    Li, C.5    Qiao, M.6
  • 33
    • 33644836549 scopus 로고    scopus 로고
    • Clinical experience with intravenous and oral formulations of the novel histone deacetylase inhibitor suberoylanilide hydroxamic acid in patients with advanced hematologic malignancies
    • O'Connor O.A., Heaney M.L., Schwartz L., Richardson S., Willim R., MacGregor-Cortelli B., et al. Clinical experience with intravenous and oral formulations of the novel histone deacetylase inhibitor suberoylanilide hydroxamic acid in patients with advanced hematologic malignancies. J Clin Oncol 2006, 24:166-173.
    • (2006) J Clin Oncol , vol.24 , pp. 166-173
    • O'Connor, O.A.1    Heaney, M.L.2    Schwartz, L.3    Richardson, S.4    Willim, R.5    MacGregor-Cortelli, B.6
  • 34
    • 29144529317 scopus 로고    scopus 로고
    • Binding of barrier to autointegration factor (BAF) to histone H3 and selected linker histones including H1.1
    • Montes de Oca R., Lee K.K., Wilson K.L. Binding of barrier to autointegration factor (BAF) to histone H3 and selected linker histones including H1.1. J Biol Chem 2005, 280:42252-42262.
    • (2005) J Biol Chem , vol.280 , pp. 42252-42262
    • Montes de Oca, R.1    Lee, K.K.2    Wilson, K.L.3
  • 35
    • 73149088831 scopus 로고    scopus 로고
    • Histone post-translational modifications by HPLC-ESI-MS after HT29 cell treatment with histone deacetylase inhibitors
    • Naldi M., Calonghi N., Masotti L., Parolin C., Valente S., Mai A., et al. Histone post-translational modifications by HPLC-ESI-MS after HT29 cell treatment with histone deacetylase inhibitors. Proteomics 2009, 9:5437-5445.
    • (2009) Proteomics , vol.9 , pp. 5437-5445
    • Naldi, M.1    Calonghi, N.2    Masotti, L.3    Parolin, C.4    Valente, S.5    Mai, A.6
  • 36
    • 0344668558 scopus 로고    scopus 로고
    • Mitochondrial translocation of cofilin is an early step in apoptosis induction
    • Chua B.T., Volbracht C., Tan K.O., Li R., Yu V.C., Li P. Mitochondrial translocation of cofilin is an early step in apoptosis induction. Nat Cell Biol 2003, 5:1083-1089.
    • (2003) Nat Cell Biol , vol.5 , pp. 1083-1089
    • Chua, B.T.1    Volbracht, C.2    Tan, K.O.3    Li, R.4    Yu, V.C.5    Li, P.6
  • 37
    • 16244370745 scopus 로고    scopus 로고
    • Activated cofilin colocalises with Arp2/3 complex in apoptotic blebs during programmed cell death
    • Mannherz H.G., Gonsior S.M., Gremm D., Wu X., Pope B.J., Weeds A.G. Activated cofilin colocalises with Arp2/3 complex in apoptotic blebs during programmed cell death. Eur J Cell Biol 2005, 84:503-515.
    • (2005) Eur J Cell Biol , vol.84 , pp. 503-515
    • Mannherz, H.G.1    Gonsior, S.M.2    Gremm, D.3    Wu, X.4    Pope, B.J.5    Weeds, A.G.6
  • 38
    • 53349090281 scopus 로고    scopus 로고
    • Mitochondrial shuttling of CAP1 promotes actin- and cofilin-dependent apoptosis
    • Wang C., Zhou G.L., Vedantam S., Li P., Field J. Mitochondrial shuttling of CAP1 promotes actin- and cofilin-dependent apoptosis. J Cell Sci 2008, 121:2913-2920.
    • (2008) J Cell Sci , vol.121 , pp. 2913-2920
    • Wang, C.1    Zhou, G.L.2    Vedantam, S.3    Li, P.4    Field, J.5
  • 39
    • 34249682108 scopus 로고    scopus 로고
    • Novel functions of vimentin in cell adhesion, migration, and signaling
    • Ivaska J., Pallari H.M., Nevo J., Eriksson J.E. Novel functions of vimentin in cell adhesion, migration, and signaling. Exp Cell Res 2007, 313:2050-2062.
    • (2007) Exp Cell Res , vol.313 , pp. 2050-2062
    • Ivaska, J.1    Pallari, H.M.2    Nevo, J.3    Eriksson, J.E.4
  • 40
    • 77958038961 scopus 로고    scopus 로고
    • Keeping the vimentin network under control: cell-matrix adhesion-associated plectin 1f affects cell shape and polarity of fibroblasts
    • Burgstaller G., Gregor M., Winter L., Wiche G. Keeping the vimentin network under control: cell-matrix adhesion-associated plectin 1f affects cell shape and polarity of fibroblasts. Mol Biol Cell 2010, 21:3362-3375.
    • (2010) Mol Biol Cell , vol.21 , pp. 3362-3375
    • Burgstaller, G.1    Gregor, M.2    Winter, L.3    Wiche, G.4
  • 41
    • 77953230270 scopus 로고    scopus 로고
    • Regulation of cell adhesion to collagen via beta1 integrins is dependent on interactions of filamin A with vimentin and protein kinase C epsilon
    • Kim H., Nakamura F., Lee W., Hong C., Perez-Sala D., McCulloch C.A. Regulation of cell adhesion to collagen via beta1 integrins is dependent on interactions of filamin A with vimentin and protein kinase C epsilon. Exp Cell Res 2010, 316:1829-1844.
    • (2010) Exp Cell Res , vol.316 , pp. 1829-1844
    • Kim, H.1    Nakamura, F.2    Lee, W.3    Hong, C.4    Perez-Sala, D.5    McCulloch, C.A.6
  • 43
    • 80053944532 scopus 로고    scopus 로고
    • FAK is required for the assembly of podosome rosettes
    • Pan Y.R., Chen C.L., Chen H.C. FAK is required for the assembly of podosome rosettes. J Cell Biol 2011, 195:113-129.
    • (2011) J Cell Biol , vol.195 , pp. 113-129
    • Pan, Y.R.1    Chen, C.L.2    Chen, H.C.3
  • 44
    • 77953484480 scopus 로고    scopus 로고
    • Vimentin induces changes in cell shape, motility, and adhesion during the epithelial to mesenchymal transition
    • Mendez M.G., Kojima S., Goldman R.D. Vimentin induces changes in cell shape, motility, and adhesion during the epithelial to mesenchymal transition. FASEB J 2010, 24:1838-1851.
    • (2010) FASEB J , vol.24 , pp. 1838-1851
    • Mendez, M.G.1    Kojima, S.2    Goldman, R.D.3
  • 46
    • 0035020420 scopus 로고    scopus 로고
    • Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis
    • Byun Y., Chen F., Chang R., Trivedi M., Green K.J., Cryns V.L. Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis. Cell Death Differ 2001, 8:443-450.
    • (2001) Cell Death Differ , vol.8 , pp. 443-450
    • Byun, Y.1    Chen, F.2    Chang, R.3    Trivedi, M.4    Green, K.J.5    Cryns, V.L.6
  • 47
    • 0342936426 scopus 로고    scopus 로고
    • Changes in vimentin in human macrophages during apoptosis induced by oxidised low density lipoprotein
    • Muller K., Dulku S., Hardwick S.J., Skepper J.N., Mitchinson M.J. Changes in vimentin in human macrophages during apoptosis induced by oxidised low density lipoprotein. Atherosclerosis 2001, 156:133-144.
    • (2001) Atherosclerosis , vol.156 , pp. 133-144
    • Muller, K.1    Dulku, S.2    Hardwick, S.J.3    Skepper, J.N.4    Mitchinson, M.J.5
  • 48
    • 77956301589 scopus 로고    scopus 로고
    • Vimentin is a novel anti-cancer therapeutic target; insights from in vitro and in vivo mice xenograft studies
    • Lahat G., Zhu Q.S., Huang K.L., Wang S., Bolshakov S., Liu J., et al. Vimentin is a novel anti-cancer therapeutic target; insights from in vitro and in vivo mice xenograft studies. PLoS One 2010, 5:e10105.
    • (2010) PLoS One , vol.5
    • Lahat, G.1    Zhu, Q.S.2    Huang, K.L.3    Wang, S.4    Bolshakov, S.5    Liu, J.6
  • 50
    • 0026001739 scopus 로고
    • Characterization of the gene for a proliferation-related phosphoprotein (oncoprotein 18) expressed in high amounts in acute leukemia
    • Melhem R.F., Zhu X.X., Hailat N., Strahler J.R., Hanash S.M. Characterization of the gene for a proliferation-related phosphoprotein (oncoprotein 18) expressed in high amounts in acute leukemia. J Biol Chem 1991, 266:17747-17753.
    • (1991) J Biol Chem , vol.266 , pp. 17747-17753
    • Melhem, R.F.1    Zhu, X.X.2    Hailat, N.3    Strahler, J.R.4    Hanash, S.M.5
  • 51
    • 0038577270 scopus 로고    scopus 로고
    • Stathmin expression and megakaryocyte differentiation: a potential role in polyploidy
    • Rubin C.I., French D.L., Atweh G.F. Stathmin expression and megakaryocyte differentiation: a potential role in polyploidy. Exp Hematol 2003, 31:389-397.
    • (2003) Exp Hematol , vol.31 , pp. 389-397
    • Rubin, C.I.1    French, D.L.2    Atweh, G.F.3
  • 52
    • 0033019054 scopus 로고    scopus 로고
    • Mutations of oncoprotein 18/stathmin identify tubulin-directed regulatory activities distinct from tubulin association
    • Larsson N., Segerman B., Gradin H.M., Wandzioch E., Cassimeris L., Gullberg M. Mutations of oncoprotein 18/stathmin identify tubulin-directed regulatory activities distinct from tubulin association. Mol Cell Biol 1999, 19:2242-2250.
    • (1999) Mol Cell Biol , vol.19 , pp. 2242-2250
    • Larsson, N.1    Segerman, B.2    Gradin, H.M.3    Wandzioch, E.4    Cassimeris, L.5    Gullberg, M.6
  • 53
  • 55
    • 34447315270 scopus 로고    scopus 로고
    • HDAC6 modulates cell motility by altering the acetylation level of cortactin
    • Zhang X., Yuan Z., Zhang Y., Yong S., Salas-Burgos A., Koomen J., et al. HDAC6 modulates cell motility by altering the acetylation level of cortactin. Mol Cell 2007, 27:197-213.
    • (2007) Mol Cell , vol.27 , pp. 197-213
    • Zhang, X.1    Yuan, Z.2    Zhang, Y.3    Yong, S.4    Salas-Burgos, A.5    Koomen, J.6
  • 56
    • 67349256384 scopus 로고    scopus 로고
    • PAK kinase regulates Rac GTPase and is a potential target in human schwannomas
    • Flaiz C., Chernoff J., Ammoun S., Peterson J.R., Hanemann C.O. PAK kinase regulates Rac GTPase and is a potential target in human schwannomas. Exp Neurol 2009, 218:137-144.
    • (2009) Exp Neurol , vol.218 , pp. 137-144
    • Flaiz, C.1    Chernoff, J.2    Ammoun, S.3    Peterson, J.R.4    Hanemann, C.O.5
  • 58
    • 68249135245 scopus 로고    scopus 로고
    • Calpain inhibition induces activation of the distinct signalling pathways and cell migration in human monocytes
    • Noma H., Kato T., Fujita H., Kitagawa M., Yamano T., Kitagawa S. Calpain inhibition induces activation of the distinct signalling pathways and cell migration in human monocytes. Immunology 2009, 128:e487-e496.
    • (2009) Immunology , vol.128
    • Noma, H.1    Kato, T.2    Fujita, H.3    Kitagawa, M.4    Yamano, T.5    Kitagawa, S.6
  • 59
    • 77952289448 scopus 로고    scopus 로고
    • RhoH plays distinct roles in T-cell migrations induced by different doses of SDF1 alpha
    • Wang H., Zeng X., Fan Z., Lim B. RhoH plays distinct roles in T-cell migrations induced by different doses of SDF1 alpha. Cell Signal 2010, 22:1022-1032.
    • (2010) Cell Signal , vol.22 , pp. 1022-1032
    • Wang, H.1    Zeng, X.2    Fan, Z.3    Lim, B.4
  • 60
    • 34247621290 scopus 로고    scopus 로고
    • Rho GTPase Cdc42 coordinates hematopoietic stem cell quiescence and niche interaction in the bone marrow
    • Yang L., Wang L., Geiger H., Cancelas J.A., Mo J., Zheng Y. Rho GTPase Cdc42 coordinates hematopoietic stem cell quiescence and niche interaction in the bone marrow. Proc Natl Acad Sci U S A 2007, 104:5091-5096.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 5091-5096
    • Yang, L.1    Wang, L.2    Geiger, H.3    Cancelas, J.A.4    Mo, J.5    Zheng, Y.6
  • 61
    • 41949100602 scopus 로고    scopus 로고
    • An isoform-selective, small-molecule inhibitor targets the autoregulatory mechanism of p21-activated kinase
    • Deacon S.W., Beeser A., Fukui J.A., Rennefahrt U.E., Myers C., Chernoff J., et al. An isoform-selective, small-molecule inhibitor targets the autoregulatory mechanism of p21-activated kinase. Chem Biol 2008, 15:322-331.
    • (2008) Chem Biol , vol.15 , pp. 322-331
    • Deacon, S.W.1    Beeser, A.2    Fukui, J.A.3    Rennefahrt, U.E.4    Myers, C.5    Chernoff, J.6
  • 62
    • 70349484472 scopus 로고    scopus 로고
    • An allosteric kinase inhibitor binds the p21-activated kinase autoregulatory domain covalently
    • Viaud J., Peterson J.R. An allosteric kinase inhibitor binds the p21-activated kinase autoregulatory domain covalently. Mol Cancer Ther 2009, 8:2559-2565.
    • (2009) Mol Cancer Ther , vol.8 , pp. 2559-2565
    • Viaud, J.1    Peterson, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.