메뉴 건너뛰기




Volumn 78, Issue 8, 2009, Pages 1017-1025

Phosphorylation of human enhancer of filamentation (HEF1) on serine 369 induces its proteasomal degradation

Author keywords

Hesperadin; Human enhancer of filamentation 1; Protein phosphatase 2A; Protein stability

Indexed keywords

AURORA B KINASE; CELL PROTEIN; DOCKING PROTEIN; HESPERADIN; HUMAN ENHANCER OF FILAMENTATION 1 PROTEIN; OKADAIC ACID; P105 HUMAN ENHANCER OF FILAMENTATION 1 PROTEIN; P115 HUMAN ENHANCER OF FILAMENTATION 1 PROTEIN; PROTEASOME; SERINE; UNCLASSIFIED DRUG;

EID: 69349084808     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2009.06.005     Document Type: Article
Times cited : (10)

References (43)
  • 1
    • 0034160011 scopus 로고    scopus 로고
    • Integrin signalling: a new Cas(t) of characters enters the stage
    • O'Neill G.M., Fashena S.J., and Golemis E.A. Integrin signalling: a new Cas(t) of characters enters the stage. Trends Cell Biol 10 (2000) 111-119
    • (2000) Trends Cell Biol , vol.10 , pp. 111-119
    • O'Neill, G.M.1    Fashena, S.J.2    Golemis, E.A.3
  • 2
    • 0029891787 scopus 로고    scopus 로고
    • Human enhancer of filamentation 1, a novel p130cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae
    • Law S.F., Estojak J., Wang B., Mysliwiec T., Kruh G., and Golemis E.A. Human enhancer of filamentation 1, a novel p130cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae. Mol Cell Biol 16 (1996) 3327-3337
    • (1996) Mol Cell Biol , vol.16 , pp. 3327-3337
    • Law, S.F.1    Estojak, J.2    Wang, B.3    Mysliwiec, T.4    Kruh, G.5    Golemis, E.A.6
  • 3
    • 0029904694 scopus 로고    scopus 로고
    • Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes
    • Minegishi M., Tachibana K., Sato T., Iwata S., Nojima Y., and Morimoto C. Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes. J Exp Med 184 (1996) 1365-1375
    • (1996) J Exp Med , vol.184 , pp. 1365-1375
    • Minegishi, M.1    Tachibana, K.2    Sato, T.3    Iwata, S.4    Nojima, Y.5    Morimoto, C.6
  • 4
    • 0030614912 scopus 로고    scopus 로고
    • Involvement of p130(Cas) and p105(HEF1), a novel Cas-like docking protein, in a cytoskeleton-dependent signaling pathway initiated by ligation of integrin or antigen receptor on human B cells
    • Manie S.N., Beck A.R., Astier A., Law S.F., Canty T., Hirai H., et al. Involvement of p130(Cas) and p105(HEF1), a novel Cas-like docking protein, in a cytoskeleton-dependent signaling pathway initiated by ligation of integrin or antigen receptor on human B cells. J Biol Chem 272 (1997) 4230-4236
    • (1997) J Biol Chem , vol.272 , pp. 4230-4236
    • Manie, S.N.1    Beck, A.R.2    Astier, A.3    Law, S.F.4    Canty, T.5    Hirai, H.6
  • 5
    • 0033214510 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Crk-associated substrate lymphocyte-type is a critical element in TCR- and beta 1 integrin-induced T lymphocyte migration
    • Ohashi Y., Iwata S., Kamiguchi K., and Morimoto C. Tyrosine phosphorylation of Crk-associated substrate lymphocyte-type is a critical element in TCR- and beta 1 integrin-induced T lymphocyte migration. J Immunol 163 (1999) 3727-3734
    • (1999) J Immunol , vol.163 , pp. 3727-3734
    • Ohashi, Y.1    Iwata, S.2    Kamiguchi, K.3    Morimoto, C.4
  • 6
    • 0035006726 scopus 로고    scopus 로고
    • Focal adhesion kinase regulates beta1 integrin-dependent T cell migration through an HEF1 effector pathway
    • van Seventer G.A., Salmen H.J., Law S.F., O'Neill G.M., Mullen M.M., Franz A.M., et al. Focal adhesion kinase regulates beta1 integrin-dependent T cell migration through an HEF1 effector pathway. Eur J Immunol 31 (2001) 1417-1427
    • (2001) Eur J Immunol , vol.31 , pp. 1417-1427
    • van Seventer, G.A.1    Salmen, H.J.2    Law, S.F.3    O'Neill, G.M.4    Mullen, M.M.5    Franz, A.M.6
  • 7
    • 0034711316 scopus 로고    scopus 로고
    • Integrin engagement, the actin cytoskeleton, and c-Src are required for the calcitonin-induced tyrosine phosphorylation of paxillin and HEF1, but not for calcitonin-induced Erk1/2 phosphorylation
    • Zhang Z., Baron R., and Horne W.C. Integrin engagement, the actin cytoskeleton, and c-Src are required for the calcitonin-induced tyrosine phosphorylation of paxillin and HEF1, but not for calcitonin-induced Erk1/2 phosphorylation. J Biol Chem 275 (2000) 37219-37223
    • (2000) J Biol Chem , vol.275 , pp. 37219-37223
    • Zhang, Z.1    Baron, R.2    Horne, W.C.3
  • 8
    • 0031416275 scopus 로고    scopus 로고
    • Association of the Cas-like molecule HEF1 with CrkL following integrin and antigen receptor signaling in human B-cells: potential relevance to neoplastic lymphohematopoietic cells
    • Astier A., Manie S.N., Law S.F., Canty T., Haghayghi N., Druker B.J., et al. Association of the Cas-like molecule HEF1 with CrkL following integrin and antigen receptor signaling in human B-cells: potential relevance to neoplastic lymphohematopoietic cells. Leuk Lymphoma 28 (1997) 65-72
    • (1997) Leuk Lymphoma , vol.28 , pp. 65-72
    • Astier, A.1    Manie, S.N.2    Law, S.F.3    Canty, T.4    Haghayghi, N.5    Druker, B.J.6
  • 9
    • 0037438577 scopus 로고    scopus 로고
    • The GDP exchange factor AND-34 is expressed in B cells, associates with HEF1, and activates Cdc42
    • Cai D., Felekkis K.N., Near R.I., O'Neill G.M., van Seventer J.M., Golemis E.A., et al. The GDP exchange factor AND-34 is expressed in B cells, associates with HEF1, and activates Cdc42. J Immunol 170 (2003) 969-978
    • (2003) J Immunol , vol.170 , pp. 969-978
    • Cai, D.1    Felekkis, K.N.2    Near, R.I.3    O'Neill, G.M.4    van Seventer, J.M.5    Golemis, E.A.6
  • 10
    • 33644868709 scopus 로고    scopus 로고
    • Deregulation of HEF1 impairs M-phase progression by disrupting the RhoA activation cycle
    • Dadke D., Jarnik M., Pugacheva E.N., Singh M.K., and Golemis E.A. Deregulation of HEF1 impairs M-phase progression by disrupting the RhoA activation cycle. Mol Biol Cell 17 (2006) 1204-1217
    • (2006) Mol Biol Cell , vol.17 , pp. 1204-1217
    • Dadke, D.1    Jarnik, M.2    Pugacheva, E.N.3    Singh, M.K.4    Golemis, E.A.5
  • 11
    • 33845490019 scopus 로고    scopus 로고
    • The hematopoietic isoform of Cas-Hef1-associated signal transducer regulates chemokine-induced inside-out signaling and T cell trafficking
    • Regelmann A.G., Danzl N.M., Wanjalla C., and Alexandropoulos K. The hematopoietic isoform of Cas-Hef1-associated signal transducer regulates chemokine-induced inside-out signaling and T cell trafficking. Immunity 25 (2006) 907-918
    • (2006) Immunity , vol.25 , pp. 907-918
    • Regelmann, A.G.1    Danzl, N.M.2    Wanjalla, C.3    Alexandropoulos, K.4
  • 12
    • 0030611712 scopus 로고    scopus 로고
    • Differential signaling after beta1 integrin ligation is mediated through binding of CRKL to p120(CBL) and p110(HEF1)
    • Sattler M., Salgia R., Shrikhande G., Verma S., Uemura N., Law S.F., et al. Differential signaling after beta1 integrin ligation is mediated through binding of CRKL to p120(CBL) and p110(HEF1). J Biol Chem 272 (1997) 14320-14326
    • (1997) J Biol Chem , vol.272 , pp. 14320-14326
    • Sattler, M.1    Salgia, R.2    Shrikhande, G.3    Verma, S.4    Uemura, N.5    Law, S.F.6
  • 13
    • 0036153173 scopus 로고    scopus 로고
    • Dissection of HEF1-dependent functions in motility and transcriptional regulation
    • Fashena S.J., Einarson M.B., O'Neill G.M., Patriotis C., and Golemis E.A. Dissection of HEF1-dependent functions in motility and transcriptional regulation. J Cell Sci 115 (2002) 99-111
    • (2002) J Cell Sci , vol.115 , pp. 99-111
    • Fashena, S.J.1    Einarson, M.B.2    O'Neill, G.M.3    Patriotis, C.4    Golemis, E.A.5
  • 14
    • 24744452389 scopus 로고    scopus 로고
    • Crk-associated substrate lymphocyte type is required for lymphocyte trafficking and marginal zone B cell maintenance
    • Seo S., Asai T., Saito T., Suzuki T., Morishita Y., Nakamoto T., et al. Crk-associated substrate lymphocyte type is required for lymphocyte trafficking and marginal zone B cell maintenance. J Immunol 175 (2005) 3492-3501
    • (2005) J Immunol , vol.175 , pp. 3492-3501
    • Seo, S.1    Asai, T.2    Saito, T.3    Suzuki, T.4    Morishita, Y.5    Nakamoto, T.6
  • 15
    • 33745288277 scopus 로고    scopus 로고
    • Comparative oncogenomics identifies NEDD9 as a melanoma metastasis gene
    • Kim M., Gans J.D., Nogueira C., Wang A., Paik J.H., Feng B., et al. Comparative oncogenomics identifies NEDD9 as a melanoma metastasis gene. Cell 125 (2006) 1269-1281
    • (2006) Cell , vol.125 , pp. 1269-1281
    • Kim, M.1    Gans, J.D.2    Nogueira, C.3    Wang, A.4    Paik, J.H.5    Feng, B.6
  • 16
    • 0034671642 scopus 로고    scopus 로고
    • A novel ability of Smad3 to regulate proteasomal degradation of a Cas family member HEF1
    • Liu X., Elia A.E., Law S.F., Golemis E.A., Farley J., and Wang T. A novel ability of Smad3 to regulate proteasomal degradation of a Cas family member HEF1. EMBO J 19 (2000) 6759-6769
    • (2000) EMBO J , vol.19 , pp. 6759-6769
    • Liu, X.1    Elia, A.E.2    Law, S.F.3    Golemis, E.A.4    Farley, J.5    Wang, T.6
  • 17
    • 10444279104 scopus 로고    scopus 로고
    • Direct interaction between Smad3, APC10, CDH1 and HEF1 in proteasomal degradation of HEF1
    • Nourry C., Maksumova L., Pang M., Liu X., and Wang T. Direct interaction between Smad3, APC10, CDH1 and HEF1 in proteasomal degradation of HEF1. BMC Cell Biol 5 (2004) 20
    • (2004) BMC Cell Biol , vol.5 , pp. 20
    • Nourry, C.1    Maksumova, L.2    Pang, M.3    Liu, X.4    Wang, T.5
  • 18
    • 3142723481 scopus 로고    scopus 로고
    • Atrophin-1-interacting protein 4/human Itch is a ubiquitin E3 ligase for human enhancer of filamentation 1 in transforming growth factor-beta signaling pathways
    • Feng L., Guedes S., and Wang T. Atrophin-1-interacting protein 4/human Itch is a ubiquitin E3 ligase for human enhancer of filamentation 1 in transforming growth factor-beta signaling pathways. J Biol Chem 279 (2004) 29681-29690
    • (2004) J Biol Chem , vol.279 , pp. 29681-29690
    • Feng, L.1    Guedes, S.2    Wang, T.3
  • 19
    • 31644445295 scopus 로고    scopus 로고
    • Cell adhesion regulates Ser/Thr phosphorylation and proteasomal degradation of HEF1
    • Zheng M., and McKeown-Longo P.J. Cell adhesion regulates Ser/Thr phosphorylation and proteasomal degradation of HEF1. J Cell Sci 119 (2006) 96-103
    • (2006) J Cell Sci , vol.119 , pp. 96-103
    • Zheng, M.1    McKeown-Longo, P.J.2
  • 20
    • 0031813880 scopus 로고    scopus 로고
    • Cell cycle-regulated processing of HEF1 to multiple protein forms differentially targeted to multiple subcellular compartments
    • Law S.F., Zhang Y.Z., Klein-Szanto A.J., and Golemis E.A. Cell cycle-regulated processing of HEF1 to multiple protein forms differentially targeted to multiple subcellular compartments. Mol Cell Biol 18 (1998) 3540-3551
    • (1998) Mol Cell Biol , vol.18 , pp. 3540-3551
    • Law, S.F.1    Zhang, Y.Z.2    Klein-Szanto, A.J.3    Golemis, E.A.4
  • 21
    • 0037131380 scopus 로고    scopus 로고
    • Regulation of HEF1 expression and phosphorylation by TGF-beta 1 and cell adhesion
    • Zheng M., and McKeown-Longo P.J. Regulation of HEF1 expression and phosphorylation by TGF-beta 1 and cell adhesion. J Biol Chem 277 (2002) 39599-39608
    • (2002) J Biol Chem , vol.277 , pp. 39599-39608
    • Zheng, M.1    McKeown-Longo, P.J.2
  • 22
    • 27144495462 scopus 로고    scopus 로고
    • The focal adhesion scaffolding protein HEF1 regulates activation of the Aurora-A and Nek2 kinases at the centrosome
    • Pugacheva E.N., and Golemis E.A. The focal adhesion scaffolding protein HEF1 regulates activation of the Aurora-A and Nek2 kinases at the centrosome. Nat Cell Biol 7 (2005) 937-946
    • (2005) Nat Cell Biol , vol.7 , pp. 937-946
    • Pugacheva, E.N.1    Golemis, E.A.2
  • 23
    • 0033601745 scopus 로고    scopus 로고
    • Dissociation of FAK/p130(CAS)/c-Src complex during mitosis: role of mitosis-specific serine phosphorylation of FAK
    • Yamakita Y., Totsukawa G., Yamashiro S., Fry D., Zhang X., Hanks S.K., et al. Dissociation of FAK/p130(CAS)/c-Src complex during mitosis: role of mitosis-specific serine phosphorylation of FAK. J Cell Biol 144 (1999) 315-324
    • (1999) J Cell Biol , vol.144 , pp. 315-324
    • Yamakita, Y.1    Totsukawa, G.2    Yamashiro, S.3    Fry, D.4    Zhang, X.5    Hanks, S.K.6
  • 24
    • 0037143091 scopus 로고    scopus 로고
    • Protein phosphatase-2A regulates endothelial cell motility and both the phosphorylation and the stability of focal adhesion complexes
    • Young M.R., Kolesiak K., and Meisinger J. Protein phosphatase-2A regulates endothelial cell motility and both the phosphorylation and the stability of focal adhesion complexes. Int J Cancer 100 (2002) 276-282
    • (2002) Int J Cancer , vol.100 , pp. 276-282
    • Young, M.R.1    Kolesiak, K.2    Meisinger, J.3
  • 27
    • 0242551545 scopus 로고    scopus 로고
    • The cellular geography of aurora kinases
    • Carmena M., and Earnshaw W.C. The cellular geography of aurora kinases. Nat Rev Mol Cell Biol 4 (2003) 842-854
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 842-854
    • Carmena, M.1    Earnshaw, W.C.2
  • 28
    • 6344270057 scopus 로고    scopus 로고
    • Aurora kinases in spindle assembly and chromosome segregation
    • Ducat D., and Zheng Y. Aurora kinases in spindle assembly and chromosome segregation. Exp Cell Res 301 (2004) 60-67
    • (2004) Exp Cell Res , vol.301 , pp. 60-67
    • Ducat, D.1    Zheng, Y.2
  • 29
    • 0034609753 scopus 로고    scopus 로고
    • The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation
    • Walter A.O., Seghezzi W., Korver W., Sheung J., and Lees E. The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation. Oncogene 19 (2000) 4906-4916
    • (2000) Oncogene , vol.19 , pp. 4906-4916
    • Walter, A.O.1    Seghezzi, W.2    Korver, W.3    Sheung, J.4    Lees, E.5
  • 30
    • 85047696924 scopus 로고    scopus 로고
    • Aurora-B associated protein phosphatases as negative regulators of kinase activation
    • Sugiyama K., Sugiura K., Hara T., Sugimoto K., Shima H., Honda K., et al. Aurora-B associated protein phosphatases as negative regulators of kinase activation. Oncogene 21 (2002) 3103-3111
    • (2002) Oncogene , vol.21 , pp. 3103-3111
    • Sugiyama, K.1    Sugiura, K.2    Hara, T.3    Sugimoto, K.4    Shima, H.5    Honda, K.6
  • 31
    • 0038746733 scopus 로고    scopus 로고
    • The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint
    • Hauf S., Cole R.W., LaTerra S., Zimmer C., Schnapp G., Walter R., et al. The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint. J Cell Biol 161 (2003) 281-294
    • (2003) J Cell Biol , vol.161 , pp. 281-294
    • Hauf, S.1    Cole, R.W.2    LaTerra, S.3    Zimmer, C.4    Schnapp, G.5    Walter, R.6
  • 32
    • 0013057087 scopus 로고    scopus 로고
    • Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores
    • Ditchfield C., Johnson V.L., Tighe A., Ellston R., Haworth C., Johnson T., et al. Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores. J Cell Biol 161 (2003) 267-280
    • (2003) J Cell Biol , vol.161 , pp. 267-280
    • Ditchfield, C.1    Johnson, V.L.2    Tighe, A.3    Ellston, R.4    Haworth, C.5    Johnson, T.6
  • 33
    • 0347324949 scopus 로고    scopus 로고
    • Aurora-A kinase maintains the fidelity of early and late mitotic events in HeLa cells
    • Marumoto T., Honda S., Hara T., Nitta M., Hirota T., Kohmura E., et al. Aurora-A kinase maintains the fidelity of early and late mitotic events in HeLa cells. J Biol Chem 278 (2003) 51786-51795
    • (2003) J Biol Chem , vol.278 , pp. 51786-51795
    • Marumoto, T.1    Honda, S.2    Hara, T.3    Nitta, M.4    Hirota, T.5    Kohmura, E.6
  • 34
    • 11144354860 scopus 로고    scopus 로고
    • Autophosphorylation of a newly identified site of Aurora-B is indispensable for cytokinesis
    • Yasui Y., Urano T., Kawajiri A., Nagata K., Tatsuka M., Saya H., et al. Autophosphorylation of a newly identified site of Aurora-B is indispensable for cytokinesis. J Biol Chem 279 (2004) 12997-13003
    • (2004) J Biol Chem , vol.279 , pp. 12997-13003
    • Yasui, Y.1    Urano, T.2    Kawajiri, A.3    Nagata, K.4    Tatsuka, M.5    Saya, H.6
  • 35
    • 33749626550 scopus 로고    scopus 로고
    • Phosphorylation of Chk1 by ATR is antagonized by a Chk1-regulated protein phosphatase 2A circuit
    • Leung-Pineda V., Ryan C.E., and Piwnica-Worms H. Phosphorylation of Chk1 by ATR is antagonized by a Chk1-regulated protein phosphatase 2A circuit. Mol Cell Biol 26 (2006) 7529-7538
    • (2006) Mol Cell Biol , vol.26 , pp. 7529-7538
    • Leung-Pineda, V.1    Ryan, C.E.2    Piwnica-Worms, H.3
  • 36
    • 0035105516 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase-dependent activation of protein phosphatases 1 and 2A inhibits MEK1 and MEK2 activity and collagenase 1 (MMP-1) gene expression
    • Westermarck J., Li S.P., Kallunki T., Han J., and Kahari V.M. p38 mitogen-activated protein kinase-dependent activation of protein phosphatases 1 and 2A inhibits MEK1 and MEK2 activity and collagenase 1 (MMP-1) gene expression. Mol Cell Biol 21 (2001) 2373-2383
    • (2001) Mol Cell Biol , vol.21 , pp. 2373-2383
    • Westermarck, J.1    Li, S.P.2    Kallunki, T.3    Han, J.4    Kahari, V.M.5
  • 37
    • 34248199965 scopus 로고    scopus 로고
    • Activation of protein phosphatase 2A by palmitate inhibits AMP-activated protein kinase
    • Wu Y., Song P., Xu J., Zhang M., and Zou M.H. Activation of protein phosphatase 2A by palmitate inhibits AMP-activated protein kinase. J Biol Chem 282 (2007) 9777-9788
    • (2007) J Biol Chem , vol.282 , pp. 9777-9788
    • Wu, Y.1    Song, P.2    Xu, J.3    Zhang, M.4    Zou, M.H.5
  • 38
    • 0035921772 scopus 로고    scopus 로고
    • Protein phosphatase 2A interacts with the Src kinase substrate p130(CAS)
    • Yokoyama N., and Miller W.T. Protein phosphatase 2A interacts with the Src kinase substrate p130(CAS). Oncogene 20 (2001) 6057-6065
    • (2001) Oncogene , vol.20 , pp. 6057-6065
    • Yokoyama, N.1    Miller, W.T.2
  • 39
    • 0033152210 scopus 로고    scopus 로고
    • Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors
    • Zhu X., Kim J.L., Newcomb J.R., Rose P.E., Stover D.R., Toledo L.M., et al. Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors. Structure 7 (1999) 651-661
    • (1999) Structure , vol.7 , pp. 651-661
    • Zhu, X.1    Kim, J.L.2    Newcomb, J.R.3    Rose, P.E.4    Stover, D.R.5    Toledo, L.M.6
  • 40
  • 41
    • 37549026472 scopus 로고    scopus 로고
    • Mitotic histone H3 phosphorylation by vaccinia-related kinase 1 in mammalian cells
    • Kang T.H., Park D.Y., Choi Y.H., Kim K.J., Yoon H.S., and Kim K.T. Mitotic histone H3 phosphorylation by vaccinia-related kinase 1 in mammalian cells. Mol Cell Biol 27 (2007) 8533-8546
    • (2007) Mol Cell Biol , vol.27 , pp. 8533-8546
    • Kang, T.H.1    Park, D.Y.2    Choi, Y.H.3    Kim, K.J.4    Yoon, H.S.5    Kim, K.T.6
  • 42
    • 32544435801 scopus 로고    scopus 로고
    • Phosphorylation of the cytokinesis regulator ECT2 at G2/M phase stimulates association of the mitotic kinase Plk1 and accumulation of GTP-bound RhoA
    • Niiya F., Tatsumoto T., Lee K.S., and Miki T. Phosphorylation of the cytokinesis regulator ECT2 at G2/M phase stimulates association of the mitotic kinase Plk1 and accumulation of GTP-bound RhoA. Oncogene 25 (2006) 827-837
    • (2006) Oncogene , vol.25 , pp. 827-837
    • Niiya, F.1    Tatsumoto, T.2    Lee, K.S.3    Miki, T.4
  • 43
    • 33645220356 scopus 로고    scopus 로고
    • A interactions: points of dialog between the cell cycle and cell attachment signaling networks
    • Pugacheva E.N., Golemis E.A., and HEF1-aurora. A interactions: points of dialog between the cell cycle and cell attachment signaling networks. Cell Cycle 5 (2006) 384-391
    • (2006) Cell Cycle , vol.5 , pp. 384-391
    • Pugacheva, E.N.1    Golemis, E.A.2    HEF1-aurora3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.