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Volumn 6, Issue 293, 2013, Pages

A cancer-associated mutation in atypical protein kinase Cι occurs in a substrate-specific recruitment motif

Author keywords

[No Author keywords available]

Indexed keywords

LLGL2 PROTEIN; MYOSIN; PROTEIN KINASE C IOTA; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84885770661     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2004068     Document Type: Article
Times cited : (24)

References (74)
  • 1
    • 0028298476 scopus 로고
    • A new member of the third class in the protein kinase C family, PKCλ, expressed dominantly in an undifferentiated mouse embryonal carcinoma cell line and also in many tissues and cells
    • K. Akimoto, K. Mizuno, S. Osada, S. Hirai, S. Tanuma, K. Suzuki, S. Ohno, A new member of the third class in the protein kinase C family, PKCλ, expressed dominantly in an undifferentiated mouse embryonal carcinoma cell line and also in many tissues and cells. J. Biol. Chem. 269, 12677-12683 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 12677-12683
    • Akimoto, K.1    Mizuno, K.2    Osada, S.3    Hirai, S.4    Tanuma, S.5    Suzuki, K.6    Ohno, S.7
  • 2
    • 0034253536 scopus 로고    scopus 로고
    • The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
    • G. Joberty, C. Petersen, L. Gao, I. G. Macara, The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat. Cell Biol. 2, 531-539 (2000).
    • (2000) Nat. Cell Biol. , vol.2 , pp. 531-539
    • Joberty, G.1    Petersen, C.2    Gao, L.3    Macara, I.G.4
  • 3
    • 0033153320 scopus 로고    scopus 로고
    • The interaction of p62 with RIP links the atypical PKCs to NF-κB activation
    • L. Sanz, P. Sanchez, M. J. Lallena, M. T. Diaz-Meco, J. Moscat, The interaction of p62 with RIP links the atypical PKCs to NF-κB activation. EMBO J. 18, 3044-3053 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3044-3053
    • Sanz, L.1    Sanchez, P.2    Lallena, M.J.3    Diaz-Meco, M.T.4    Moscat, J.5
  • 9
    • 77950250455 scopus 로고    scopus 로고
    • Protein kinase Cι is required for pancreatic cancer cell transformed growth and tumorigenesis
    • M. L. Scotti, W. R. Bamlet, T. C. Smyrk, A. P. Fields, N. R. Murray, Protein kinase Cι is required for pancreatic cancer cell transformed growth and tumorigenesis. Cancer Res. 70, 2064-2074 (2010).
    • (2010) Cancer Res. , vol.70 , pp. 2064-2074
    • Scotti, M.L.1    Bamlet, W.R.2    Smyrk, T.C.3    Fields, A.P.4    Murray, N.R.5
  • 11
    • 39049087115 scopus 로고    scopus 로고
    • Correlation of aPKC-iota and E-cadherin expression with invasion and prognosis of cholangiocarcinoma
    • Q. Li, J. M. Wang, C. Liu, B. L. Xiao, J. X. Lu, S. Q. Zou, Correlation of aPKC-iota and E-cadherin expression with invasion and prognosis of cholangiocarcinoma. Hepatobiliary Pancreat. Dis. Int. 7, 70-75 (2008).
    • (2008) Hepatobiliary Pancreat. Dis. Int. , vol.7 , pp. 70-75
    • Li, Q.1    Wang, J.M.2    Liu, C.3    Xiao, B.L.4    Lu, J.X.5    Zou, S.Q.6
  • 13
    • 34447102014 scopus 로고    scopus 로고
    • Polarity regulators and the control of epithelial architecture, cell migration, and tumorigenesis
    • L. E. Dow, P. O. Humbert, Polarity regulators and the control of epithelial architecture, cell migration, and tumorigenesis. Int. Rev. Cytol. 262, 253-302 (2007).
    • (2007) Int. Rev. Cytol. , vol.262 , pp. 253-302
    • Dow, L.E.1    Humbert, P.O.2
  • 14
    • 67650661180 scopus 로고    scopus 로고
    • Cell polarity protein Lgl2 is lost or aberrantly localized in gastric dysplasia and adenocarcinoma: An immunohistochemical study
    • M. Lisovsky, K. Dresser, S. Baker, A. Fisher, B. Woda, B. Banner, G. Y. Lauwers, Cell polarity protein Lgl2 is lost or aberrantly localized in gastric dysplasia and adenocarcinoma: An immunohistochemical study. Mod. Pathol. 22, 977-984 (2009).
    • (2009) Mod. Pathol. , vol.22 , pp. 977-984
    • Lisovsky, M.1    Dresser, K.2    Baker, S.3    Fisher, A.4    Woda, B.5    Banner, B.6    Lauwers, G.Y.7
  • 16
    • 77951937872 scopus 로고    scopus 로고
    • Immunohistochemistry for cell polarity protein lethal giant larvae 2 differentiates pancreatic intraepithelial neoplasia-3 and ductal adenocarcinoma of the pancreas from lower-grade pancreatic intraepithelial neoplasias
    • M. Lisovsky, K. Dresser, B. Woda, M. Mino-Kenudson, Immunohistochemistry for cell polarity protein lethal giant larvae 2 differentiates pancreatic intraepithelial neoplasia-3 and ductal adenocarcinoma of the pancreas from lower-grade pancreatic intraepithelial neoplasias. Hum. Pathol. 41, 902-909 (2010).
    • (2010) Hum. Pathol. , vol.41 , pp. 902-909
    • Lisovsky, M.1    Dresser, K.2    Woda, B.3    Mino-Kenudson, M.4
  • 20
    • 54749152429 scopus 로고    scopus 로고
    • Identification of a small molecule with synthetic lethality for K-ras and protein kinase C iota
    • W. Guo, S. Wu, J. Liu, B. Fang, Identification of a small molecule with synthetic lethality for K-ras and protein kinase C iota. Cancer Res. 68, 7403-7408 (2008).
    • (2008) Cancer Res. , vol.68 , pp. 7403-7408
    • Guo, W.1    Wu, S.2    Liu, J.3    Fang, B.4
  • 22
    • 0032487494 scopus 로고    scopus 로고
    • An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3
    • Y. Izumi, T. Hirose, Y. Tamai, S. Hirai, Y. Nagashima, T. Fujimoto, Y. Tabuse, K. J. Kemphues, S. Ohno, An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3. J. Cell Biol. 143, 95-106 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 95-106
    • Izumi, Y.1    Hirose, T.2    Tamai, Y.3    Hirai, S.4    Nagashima, Y.5    Fujimoto, T.6    Tabuse, Y.7    Kemphues, K.J.8    Ohno, S.9
  • 23
    • 84861073615 scopus 로고    scopus 로고
    • Substrate recognition mechanism of atypical protein kinase Cs revealed by the structure of PKCι in complex with a substrate peptide from Par-3
    • C. Wang, Y. Shang, J. Yu, M. Zhang, Substrate recognition mechanism of atypical protein kinase Cs revealed by the structure of PKCι in complex with a substrate peptide from Par-3. Structure 20, 791-801 (2012).
    • (2012) Structure , vol.20 , pp. 791-801
    • Wang, C.1    Shang, Y.2    Yu, J.3    Zhang, M.4
  • 24
    • 0032949091 scopus 로고    scopus 로고
    • PAR-6 is a conserved PDZ domain-containing protein that colocalizes with PAR-3 in Caenorhabditis elegans embryos
    • T. J. Hung, K. J. Kemphues, PAR-6 is a conserved PDZ domain-containing protein that colocalizes with PAR-3 in Caenorhabditis elegans embryos. Development 126, 127-135 (1999).
    • (1999) Development , vol.126 , pp. 127-135
    • Hung, T.J.1    Kemphues, K.J.2
  • 27
    • 0037456795 scopus 로고    scopus 로고
    • The Par complex directs asymmetric cell division by phosphorylating the cytoskeletal protein Lgl
    • J. Betschinger, K. Mechtler, J. A. Knoblich, The Par complex directs asymmetric cell division by phosphorylating the cytoskeletal protein Lgl. Nature 422, 326-330 (2003).
    • (2003) Nature , vol.422 , pp. 326-330
    • Betschinger, J.1    Mechtler, K.2    Knoblich, J.A.3
  • 28
    • 2942626082 scopus 로고    scopus 로고
    • Sequential roles of Cdc42, Par-6, aPKC, and Lgl in the establishment of epithelial polarity during Drosophila embryogenesis
    • A. Hutterer, J. Betschinger, M. Petronczki, J. A. Knoblich, Sequential roles of Cdc42, Par-6, aPKC, and Lgl in the establishment of epithelial polarity during Drosophila embryogenesis. Dev. Cell 6, 845-854 (2004).
    • (2004) Dev. Cell , vol.6 , pp. 845-854
    • Hutterer, A.1    Betschinger, J.2    Petronczki, M.3    Knoblich, J.A.4
  • 29
    • 13444267951 scopus 로고    scopus 로고
    • Phosphorylation-induced autoinhibition regulates the cytoskeletal protein Lethal (2) giant larvae
    • J. Betschinger, F. Eisenhaber, J. A. Knoblich, Phosphorylation-induced autoinhibition regulates the cytoskeletal protein Lethal (2) giant larvae. Curr. Biol. 15, 276-282 (2005).
    • (2005) Curr. Biol. , vol.15 , pp. 276-282
    • Betschinger, J.1    Eisenhaber, F.2    Knoblich, J.A.3
  • 31
    • 1942540791 scopus 로고    scopus 로고
    • Atypical PKC phosphorylates PAR-1 kinases to regulate localization and activity
    • J. B. Hurov, J. L. Watkins, H. Piwnica-Worms, Atypical PKC phosphorylates PAR-1 kinases to regulate localization and activity. Curr. Biol. 14, 736-741 (2004).
    • (2004) Curr. Biol. , vol.14 , pp. 736-741
    • Hurov, J.B.1    Watkins, J.L.2    Piwnica-Worms, H.3
  • 32
    • 79959927412 scopus 로고    scopus 로고
    • Willin and Par3 cooperatively regulate epithelial apical constriction through aPKC-mediated ROCK phosphorylation
    • T. Ishiuchi, M. Takeichi, Willin and Par3 cooperatively regulate epithelial apical constriction through aPKC-mediated ROCK phosphorylation. Nat. Cell Biol. 13, 860-866 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 860-866
    • Ishiuchi, T.1    Takeichi, M.2
  • 35
    • 0037954572 scopus 로고    scopus 로고
    • Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions
    • R. M. Biondi, A. R. Nebreda, Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions. Biochem. J. 372, 1-13 (2003).
    • (2003) Biochem. J. , vol.372 , pp. 1-13
    • Biondi, R.M.1    Nebreda, A.R.2
  • 36
    • 0037400611 scopus 로고    scopus 로고
    • Molecular recognitions in the MAP kinase cascades
    • T. Tanoue, E. Nishida, Molecular recognitions in the MAP kinase cascades. Cell. Signal. 15, 455-462 (2003).
    • (2003) Cell. Signal. , vol.15 , pp. 455-462
    • Tanoue, T.1    Nishida, E.2
  • 38
    • 24644488646 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif
    • A. Messerschmidt, S. Macieira, M. Velarde, M. Bädeker, C. Benda, A. Jestel, H. Brandstetter, T. Neuefeind, M. Blaesse, Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif. J. Mol. Biol. 352, 918-931 (2005).
    • (2005) J. Mol. Biol. , vol.352 , pp. 918-931
    • Messerschmidt, A.1    Macieira, S.2    Velarde, M.3    Bädeker, M.4    Benda, C.5    Jestel, A.6    Brandstetter, H.7    Neuefeind, T.8    Blaesse, M.9
  • 39
    • 77952076018 scopus 로고    scopus 로고
    • Structures of the PKC-ι kinase domain in its ATP-bound and apo forms reveal defined structures of residues 533-551 in the C-terminal tail and their roles in ATP binding
    • T. Takimura, K. Kamata, K. Fukasawa, H. Ohsawa, H. Komatani, T. Yoshizumi, I. Takahashi, H. Kotani, Y. Iwasawa, Structures of the PKC-ι kinase domain in its ATP-bound and apo forms reveal defined structures of residues 533-551 in the C-terminal tail and their roles in ATP binding. Acta Crystallogr. D Biol. Crystallogr. 66, 577-583 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 577-583
    • Takimura, T.1    Kamata, K.2    Fukasawa, K.3    Ohsawa, H.4    Komatani, H.5    Yoshizumi, T.6    Takahashi, I.7    Kotani, H.8    Iwasawa, Y.9
  • 40
    • 36749011864 scopus 로고    scopus 로고
    • Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface
    • X. Zhang, K. A. Pickin, R. Bose, N. Jura, P. A. Cole, J. Kuriyan, Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface. Nature 450, 741-744 (2007).
    • (2007) Nature , vol.450 , pp. 741-744
    • Zhang, X.1    Pickin, K.A.2    Bose, R.3    Jura, N.4    Cole, P.A.5    Kuriyan, J.6
  • 41
    • 67349125149 scopus 로고    scopus 로고
    • PKC maturation is promoted by nucleotide pocket occupation independently of intrinsic kinase activity
    • A. J. Cameron, C. Escribano, A. T. Saurin, B. Kostelecky, P. J. Parker, PKC maturation is promoted by nucleotide pocket occupation independently of intrinsic kinase activity. Nat. Struct. Mol. Biol. 16, 624-630 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 624-630
    • Cameron, A.J.1    Escribano, C.2    Saurin, A.T.3    Kostelecky, B.4    Parker, P.J.5
  • 43
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • M. D. Resh, Myristylation and palmitylation of Src family members: The fats of the matter. Cell 76, 411-413 (1994).
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 44
    • 0024500964 scopus 로고
    • Unique substrate specificity and regulatory properties of PKC- e: A rationale for diversity
    • D. Schaap, P. J. Parker, A. Bristol, R. Kriz, J. Knopf, Unique substrate specificity and regulatory properties of PKC- e: A rationale for diversity. FEBS Lett. 243, 351-357 (1989).
    • (1989) FEBS Lett. , vol.243 , pp. 351-357
    • Schaap, D.1    Parker, P.J.2    Bristol, A.3    Kriz, R.4    Knopf, J.5
  • 45
    • 0035911955 scopus 로고    scopus 로고
    • Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures
    • A. Suzuki, T. Yamanaka, T. Hirose, N. Manabe, K. Mizuno, M. Shimizu, K. Akimoto, Y. Izumi, T. Ohnishi, S. Ohno, Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures. J. Cell Biol. 152, 1183-1196 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 1183-1196
    • Suzuki, A.1    Yamanaka, T.2    Hirose, T.3    Manabe, N.4    Mizuno, K.5    Shimizu, M.6    Akimoto, K.7    Izumi, Y.8    Ohnishi, T.9    Ohno, S.10
  • 47
    • 25444443688 scopus 로고    scopus 로고
    • Modelling glandular epithelial cancers in three-dimensional cultures
    • J. Debnath, J. S. Brugge, Modelling glandular epithelial cancers in three-dimensional cultures. Nat. Rev. Cancer 5, 675-688 (2005).
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 675-688
    • Debnath, J.1    Brugge, J.S.2
  • 48
    • 58149191544 scopus 로고    scopus 로고
    • Cdc42 controls spindle orientation to position the apical surface during epithelial morphogenesis
    • A. B. Jaffe, N. Kaji, J. Durgan, A. Hall, Cdc42 controls spindle orientation to position the apical surface during epithelial morphogenesis. J. Cell Biol. 183, 625-633 (2008).
    • (2008) J. Cell Biol. , vol.183 , pp. 625-633
    • Jaffe, A.B.1    Kaji, N.2    Durgan, J.3    Hall, A.4
  • 49
    • 79953293527 scopus 로고    scopus 로고
    • Par6B and atypical PKC regulate mitotic spindle orientation during epithelial morphogenesis
    • J. Durgan, N. Kaji, D. Jin, A. Hall, Par6B and atypical PKC regulate mitotic spindle orientation during epithelial morphogenesis. J. Biol. Chem. 286, 12461-12474 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 12461-12474
    • Durgan, J.1    Kaji, N.2    Jin, D.3    Hall, A.4
  • 50
    • 14744275517 scopus 로고    scopus 로고
    • PATJ regulates tight junction formation and polarity in mammalian epithelial cells
    • K. Shin, S. Straight, B. Margolis, PATJ regulates tight junction formation and polarity in mammalian epithelial cells. J. Cell Biol. 168, 705-711 (2005).
    • (2005) J. Cell Biol. , vol.168 , pp. 705-711
    • Shin, K.1    Straight, S.2    Margolis, B.3
  • 54
    • 4644326930 scopus 로고    scopus 로고
    • A microtubule-binding myosin required for nuclear anchoring and spindle assembly
    • K. L. Weber, A. M. Sokac, J. S. Berg, R. E. Cheney, W. M. Bement, A microtubule-binding myosin required for nuclear anchoring and spindle assembly. Nature 431, 325-329 (2004).
    • (2004) Nature , vol.431 , pp. 325-329
    • Weber, K.L.1    Sokac, A.M.2    Berg, J.S.3    Cheney, R.E.4    Bement, W.M.5
  • 55
    • 33747886310 scopus 로고    scopus 로고
    • Cell signaling and function organized by PB1 domain interactions
    • J. Moscat, M. T. Diaz-Meco, A. Albert, S. Campuzano, Cell signaling and function organized by PB1 domain interactions. Mol. Cell 23, 631-640 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 631-640
    • Moscat, J.1    Diaz-Meco, M.T.2    Albert, A.3    Campuzano, S.4
  • 56
    • 79959838081 scopus 로고    scopus 로고
    • Integrated genomic analyses of ovarian carcinoma
    • Cancer Genome Atlas Research Network
    • Cancer Genome Atlas Research Network, Integrated genomic analyses of ovarian carcinoma. Nature 474, 609-615 (2011).
    • (2011) Nature , vol.474 , pp. 609-615
  • 58
    • 0024413921 scopus 로고
    • A synthetic peptide analog of the putative substrate-binding motif activates protein kinase C
    • C. House, P. J. Robinson, B. E. Kemp, A synthetic peptide analog of the putative substrate-binding motif activates protein kinase C. FEBS Lett. 249, 243-247 (1989).
    • (1989) FEBS Lett , vol.249 , pp. 243-247
    • House, C.1    Robinson, P.J.2    Kemp, B.E.3
  • 59
    • 1842581909 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network
    • M. Brajenovic, G. Joberty, B. Küster, T. Bouwmeester, G. Drewes, Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network. J. Biol. Chem. 279, 12804-12811 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 12804-12811
    • Brajenovic, M.1    Joberty, G.2    Küster, B.3    Bouwmeester, T.4    Drewes, G.5
  • 61
    • 0035823492 scopus 로고    scopus 로고
    • Motor function and regulation of myosin X
    • K. Homma, J. Saito, R. Ikebe, M. Ikebe, Motor function and regulation of myosin X. J. Biol. Chem. 276, 34348-34354 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 34348-34354
    • Homma, K.1    Saito, J.2    Ikebe, R.3    Ikebe, M.4
  • 62
    • 0036122307 scopus 로고    scopus 로고
    • Myosin-X is an unconventional myosin that undergoes intrafilopodial motility
    • J. S. Berg, R. E. Cheney, Myosin-X is an unconventional myosin that undergoes intrafilopodial motility. Nat. Cell Biol. 4, 246-250 (2002).
    • (2002) Nat. Cell Biol. , vol.4 , pp. 246-250
    • Berg, J.S.1    Cheney, R.E.2
  • 63
    • 77953509417 scopus 로고    scopus 로고
    • Myosin-X induces filopodia by multiple elongation mechanism
    • T. M. Watanabe, H. Tokuo, K. Gonda, H. Higuchi, M. Ikebe, Myosin-X induces filopodia by multiple elongation mechanism. J. Biol. Chem. 285, 19605-19614 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 19605-19614
    • Watanabe, T.M.1    Tokuo, H.2    Gonda, K.3    Higuchi, H.4    Ikebe, M.5
  • 64
    • 33947596005 scopus 로고    scopus 로고
    • Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1- and myosin X-dependent manner
    • F. Toyoshima, E. Nishida, Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1- and myosin X-dependent manner. EMBO J. 26, 1487-1498 (2007).
    • (2007) EMBO J. , vol.26 , pp. 1487-1498
    • Toyoshima, F.1    Nishida, E.2
  • 65
    • 47549089279 scopus 로고    scopus 로고
    • Myosin-10 and actin filaments are essential for mitotic spindle function
    • S. Woolner, L. L. O'Brien, C. Wiese, W. M. Bement, Myosin-10 and actin filaments are essential for mitotic spindle function. J. Cell Biol. 182, 77-88 (2008).
    • (2008) J. Cell Biol. , vol.182 , pp. 77-88
    • Woolner, S.1    O'Brien, L.L.2    Wiese, C.3    Bement, W.M.4
  • 66
    • 67449114979 scopus 로고    scopus 로고
    • Interaction between PAR-3 and the aPKC-PAR-6 complex is indispensable for apical domain development of epithelial cells
    • Y. Horikoshi, A. Suzuki, T. Yamanaka, K. Sasaki, K. Mizuno, H. Sawada, S. Yonemura, S. Ohno, Interaction between PAR-3 and the aPKC-PAR-6 complex is indispensable for apical domain development of epithelial cells. J. Cell Sci. 122, 1595-1606 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 1595-1606
    • Horikoshi, Y.1    Suzuki, A.2    Yamanaka, T.3    Sasaki, K.4    Mizuno, K.5    Sawada, H.6    Yonemura, S.7    Ohno, S.8
  • 67
    • 76049106434 scopus 로고    scopus 로고
    • Polarity protein alterations in carcinoma: A focus on emerging roles for polarity regulators
    • L. Huang, S. K. Muthuswamy, Polarity protein alterations in carcinoma: A focus on emerging roles for polarity regulators. Curr. Opin. Genet. Dev. 20, 41-50 (2010).
    • (2010) Curr. Opin. Genet. Dev. , vol.20 , pp. 41-50
    • Huang, L.1    Muthuswamy, S.K.2
  • 68
    • 79953156769 scopus 로고    scopus 로고
    • Mitotic spindle misorientation in cancer - Out of alignment and into the fire
    • J. C. Pease, J. S. Tirnauer, Mitotic spindle misorientation in cancer - Out of alignment and into the fire. J. Cell Sci. 124, 1007-1016 (2011).
    • (2011) J. Cell Sci. , vol.124 , pp. 1007-1016
    • Pease, J.C.1    Tirnauer, J.S.2
  • 69
    • 0014546984 scopus 로고
    • Neoplasms in mutant and cultured wild-type tissues of Drosophila
    • E. Gateff, H. A. Schneiderman, Neoplasms in mutant and cultured wild-type tissues of Drosophila. Natl. Cancer Inst. Monogr. 31, 365 -397 (1969).
    • (1969) Natl. Cancer Inst. Monogr. , vol.31 , pp. 365-397
    • Gateff, E.1    Schneiderman, H.A.2
  • 73
    • 34548755067 scopus 로고    scopus 로고
    • Assay of protein kinases using radiolabeled ATP: A protocol
    • C. J. Hastie, H. J. McLauchlan, P. Cohen, Assay of protein kinases using radiolabeled ATP: A protocol. Nat. Protoc. 1, 968-971 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 968-971
    • Hastie, C.J.1    McLauchlan, H.J.2    Cohen, P.3


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