메뉴 건너뛰기




Volumn 19, Issue 10, 2011, Pages 1496-1508

Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68

Author keywords

[No Author keywords available]

Indexed keywords

APC PROTEIN; ARMADILLO DOMAIN PROTEIN; PROTEIN SAM68; TYROSINE;

EID: 80054060426     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2011.07.013     Document Type: Article
Times cited : (31)

References (66)
  • 2
    • 0029781509 scopus 로고    scopus 로고
    • Functional interaction of β-catenin with the transcription factor LEF- 1
    • DOI 10.1038/382638a0
    • J. Behrens, J.P. von Kries, M. Kühl, L. Bruhn, D. Wedlich, R. Grosschedl, and W. Birchmeier Functional interaction of β-catenin with the transcription factor LEF-1 Nature 382 1996 638 642 (Pubitemid 26268958)
    • (1996) Nature , vol.382 , Issue.6592 , pp. 638-642
    • Behrens, J.1    Von Kries, J.P.2    Kuhl, M.3    Bruhn, L.4    Wedlich, D.5    Grosschedl, R.6    Birchmeier, W.7
  • 4
    • 0023223410 scopus 로고
    • Localization of the gene for familial adenomatous polyposis on chromosome 5
    • DOI 10.1038/328614a0
    • W.F. Bodmer, C.J. Bailey, J. Bodmer, H.J. Bussey, A. Ellis, P. Gorman, F.C. Lucibello, V.A. Murday, S.H. Rider, and P. Scambler Localization of the gene for familial adenomatous polyposis on chromosome 5 Nature 328 1987 614 616 (Pubitemid 17103960)
    • (1987) Nature , vol.328 , Issue.6131 , pp. 614-616
    • Bodmer, W.F.1    Bailey, C.J.2    Bodmer, J.3
  • 5
    • 50849096682 scopus 로고    scopus 로고
    • The armadillo repeat domain of the APC tumor suppressor protein interacts with Striatin family members
    • M. Breitman, A. Zilberberg, M. Caspi, and R. Rosin-Arbesfeld The armadillo repeat domain of the APC tumor suppressor protein interacts with Striatin family members Biochim. Biophys. Acta 1783 2008 1792 1802
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1792-1802
    • Breitman, M.1    Zilberberg, A.2    Caspi, M.3    Rosin-Arbesfeld, R.4
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 7
    • 0032563246 scopus 로고    scopus 로고
    • Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin α
    • DOI 10.1016/S0092-8674(00)81419-1
    • E. Conti, M. Uy, L. Leighton, G. Blobel, and J. Kuriyan Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin α Cell 94 1998 193 204 (Pubitemid 28348007)
    • (1998) Cell , vol.94 , Issue.2 , pp. 193-204
    • Conti, E.1    Uy, M.2    Leighton, L.3    Blobel, G.4    Kuriyan, J.5
  • 8
    • 4143106996 scopus 로고    scopus 로고
    • Identification of APC gene mutations in colorectal cancer using universal microarray-based combinatorial sequencing-by-hybridization
    • DOI 10.1002/humu.20078
    • S. Cowie, S. Drmanac, D. Swanson, K. Delgrosso, S. Huang, D. du Sart, R. Drmanac, S. Surrey, and P. Fortina Identification of APC gene mutations in colorectal cancer using universal microarray-based combinatorial sequencing-by-hybridization Hum. Mutat. 24 2004 261 271 (Pubitemid 39095602)
    • (2004) Human Mutation , vol.24 , Issue.3 , pp. 261-271
    • Cowie, S.1    Drmanac, S.2    Swanson, D.3    Delgrosso, K.4    Huang, S.5    Du Sart, D.6    Drmanac, R.7    Surrey, S.8    Fortina, P.9
  • 9
    • 0036754604 scopus 로고    scopus 로고
    • ICAT inhibits β-catenin binding to tcf/lef-family transcription factors and the general coactivator p300 using independent structural modules
    • DOI 10.1016/S1097-2765(02)00631-7
    • D.L. Daniels, and W.I. Weis ICAT inhibits β-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules Mol. Cell 10 2002 573 584 (Pubitemid 35291069)
    • (2002) Molecular Cell , vol.10 , Issue.3 , pp. 573-584
    • Daniels, D.L.1    Weis, W.I.2
  • 10
    • 0035890060 scopus 로고    scopus 로고
    • Molecular mechanisms of β-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-β-catenin complex
    • DOI 10.1093/emboj/20.22.6203
    • K. Eklof Spink, S.G. Fridman, and W.I. Weis Molecular mechanisms of β-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-β-catenin complex EMBO J. 20 2001 6203 6212 (Pubitemid 33078694)
    • (2001) EMBO Journal , vol.20 , Issue.22 , pp. 6203-6212
    • Spink, K.E.1    Fridman, S.G.2    Weis, W.I.3
  • 12
    • 0028220672 scopus 로고
    • A target for Src in mitosis
    • DOI 10.1038/368871a0
    • S. Fumagalli, N.F. Totty, J.J. Hsuan, and S.A. Courtneidge A target for Src in mitosis Nature 368 1994 871 874 (Pubitemid 24137754)
    • (1994) Nature , vol.368 , Issue.6474 , pp. 871-874
    • Fumagalli, S.1    Totty, N.F.2    Hsuan, J.J.3    Courtneidge, S.A.4
  • 13
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • DOI 10.1093/bioinformatics/15.4.305
    • P. Gouet, E. Courcelle, D.I. Stuart, and F. Métoz ESPript: analysis of multiple sequence alignments in PostScript Bioinformatics 15 1999 305 308 (Pubitemid 29213756)
    • (1999) Bioinformatics , vol.15 , Issue.4 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 14
    • 0033635606 scopus 로고    scopus 로고
    • Crystal structure of a β-catenin/Tcf complex
    • T.A. Graham, C. Weaver, F. Mao, D. Kimelman, and W. Xu Crystal structure of a β-catenin/Tcf complex Cell 103 2000 885 896
    • (2000) Cell , vol.103 , pp. 885-896
    • Graham, T.A.1    Weaver, C.2    Mao, F.3    Kimelman, D.4    Xu, W.5
  • 15
    • 0035180690 scopus 로고    scopus 로고
    • Tcf4 can specifically recognize β-catenin using alternative conformations
    • DOI 10.1038/nsb718
    • T.A. Graham, D.M. Ferkey, F. Mao, D. Kimelman, and W. Xu Tcf4 can specifically recognize β-catenin using alternative conformations Nat. Struct. Biol. 8 2001 1048 1052 (Pubitemid 33101625)
    • (2001) Nature Structural Biology , vol.8 , Issue.12 , pp. 1048-1052
    • Graham, T.A.1    Ferkey, D.M.2    Mao, F.3    Kimelman, D.4    Xu, W.5
  • 16
    • 0036753258 scopus 로고    scopus 로고
    • The crystal structure of the β-catenin/ICAT complex reveals the inhibitory mechanism of ICAT
    • DOI 10.1016/S1097-2765(02)00637-8
    • T.A. Graham, W.K. Clements, D. Kimelman, and W. Xu The crystal structure of the β-catenin/ICAT complex reveals the inhibitory mechanism of ICAT Mol. Cell 10 2002 563 571 (Pubitemid 35284174)
    • (2002) Molecular Cell , vol.10 , Issue.3 , pp. 563-571
    • Graham, T.A.1    Clements, W.K.2    Kimelman, D.3    Xu, W.4
  • 18
    • 36549030350 scopus 로고    scopus 로고
    • AMER1 regulates the distribution of the tumor suppressor APC between microtubules and the plasma membrane
    • DOI 10.1242/jcs.011320
    • A. Grohmann, K. Tanneberger, A. Alzner, J. Schneikert, and J. Behrens AMER1 regulates the distribution of the tumor suppressor APC between microtubules and the plasma membrane J. Cell Sci. 120 2007 3738 3747 (Pubitemid 350187356)
    • (2007) Journal of Cell Science , vol.120 , Issue.21 , pp. 3738-3747
    • Grohmann, A.1    Tanneberger, K.2    Alzner, A.3    Schneikert, J.4    Behrens, J.5
  • 19
    • 4344562126 scopus 로고    scopus 로고
    • Mechanism of phosphorylation-dependent binding of APC to β-catenin and its role in β-catenin degradation
    • DOI 10.1016/j.molcel.2004.08.010, PII S109727650400471X
    • N.C. Ha, T. Tonozuka, J.L. Stamos, H.J. Choi, and W.I. Weis Mechanism of phosphorylation-dependent binding of APC to β-catenin and its role in β-catenin degradation Mol. Cell 15 2004 511 521 (Pubitemid 39141779)
    • (2004) Molecular Cell , vol.15 , Issue.4 , pp. 511-521
    • Ha, N.-C.1    Tonozuka, T.2    Stamos, J.L.3    Choi, H.-J.4    Weis, W.I.5
  • 20
    • 0032492954 scopus 로고    scopus 로고
    • Downregulation of β-catenin by human Axin and its association with the APC tumor suppressor, β-catenin and GSK3β
    • M.J. Hart, R. de los Santos, I.N. Albert, B. Rubinfeld, and P. Polakis Downregulation of β-catenin by human Axin and its association with the APC tumor suppressor, β-catenin and GSK3 β Curr. Biol. 8 1998 573 581 (Pubitemid 28222891)
    • (1998) Current Biology , vol.8 , Issue.10 , pp. 573-581
    • Hart, M.J.1    De Los Santos, R.2    Albert, I.N.3    Rubinfeld, B.4    Polakis, P.5
  • 21
    • 0029930324 scopus 로고    scopus 로고
    • Secondary structure of an armadillo single repeat from the APC protein
    • DOI 10.1016/0014-5793(96)00215-3
    • D. Hirschl, P. Bayer, and O. Müller Secondary structure of an armadillo single repeat from the APC protein FEBS Lett. 383 1996 31 36 (Pubitemid 26092630)
    • (1996) FEBS Letters , vol.383 , Issue.1-2 , pp. 31-36
    • Hirschl, D.1    Bayer, P.2    Muller, O.3
  • 22
    • 0035805117 scopus 로고    scopus 로고
    • The structure of the β-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by β-catenin
    • DOI 10.1016/S0092-8674(01)00330-0
    • A.H. Huber, and W.I. Weis The structure of the β-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by β-catenin Cell 105 2001 391 402 (Pubitemid 32455345)
    • (2001) Cell , vol.105 , Issue.3 , pp. 391-402
    • Huber, A.H.1    Weis, W.I.2
  • 23
    • 0345343608 scopus 로고    scopus 로고
    • Nuclear localization of β-catenin by interaction with transcription factor LEF-1
    • DOI 10.1016/0925-4773(96)00597-7
    • O. Huber, R. Korn, J. McLaughlin, M. Ohsugi, B.G. Herrmann, and R. Kemler Nuclear localization of β-catenin by interaction with transcription factor LEF-1 Mech. Dev. 59 1996 3 10 (Pubitemid 26325455)
    • (1996) Mechanisms of Development , vol.59 , Issue.1 , pp. 3-10
    • Huber, O.1    Korn, R.2    McLaughlin, J.3    Ohsugi, M.4    Herrmann, B.G.5    Kemler, R.6
  • 24
    • 77950932981 scopus 로고    scopus 로고
    • Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion
    • N. Ishiyama, S.H. Lee, S. Liu, G.Y. Li, M.J. Smith, L.F. Reichardt, and M. Ikura Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion Cell 141 2010 117 128
    • (2010) Cell , vol.141 , pp. 117-128
    • Ishiyama, N.1    Lee, S.H.2    Liu, S.3    Li, G.Y.4    Smith, M.J.5    Reichardt, L.F.6    Ikura, M.7
  • 25
    • 0032493042 scopus 로고    scopus 로고
    • Axis determination in Xenopus involves biochemical interactions of axin, glycogen synthase kinase 3 and β-catenin
    • K. Itoh, V.E. Krupnik, and S.Y. Sokol Axis determination in Xenopus involves biochemical interactions of axin, glycogen synthase kinase 3 and β-catenin Curr. Biol. 8 1998 591 594 (Pubitemid 28222894)
    • (1998) Current Biology , vol.8 , Issue.10 , pp. 591-594
    • Itoh, K.1    Krupnik, V.E.2    Sokol, S.Y.3
  • 26
    • 0036226855 scopus 로고    scopus 로고
    • Identification of a link between the tumour suppressor APC and the kinesin superfamily
    • DOI 10.1038/ncb779
    • T. Jimbo, Y. Kawasaki, R. Koyama, R. Sato, S. Takada, K. Haraguchi, and T. Akiyama Identification of a link between the tumour suppressor APC and the kinesin superfamily Nat. Cell Biol. 4 2002 323 327 (Pubitemid 34308860)
    • (2002) Nature Cell Biology , vol.4 , Issue.4 , pp. 323-327
    • Jimbo, T.1    Kawasaki, Y.2    Koyama, R.3    Sato, R.4    Takada, S.5    Haraguchi, K.6    Akiyama, T.7
  • 27
    • 0034682888 scopus 로고    scopus 로고
    • Asef, a link between the tumor suppressor APC and G-protein signaling
    • DOI 10.1126/science.289.5482.1194
    • Y. Kawasaki, T. Senda, T. Ishidate, R. Koyama, T. Morishita, Y. Iwayama, O. Higuchi, and T. Akiyama Asef, a link between the tumor suppressor APC and G-protein signaling Science 289 2000 1194 1197 (Pubitemid 30650732)
    • (2000) Science , vol.289 , Issue.5482 , pp. 1194-1197
    • Kawasaki, Y.1    Senda, T.2    Ishidate, T.3    Koyama, R.4    Morishita, T.5    Iwayama, Y.6    Higuchi, O.7    Akiyama, T.8
  • 28
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stable-isotope labeling of milligram quantities of proteins
    • DOI 10.1016/S0014-5793(98)01620-2, PII S0014579398016202
    • T. Kigawa, T. Yabuki, Y. Yoshida, M. Tsutsui, Y. Ito, T. Shibata, and S. Yokoyama Cell-free production and stable-isotope labeling of milligram quantities of proteins FEBS Lett. 442 1999 15 19 (Pubitemid 29065369)
    • (1999) FEBS Letters , vol.442 , Issue.1 , pp. 15-19
    • Kigawa, T.1    Yabuki, T.2    Yoshida, Y.3    Tsutsui, M.4    Ito, Y.5    Shibata, T.6    Yokoyama, S.7
  • 30
    • 0032079884 scopus 로고    scopus 로고
    • Axin, a negative regulator of the Wnt signaling pathway, directly interacts with adenomatous polyposis coli and regulates the stabilization of β-catenin
    • DOI 10.1074/jbc.273.18.10823
    • S. Kishida, H. Yamamoto, S. Ikeda, M. Kishida, I. Sakamoto, S. Koyama, and A. Kikuchi Axin, a negative regulator of the wnt signaling pathway, directly interacts with adenomatous polyposis coli and regulates the stabilization of β-catenin J. Biol. Chem. 273 1998 10823 10826 (Pubitemid 28204914)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.18 , pp. 10823-10826
    • Kishida, S.1    Yamamoto, H.2    Ikeda, S.3    Kishida, M.4    Sakamoto, I.5    Koyama, S.6    Kikuchi, A.7
  • 31
    • 0030975671 scopus 로고    scopus 로고
    • Constitutive transcriptional activation by a β-catenin-Tcf complex in APC(-/-) colon carcinoma
    • DOI 10.1126/science.275.5307.1784
    • V. Korinek, N. Barker, P.J. Morin, D. van Wichen, R. de Weger, K.W. Kinzler, B. Vogelstein, and H. Clevers Constitutive transcriptional activation by a β-catenin-Tcf complex in APC-/- colon carcinoma Science 275 1997 1784 1787 (Pubitemid 27136714)
    • (1997) Science , vol.275 , Issue.5307 , pp. 1784-1787
    • Korinek, V.1    Barker, N.2    Morin, P.J.3    Van Wichen, D.4    De Weger, R.5    Kinzler, K.W.6    Vogelstein, B.7    Clevers, H.8
  • 33
    • 0004148514 scopus 로고
    • MRC Laboratory of Molecular Biology Cambridge
    • A.G.W. Leslie MOSFLM Users Guide 1995 MRC Laboratory of Molecular Biology Cambridge
    • (1995) MOSFLM Users Guide
    • Leslie, A.G.W.1
  • 35
    • 0033588939 scopus 로고    scopus 로고
    • Drosophila APC2 is a cytoskeletally-associated protein that regulates wingless signaling in the embryonic epidermis
    • DOI 10.1083/jcb.146.6.1303
    • B.M. McCartney, H.A. Dierick, C. Kirkpatrick, M.M. Moline, A. Baas, M. Peifer, and A. Bejsovec Drosophila APC2 is a cytoskeletally-associated protein that regulates wingless signaling in the embryonic epidermis J. Cell Biol. 146 1999 1303 1318 (Pubitemid 29477697)
    • (1999) Journal of Cell Biology , vol.146 , Issue.6 , pp. 1303-1318
    • McCartney, B.M.1    Dierick, H.A.2    Kirkpatrick, C.3    Moline, M.M.4    Baas, A.5    Peifer, M.6    Bejsovec, A.7
  • 36
    • 33745919542 scopus 로고    scopus 로고
    • Testing hypotheses for the functions of APC family proteins using null and truncation alleles in Drosophila
    • DOI 10.1242/dev.02398
    • B.M. McCartney, M.H. Price, R.L. Webb, M.A. Hayden, L.M. Holot, M. Zhou, A. Bejsovec, and M. Peifer Testing hypotheses for the functions of APC family proteins using null and truncation alleles in Drosophila Development 133 2006 2407 2418 (Pubitemid 44044561)
    • (2006) Development , vol.133 , Issue.12 , pp. 2407-2418
    • McCartney, B.M.1    Price, M.H.2    Webb, R.L.3    Hayden, M.A.4    Holot, L.M.5    Zhou, M.6    Bejsovec, A.7    Peifer, M.8
  • 38
    • 34548484336 scopus 로고    scopus 로고
    • Release of autoinhibition of ASEF by APC leads to CDC42 activation and tumor suppression
    • DOI 10.1038/nsmb1290, PII NSMB1290
    • N. Mitin, L. Betts, M.E. Yohe, C.J. Der, J. Sondek, and K.L. Rossman Release of autoinhibition of ASEF by APC leads to CDC42 activation and tumor suppression Nat. Struct. Mol. Biol. 14 2007 814 823 (Pubitemid 47373836)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.9 , pp. 814-823
    • Mitin, N.1    Betts, L.2    Yohe, M.E.3    Der, C.J.4    Sondek, J.5    Rossman, K.L.6
  • 41
    • 0028987249 scopus 로고
    • Regulation of intracellular β-catenin levels by the adenomatous polyposis coli (APC) tumor-suppressor protein
    • S. Munemitsu, I. Albert, B. Souza, B. Rubinfeld, and P. Polakis Regulation of intracellular β-catenin levels by the adenomatous polyposis coli (APC) tumor-suppressor protein Proc. Natl. Acad. Sci. USA 92 1995 3046 3050
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3046-3050
    • Munemitsu, S.1    Albert, I.2    Souza, B.3    Rubinfeld, B.4    Polakis, P.5
  • 42
    • 0031813650 scopus 로고    scopus 로고
    • Axin, an inhibitor of the Wnt signalling pathway, interacts with β- catenin, GSK-3β and APC and reduces the β-catenin level
    • T. Nakamura, F. Hamada, T. Ishidate, K. Anai, K. Kawahara, K. Toyoshima, and T. Akiyama Axin, an inhibitor of the Wnt signalling pathway, interacts with β-catenin, GSK-3β and APC and reduces the β-catenin level Genes Cells 3 1998 395 403 (Pubitemid 28387083)
    • (1998) Genes to Cells , vol.3 , Issue.6 , pp. 395-403
    • Nakamura, T.1    Hamada, F.2    Ishidate, T.3    Anai, K.-I.4    Kawahara, K.5    Toyoshima, K.6    Akiyama, T.7
  • 44
    • 0029047954 scopus 로고
    • Loss of Apc heterozygosity and abnormal tissue building in nascent intestinal polyps in mice carrying a truncated Apc gene
    • M. Oshima, H. Oshima, K. Kitagawa, M. Kobayashi, C. Itakura, and M. Taketo Loss of Apc heterozygosity and abnormal tissue building in nascent intestinal polyps in mice carrying a truncated Apc gene Proc. Natl. Acad. Sci. USA 92 1995 4482 4486
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4482-4486
    • Oshima, M.1    Oshima, H.2    Kitagawa, K.3    Kobayashi, M.4    Itakura, C.5    Taketo, M.6
  • 45
    • 0031005156 scopus 로고    scopus 로고
    • Morphological and molecular processes of polyp formation in Apc(Δ716) knockout mice
    • H. Oshima, M. Oshima, M. Kobayashi, M. Tsutsumi, and M.M. Taketo Morphological and molecular processes of polyp formation in Apc(delta716) knockout mice Cancer Res. 57 1997 1644 1649 (Pubitemid 27199651)
    • (1997) Cancer Research , vol.57 , Issue.9 , pp. 1644-1649
    • Oshima, H.1    Oshima, M.2    Kobayashi, M.3    Tsutsumi, M.4    Taketo, M.M.5
  • 46
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 47
    • 33947712084 scopus 로고    scopus 로고
    • The RNA-binding protein Sam68 modulates the alternative splicing of Bcl-x
    • DOI 10.1083/jcb.200701005
    • M.P. Paronetto, T. Achsel, A. Massiello, C.E. Chalfant, and C. Sette The RNA-binding protein Sam68 modulates the alternative splicing of Bcl-x J. Cell Biol. 176 2007 929 939 (Pubitemid 46506967)
    • (2007) Journal of Cell Biology , vol.176 , Issue.7 , pp. 929-939
    • Paronetto, M.P.1    Achsel, T.2    Massiello, A.3    Chalfant, C.E.4    Sette, C.5
  • 48
    • 0028266975 scopus 로고
    • A repeating amino acid motif shared by proteins with diverse cellular roles
    • DOI 10.1016/0092-8674(94)90353-0
    • M. Peifer, S. Berg, and A.B. Reynolds A repeating amino acid motif shared by proteins with diverse cellular roles Cell 76 1994 789 791 (Pubitemid 24085316)
    • (1994) Cell , vol.76 , Issue.5 , pp. 789-791
    • Peifer, M.1    Berg, S.2    Reynolds, A.B.3
  • 49
    • 0028957642 scopus 로고
    • Mutations in the APC gene and their implications for protein structure and function
    • P. Polakis Mutations in the APC gene and their implications for protein structure and function Curr. Opin. Genet. Dev. 5 1995 66 71
    • (1995) Curr. Opin. Genet. Dev. , vol.5 , pp. 66-71
    • Polakis, P.1
  • 51
    • 0028947757 scopus 로고
    • Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C γ-1
    • S. Richard, D. Yu, K.J. Blumer, D. Hausladen, M.W. Olszowy, P.A. Connelly, and A.S. Shaw Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C γ-1 Mol. Cell. Biol. 15 1995 186 197
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 186-197
    • Richard, S.1    Yu, D.2    Blumer, K.J.3    Hausladen, D.4    Olszowy, M.W.5    Connelly, P.A.6    Shaw, A.S.7
  • 54
    • 0033605639 scopus 로고    scopus 로고
    • Regulation of β-catenin signaling by the B56 subunit of protein phosphatase 2A
    • J.M. Seeling, J.R. Miller, R. Gil, R.T. Moon, R. White, and D.M. Virshup Regulation of β-catenin signaling by the B56 subunit of protein phosphatase 2A Science 283 1999 2089 2091
    • (1999) Science , vol.283 , pp. 2089-2091
    • Seeling, J.M.1    Miller, J.R.2    Gil, R.3    Moon, R.T.4    White, R.5    Virshup, D.M.6
  • 57
    • 0027756014 scopus 로고
    • Association of the APC tumor suppressor protein with catenins
    • L.K. Su, B. Vogelstein, and K.W. Kinzler Association of the APC tumor suppressor protein with catenins Science 262 1993 1734 1737 (Pubitemid 24030097)
    • (1993) Science , vol.262 , Issue.5140 , pp. 1734-1737
    • Su, L.-K.1    Vogelstein, B.2    Kinzler, K.W.3
  • 58
    • 78650882204 scopus 로고    scopus 로고
    • Biochemical and structural characterization of β-catenin interactions with nonphosphorylated and CK2-phosphorylated Lef-1
    • J. Sun, and W.I. Weis Biochemical and structural characterization of β-catenin interactions with nonphosphorylated and CK2-phosphorylated Lef-1 J. Mol. Biol. 405 2011 519 530
    • (2011) J. Mol. Biol. , vol.405 , pp. 519-530
    • Sun, J.1    Weis, W.I.2
  • 59
    • 0028329195 scopus 로고
    • An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis
    • DOI 10.1038/368867a0
    • S.J. Taylor, and D. Shalloway An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis Nature 368 1994 867 871 (Pubitemid 24137753)
    • (1994) Nature , vol.368 , Issue.6474 , pp. 867-871
    • Taylor, S.J.1    Shalloway, D.2
  • 62
    • 10644281068 scopus 로고    scopus 로고
    • Interaction with IQGAP1 links APC to Rac1, Cdc42, and actin filaments during cell polarization and migration
    • DOI 10.1016/j.devcel.2004.10.017, PII S153458070400382X
    • T. Watanabe, S. Wang, J. Noritake, K. Sato, M. Fukata, M. Takefuji, M. Nakagawa, N. Izumi, T. Akiyama, and K. Kaibuchi Interaction with IQGAP1 links APC to Rac1, Cdc42, and actin filaments during cell polarization and migration Dev. Cell 7 2004 871 883 (Pubitemid 39654731)
    • (2004) Developmental Cell , vol.7 , Issue.6 , pp. 871-883
    • Watanabe, T.1    Wang, S.2    Noritake, J.3    Sato, K.4    Fukata, M.5    Takefuji, M.6    Nakagawa, M.7    Izumi, N.8    Akiyama, T.9    Kaibuchi, K.10
  • 63
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • DOI 10.1016/0003-2697(89)90213-3
    • T. Wiseman, S. Williston, J.F. Brandts, and L.N. Lin Rapid measurement of binding constants and heats of binding using a new titration calorimeter Anal. Biochem. 179 1989 131 137 (Pubitemid 19149635)
    • (1989) Analytical Biochemistry , vol.179 , Issue.1 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.-N.4
  • 64
    • 0035726850 scopus 로고    scopus 로고
    • Detection of sequence variations in the adenomatous polyposis coli (APC) gene using denaturing high-performance liquid chromatography
    • DOI 10.1089/109065701753617408
    • G. Wu, W. Wu, M. Hegde, M. Fawkner, B. Chong, D. Love, L.K. Su, P. Lynch, K. Snow, and C.S. Richards Detection of sequence variations in the adenomatous polyposis coli (APC) gene using denaturing high-performance liquid chromatography Genet. Test. 5 2001 281 290 (Pubitemid 34258403)
    • (2001) Genetic Testing , vol.5 , Issue.4 , pp. 281-290
    • Wu, G.1    Wu, W.2    Hegde, M.3    Fawkner, M.4    Chong, B.5    Love, D.6    Su, L.-K.7    Lynch, P.8    Snow, K.9    Richards, C.S.10
  • 65
    • 4344684495 scopus 로고    scopus 로고
    • Crystal structure of a β-catenin/APC complex reveals a critical role for APC phosphorylation in APC function
    • DOI 10.1016/j.molcel.2004.08.001, PII S1097276504004460
    • Y. Xing, W.K. Clements, I. Le Trong, T.R. Hinds, R. Stenkamp, D. Kimelman, and W. Xu Crystal structure of a β-catenin/APC complex reveals a critical role for APC phosphorylation in APC function Mol. Cell 15 2004 523 533 (Pubitemid 39141780)
    • (2004) Molecular Cell , vol.15 , Issue.4 , pp. 523-533
    • Xing, Y.1    Clements, W.K.2    Le Trong, I.3    Hinds, T.R.4    Stenkamp, R.5    Kimelman, D.6    Xu, W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.