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Volumn 10, Issue , 2011, Pages

Messing up disorder: How do missense mutations in the tumor suppressor protein APC lead to cancer?

Author keywords

[No Author keywords available]

Indexed keywords

APC PROTEIN; WNT PROTEIN;

EID: 80052028694     PISSN: None     EISSN: 14764598     Source Type: Journal    
DOI: 10.1186/1476-4598-10-101     Document Type: Review
Times cited : (140)

References (71)
  • 1
    • 41549117418 scopus 로고    scopus 로고
    • Cell regulation by the Apc protein Apc as master regulator of epithelia
    • 10.1016/j.ceb.2008.02.001, 18359618
    • McCartney BM, Nathke IS. Cell regulation by the Apc protein Apc as master regulator of epithelia. Curr Opin Cell Biol 2008, 20:186-193. 10.1016/j.ceb.2008.02.001, 18359618.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 186-193
    • McCartney, B.M.1    Nathke, I.S.2
  • 2
    • 8444251784 scopus 로고    scopus 로고
    • The Wnt signaling pathway in development and disease
    • 10.1146/annurev.cellbio.20.010403.113126, 15473860
    • Logan CY, Nusse R. The Wnt signaling pathway in development and disease. Annu Rev Cell Dev Biol 2004, 20:781-810. 10.1146/annurev.cellbio.20.010403.113126, 15473860.
    • (2004) Annu Rev Cell Dev Biol , vol.20 , pp. 781-810
    • Logan, C.Y.1    Nusse, R.2
  • 3
    • 33746808398 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling in development and disease
    • 10.1016/j.cell.2006.10.018, 17081971
    • Clevers H. Wnt/beta-catenin signaling in development and disease. Cell 2006, 127:469-480. 10.1016/j.cell.2006.10.018, 17081971.
    • (2006) Cell , vol.127 , pp. 469-480
    • Clevers, H.1
  • 4
    • 35648988947 scopus 로고    scopus 로고
    • Adenomatous polyposis coli (APC): a multi-functional tumor suppressor gene
    • 10.1242/jcs.03485, 17881494
    • Aoki K, Taketo MM. Adenomatous polyposis coli (APC): a multi-functional tumor suppressor gene. J Cell Sci 2007, 120:3327-3335. 10.1242/jcs.03485, 17881494.
    • (2007) J Cell Sci , vol.120 , pp. 3327-3335
    • Aoki, K.1    Taketo, M.M.2
  • 5
    • 77954422924 scopus 로고    scopus 로고
    • Adenomatous polyposis coli protein nucleates actin assembly and synergizes with the formin mDia1
    • 10.1083/jcb.201001016, 2894447, 20566685
    • Okada K, Bartolini F, Deaconescu AM, Moseley JB, Dogic Z, Grigorieff N, Gundersen GG, Goode BL. Adenomatous polyposis coli protein nucleates actin assembly and synergizes with the formin mDia1. J Cell Biol 2010, 189:1087-1096. 10.1083/jcb.201001016, 2894447, 20566685.
    • (2010) J Cell Biol , vol.189 , pp. 1087-1096
    • Okada, K.1    Bartolini, F.2    Deaconescu, A.M.3    Moseley, J.B.4    Dogic, Z.5    Grigorieff, N.6    Gundersen, G.G.7    Goode, B.L.8
  • 6
    • 0037440378 scopus 로고    scopus 로고
    • Requirement for tumor suppressor Apc in the morphogenesis of anterior and ventral mouse embryo
    • 10.1016/S0012-1606(02)00020-9, 12645927
    • Ishikawa TO, Tamai Y, Li Q, Oshima M, Taketo MM. Requirement for tumor suppressor Apc in the morphogenesis of anterior and ventral mouse embryo. Dev Biol 2003, 253:230-246. 10.1016/S0012-1606(02)00020-9, 12645927.
    • (2003) Dev Biol , vol.253 , pp. 230-246
    • Ishikawa, T.O.1    Tamai, Y.2    Li, Q.3    Oshima, M.4    Taketo, M.M.5
  • 8
    • 0029047954 scopus 로고
    • Loss of Apc heterozygosity and abnormal tissue building in nascent intestinal polyps in mice carrying a truncated Apc gene
    • 10.1073/pnas.92.10.4482, 41968, 7753829
    • Oshima M, Oshima H, Kitagawa K, Kobayashi M, Itakura C, Taketo M. Loss of Apc heterozygosity and abnormal tissue building in nascent intestinal polyps in mice carrying a truncated Apc gene. Proc Natl Acad Sci USA 1995, 92:4482-4486. 10.1073/pnas.92.10.4482, 41968, 7753829.
    • (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
  • 9
    • 0030871048 scopus 로고    scopus 로고
    • Loss of beta-catenin regulation by the APC tumor suppressor protein correlates with loss of structure due to common somatic mutations of the gene
    • Rubinfeld B, Albert I, Porfiri E, Munemitsu S, Polakis P. Loss of beta-catenin regulation by the APC tumor suppressor protein correlates with loss of structure due to common somatic mutations of the gene. Cancer Res 1997, 57:4624-4630.
    • (1997) Cancer Res , vol.57 , pp. 4624-4630
    • Rubinfeld, B.1    Albert, I.2    Porfiri, E.3    Munemitsu, S.4    Polakis, P.5
  • 10
    • 0028987249 scopus 로고
    • Regulation of intracellular beta-catenin levels by the adenomatous polyposis coli (APC) tumor-suppressor protein
    • 10.1073/pnas.92.7.3046, 42356, 7708772
    • Munemitsu S, Albert I, Souza B, Rubinfeld B, Polakis P. Regulation of intracellular beta-catenin levels by the adenomatous polyposis coli (APC) tumor-suppressor protein. Proc Natl Acad Sci USA 1995, 92:3046-3050. 10.1073/pnas.92.7.3046, 42356, 7708772.
    • (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
  • 12
    • 0027756014 scopus 로고
    • Association of the APC tumor suppressor protein with catenins
    • 10.1126/science.8259519, 8259519
    • Su LK, Vogelstein B, Kinzler KW. Association of the APC tumor suppressor protein with catenins. Science 1993, 262:1734-1737. 10.1126/science.8259519, 8259519.
    • (1993) Science , vol.262 , pp. 1734-1737
    • Su, L.K.1    Vogelstein, B.2    Kinzler, K.W.3
  • 13
    • 0035890060 scopus 로고    scopus 로고
    • Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex
    • 10.1093/emboj/20.22.6203, 125720, 11707392
    • Eklof Spink K, Fridman SG, Weis WI. Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex. EMBO J 2001, 20:6203-6212. 10.1093/emboj/20.22.6203, 125720, 11707392.
    • (2001) EMBO J , vol.20 , pp. 6203-6212
    • Eklof Spink, K.1    Fridman, S.G.2    Weis, W.I.3
  • 14
    • 7744246985 scopus 로고    scopus 로고
    • The APC tumor suppressor binds to C-terminal binding protein to divert nuclear beta-catenin from TCF
    • 10.1016/j.devcel.2004.08.022, 15525529
    • Hamada F, Bienz M. The APC tumor suppressor binds to C-terminal binding protein to divert nuclear beta-catenin from TCF. Dev Cell 2004, 7:677-685. 10.1016/j.devcel.2004.08.022, 15525529.
    • (2004) Dev Cell , vol.7 , pp. 677-685
    • Hamada, F.1    Bienz, M.2
  • 15
    • 33644763022 scopus 로고    scopus 로고
    • The APC tumor suppressor counteracts beta-catenin activation and H3K4 methylation at Wnt target genes
    • 10.1101/gad.1385806, 1410807, 16510874
    • Sierra J, Yoshida T, Joazeiro CA, Jones KA. The APC tumor suppressor counteracts beta-catenin activation and H3K4 methylation at Wnt target genes. Genes Dev 2006, 20:586-600. 10.1101/gad.1385806, 1410807, 16510874.
    • (2006) Genes Dev , vol.20 , pp. 586-600
    • Sierra, J.1    Yoshida, T.2    Joazeiro, C.A.3    Jones, K.A.4
  • 16
    • 80052258209 scopus 로고    scopus 로고
    • APC mutations in colorectal tumours from FAP patients are selected for CtBP-mediated oligomerization of truncated APC
    • Schneikert J, Brauburger K, Behrens J. APC mutations in colorectal tumours from FAP patients are selected for CtBP-mediated oligomerization of truncated APC. Hum Mol Genet 2011,
    • (2011) Hum Mol Genet
    • Schneikert, J.1    Brauburger, K.2    Behrens, J.3
  • 17
    • 0032562603 scopus 로고    scopus 로고
    • Functional interaction of an axin homolog, conductin, with beta-catenin, APC, and GSK3 beta
    • 10.1126/science.280.5363.596, 9554852
    • Behrens J, Jerchow BA, Wurtele M, Grimm J, Asbrand C, Wirtz R, Kuhl M, Wedlich D, Birchmeier W. Functional interaction of an axin homolog, conductin, with beta-catenin, APC, and GSK3 beta. Science 1998, 280:596-599. 10.1126/science.280.5363.596, 9554852.
    • (1998) Science , vol.280 , pp. 596-599
    • Behrens, J.1    Jerchow, B.A.2    Wurtele, M.3    Grimm, J.4    Asbrand, C.5    Wirtz, R.6    Kuhl, M.7    Wedlich, D.8    Birchmeier, W.9
  • 18
    • 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 beta-catenin
    • 10.1074/jbc.273.18.10823, 9556553
    • Kishida S, Yamamoto H, Ikeda S, Kishida M, Sakamoto I, Koyama S, Kikuchi A. Axin, a negative regulator of the wnt signaling pathway, directly interacts with adenomatous polyposis coli and regulates the stabilization of beta-catenin. J Biol Chem 1998, 273:10823-10826. 10.1074/jbc.273.18.10823, 9556553.
    • (1998) J Biol Chem , vol.273 , pp. 10823-10826
    • Kishida, S.1    Yamamoto, H.2    Ikeda, S.3    Kishida, M.4    Sakamoto, I.5    Koyama, S.6    Kikuchi, A.7
  • 19
    • 0031813650 scopus 로고    scopus 로고
    • Axin, an inhibitor of the Wnt signalling pathway, interacts with beta-catenin, GSK-3 beta and APC and reduces the beta-catenin level
    • 10.1046/j.1365-2443.1998.00198.x, 9734785
    • Nakamura T, Hamada F, Ishidate T, Anai K, Kawahara K, Toyoshima K, Akiyama T. Axin, an inhibitor of the Wnt signalling pathway, interacts with beta-catenin, GSK-3 beta and APC and reduces the beta-catenin level. Genes Cells 1998, 3:395-403. 10.1046/j.1365-2443.1998.00198.x, 9734785.
    • (1998) Genes Cells , vol.3 , pp. 395-403
    • Nakamura, T.1    Hamada, F.2    Ishidate, T.3    Anai, K.4    Kawahara, K.5    Toyoshima, K.6    Akiyama, T.7
  • 20
    • 4344684495 scopus 로고    scopus 로고
    • Crystal structure of a beta-catenin/APC complex reveals a critical role for APC phosphorylation in APC function
    • 10.1016/j.molcel.2004.08.001, 15327769
    • Xing Y, Clements WK, Le Trong I, Hinds TR, Stenkamp R, Kimelman D, Xu W. Crystal structure of a beta-catenin/APC complex reveals a critical role for APC phosphorylation in APC function. Mol Cell 2004, 15:523-533. 10.1016/j.molcel.2004.08.001, 15327769.
    • (2004) Mol Cell , vol.15 , 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
  • 21
    • 4344562126 scopus 로고    scopus 로고
    • Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation
    • 10.1016/j.molcel.2004.08.010, 15327768
    • Ha NC, Tonozuka T, Stamos JL, Choi HJ, Weis WI. Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation. Mol Cell 2004, 15:511-521. 10.1016/j.molcel.2004.08.010, 15327768.
    • (2004) Mol Cell , vol.15 , pp. 511-521
    • Ha, N.C.1    Tonozuka, T.2    Stamos, J.L.3    Choi, H.J.4    Weis, W.I.5
  • 22
    • 0033635606 scopus 로고    scopus 로고
    • Crystal structure of a beta-catenin/Tcf complex
    • 10.1016/S0092-8674(00)00192-6, 11136974
    • Graham TA, Weaver C, Mao F, Kimelman D, Xu W. Crystal structure of a beta-catenin/Tcf complex. Cell 2000, 103:885-896. 10.1016/S0092-8674(00)00192-6, 11136974.
    • (2000) Cell , vol.103 , pp. 885-896
    • Graham, T.A.1    Weaver, C.2    Mao, F.3    Kimelman, D.4    Xu, W.5
  • 23
    • 0035805117 scopus 로고    scopus 로고
    • The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin
    • 10.1016/S0092-8674(01)00330-0, 11348595
    • Huber AH, Weis WI. The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin. Cell 2001, 105:391-402. 10.1016/S0092-8674(01)00330-0, 11348595.
    • (2001) Cell , vol.105 , pp. 391-402
    • Huber, A.H.1    Weis, W.I.2
  • 24
    • 33745276261 scopus 로고    scopus 로고
    • The Third 20 Amino Acid Repeat Is the Tightest Binding Site of APC for β-Catenin
    • 10.1016/j.jmb.2006.04.064, 16753179
    • Liu J, Xing Y, Hinds TR, Zheng J, Xu W. The Third 20 Amino Acid Repeat Is the Tightest Binding Site of APC for β-Catenin. Journal of Molecular Biology 2006, 360:133-144. 10.1016/j.jmb.2006.04.064, 16753179.
    • (2006) Journal of Molecular Biology , vol.360 , pp. 133-144
    • Liu, J.1    Xing, Y.2    Hinds, T.R.3    Zheng, J.4    Xu, W.5
  • 25
    • 0344442773 scopus 로고    scopus 로고
    • Crystal structure of a β-catenin/Axin complex suggests a mechanism for the β-catenin destruction complex
    • 10.1101/gad.1142603, 21877293
    • Xing Y, Clements WK, Kimelman D, Xu W. Crystal structure of a β-catenin/Axin complex suggests a mechanism for the β-catenin destruction complex. Genes & Development 2003, 17:2753-2764. 10.1101/gad.1142603, 21877293.
    • (2003) Genes & Development , vol.17 , pp. 2753-2764
    • Xing, Y.1    Clements, W.K.2    Kimelman, D.3    Xu, W.4
  • 26
    • 56849086074 scopus 로고    scopus 로고
    • APC is essential for targeting phosphorylated beta-catenin to the SCFbeta-TrCP ubiquitin ligase
    • 10.1016/j.molcel.2008.10.023, 19061640
    • Su Y, Fu C, Ishikawa S, Stella A, Kojima M, Shitoh K, Schreiber EM, Day BW, Liu B. APC is essential for targeting phosphorylated beta-catenin to the SCFbeta-TrCP ubiquitin ligase. Mol Cell 2008, 32:652-661. 10.1016/j.molcel.2008.10.023, 19061640.
    • (2008) Mol Cell , vol.32 , pp. 652-661
    • Su, Y.1    Fu, C.2    Ishikawa, S.3    Stella, A.4    Kojima, M.5    Shitoh, K.6    Schreiber, E.M.7    Day, B.W.8    Liu, B.9
  • 27
    • 34147192003 scopus 로고    scopus 로고
    • Axin-independent phosphorylation of APC controls [beta]-catenin signaling via cytoplasmic retention of [beta]-catenin
    • 10.1016/j.bbrc.2007.03.117, 17418091
    • Seo E, Jho E. Axin-independent phosphorylation of APC controls [beta]-catenin signaling via cytoplasmic retention of [beta]-catenin. Biochemical and Biophysical Research Communications 2007, 357:81-86. 10.1016/j.bbrc.2007.03.117, 17418091.
    • (2007) Biochemical and Biophysical Research Communications , vol.357 , pp. 81-86
    • Seo, E.1    Jho, E.2
  • 28
    • 79957597124 scopus 로고    scopus 로고
    • Deconstructing the sscatenin destruction complex: mechanistic roles for the tumor suppressor APC in regulating Wnt signaling
    • 10.1091/mbc.E10-11-0871, 3103401, 21471006
    • Roberts DM, Pronobis MI, Poulton JS, Waldmann JD, Stephenson EM, Hanna S, Peifer M. Deconstructing the sscatenin destruction complex: mechanistic roles for the tumor suppressor APC in regulating Wnt signaling. Mol Biol Cell 2011, 22:1845-1863. 10.1091/mbc.E10-11-0871, 3103401, 21471006.
    • (2011) Mol Biol Cell , vol.22 , pp. 1845-1863
    • Roberts, D.M.1    Pronobis, M.I.2    Poulton, J.S.3    Waldmann, J.D.4    Stephenson, E.M.5    Hanna, S.6    Peifer, M.7
  • 29
    • 58049196841 scopus 로고    scopus 로고
    • Beta-catenin degradation mediated by the CID domain of APC provides a model for the selection of APC mutations in colorectal, desmoid and duodenal tumours
    • Kohler EM, Chandra SH, Behrens J, Schneikert J. Beta-catenin degradation mediated by the CID domain of APC provides a model for the selection of APC mutations in colorectal, desmoid and duodenal tumours. Hum Mol Genet 2009, 18:213-226.
    • (2009) Hum Mol Genet , vol.18 , pp. 213-226
    • Kohler, E.M.1    Chandra, S.H.2    Behrens, J.3    Schneikert, J.4
  • 30
    • 3242885293 scopus 로고    scopus 로고
    • The PredictProtein server
    • 10.1093/nar/gkh377, 441515, 15215403
    • Rost B, Yachdav G, Liu J. The PredictProtein server. Nucleic Acids Res 2004, 32:W321-326. 10.1093/nar/gkh377, 441515, 15215403.
    • (2004) Nucleic Acids Res , vol.32
    • Rost, B.1    Yachdav, G.2    Liu, J.3
  • 31
    • 30344485673 scopus 로고    scopus 로고
    • Exploiting heterogeneous sequence properties improves prediction of protein disorder
    • Obradovic Z, Peng K, Vucetic S, Radivojac P, Dunker AK. Exploiting heterogeneous sequence properties improves prediction of protein disorder. Proteins 2005, 61(Suppl 7):176-182.
    • (2005) Proteins , vol.61 , Issue.SUPPL. 7 , pp. 176-182
    • Obradovic, Z.1    Peng, K.2    Vucetic, S.3    Radivojac, P.4    Dunker, A.K.5
  • 32
    • 18744405418 scopus 로고    scopus 로고
    • Prediction of unfolded segments in a protein sequence based on amino acid composition
    • 10.1093/bioinformatics/bti266, 15657106
    • Coeytaux K, Poupon A. Prediction of unfolded segments in a protein sequence based on amino acid composition. Bioinformatics 2005, 21:1891-1900. 10.1093/bioinformatics/bti266, 15657106.
    • (2005) Bioinformatics , vol.21 , pp. 1891-1900
    • Coeytaux, K.1    Poupon, A.2
  • 33
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • 10.1093/nar/gkg519, 169197, 12824398
    • Linding R, Russell RB, Neduva V, Gibson TJ. GlobPlot: Exploring protein sequences for globularity and disorder. Nucleic Acids Res 2003, 31:3701-3708. 10.1093/nar/gkg519, 169197, 12824398.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 35
    • 20744437001 scopus 로고    scopus 로고
    • RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins
    • 10.1093/bioinformatics/bti534, 15947016
    • Yang ZR, Thomson R, McNeil P, Esnouf RM. RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins. Bioinformatics 2005, 21:3369-3376. 10.1093/bioinformatics/bti534, 15947016.
    • (2005) Bioinformatics , vol.21 , pp. 3369-3376
    • Yang, Z.R.1    Thomson, R.2    McNeil, P.3    Esnouf, R.M.4
  • 36
    • 40049101403 scopus 로고    scopus 로고
    • Crystal structure of a full-length beta-catenin
    • 10.1016/j.str.2007.12.021, 18334222
    • Xing Y, Takemaru K, Liu J, Berndt JD, Zheng JJ, Moon RT, Xu W. Crystal structure of a full-length beta-catenin. Structure 2008, 16:478-487. 10.1016/j.str.2007.12.021, 18334222.
    • (2008) Structure , vol.16 , pp. 478-487
    • Xing, Y.1    Takemaru, K.2    Liu, J.3    Berndt, J.D.4    Zheng, J.J.5    Moon, R.T.6    Xu, W.7
  • 38
    • 20444490811 scopus 로고    scopus 로고
    • Tumor-associated NH2-terminal fragments are the most stable part of the adenomatous polyposis coli protein and can be regulated by interactions with COOH-terminal domains
    • 10.1158/0008-5472.CAN-04-4609, 15958564
    • Li Z, Nathke IS. Tumor-associated NH2-terminal fragments are the most stable part of the adenomatous polyposis coli protein and can be regulated by interactions with COOH-terminal domains. Cancer Res 2005, 65:5195-5204. 10.1158/0008-5472.CAN-04-4609, 15958564.
    • (2005) Cancer Res , vol.65 , pp. 5195-5204
    • Li, Z.1    Nathke, I.S.2
  • 39
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: introducing the D2 concept
    • 10.1146/annurev.biophys.37.032807.125924, 18573080
    • Uversky VN, Oldfield CJ, Dunker AK. Intrinsically disordered proteins in human diseases: introducing the D2 concept. Annu Rev Biophys 2008, 37:215-246. 10.1146/annurev.biophys.37.032807.125924, 18573080.
    • (2008) Annu Rev Biophys , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 40
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life
    • 10.1016/j.jmb.2004.02.002, 15019783
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT. Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life. Journal of Molecular Biology 2004, 337:635-645. 10.1016/j.jmb.2004.02.002, 15019783.
    • (2004) Journal of Molecular Biology , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 41
    • 13644257647 scopus 로고    scopus 로고
    • Comparing and combining predictors of mostly disordered proteins
    • 10.1021/bi047993o, 15697224
    • Oldfield CJ, Cheng Y, Cortese MS, Brown CJ, Uversky VN, Dunker AK. Comparing and combining predictors of mostly disordered proteins. Biochemistry 2005, 44:1989-2000. 10.1021/bi047993o, 15697224.
    • (2005) Biochemistry , vol.44 , pp. 1989-2000
    • Oldfield, C.J.1    Cheng, Y.2    Cortese, M.S.3    Brown, C.J.4    Uversky, V.N.5    Dunker, A.K.6
  • 42
    • 50049097448 scopus 로고    scopus 로고
    • Intrinsic disorder in scaffold proteins: Getting more from less
    • 10.1016/j.pbiomolbio.2008.05.007, 2671330, 18619997
    • Cortese MS, Uversky VN, Keith Dunker A. Intrinsic disorder in scaffold proteins: Getting more from less. Progress in Biophysics and Molecular Biology 2008, 98:85-106. 10.1016/j.pbiomolbio.2008.05.007, 2671330, 18619997.
    • (2008) Progress in Biophysics and Molecular Biology , vol.98 , pp. 85-106
    • Cortese, M.S.1    Uversky, V.N.2    Keith Dunker, A.3
  • 45
    • 62849122802 scopus 로고    scopus 로고
    • Interactions between Casein kinase Iepsilon (CKIepsilon) and two substrates from disparate signaling pathways reveal mechanisms for substrate-kinase specificity
    • 10.1371/journal.pone.0004766, 2651596, 19274088
    • Dahlberg CL, Nguyen EZ, Goodlett D, Kimelman D. Interactions between Casein kinase Iepsilon (CKIepsilon) and two substrates from disparate signaling pathways reveal mechanisms for substrate-kinase specificity. PLoS ONE 2009, 4:e4766. 10.1371/journal.pone.0004766, 2651596, 19274088.
    • (2009) PLoS ONE , vol.4
    • Dahlberg, C.L.1    Nguyen, E.Z.2    Goodlett, D.3    Kimelman, D.4
  • 46
    • 0037181484 scopus 로고    scopus 로고
    • The chicken-egg scenario of protein folding revisited
    • 10.1016/S0014-5793(02)02441-9, 11943199
    • Uversky VN, Fink AL. The chicken-egg scenario of protein folding revisited. FEBS Lett 2002, 515:79-83. 10.1016/S0014-5793(02)02441-9, 11943199.
    • (2002) FEBS Lett , vol.515 , pp. 79-83
    • Uversky, V.N.1    Fink, A.L.2
  • 48
    • 0003751511 scopus 로고
    • The Behavior of Biological Macromolecules
    • (Eds.)
    • Cantor CR, Schimmel PR, . (Eds.) The Behavior of Biological Macromolecules. 1980, (Eds.).
    • (1980)
    • Cantor, C.R.1    Schimmel, P.R.2
  • 49
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • 10.1038/nrm1589, 15738986
    • Dyson HJ, Wright PE. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 2005, 6:197-208. 10.1038/nrm1589, 15738986.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 50
    • 77956332835 scopus 로고    scopus 로고
    • Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators
    • 10.1016/j.str.2010.05.015, 20826336
    • Marsh JA, Dancheck B, Ragusa MJ, Allaire M, Forman-Kay JD, Peti W. Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators. Structure 2010, 18:1094-1103. 10.1016/j.str.2010.05.015, 20826336.
    • (2010) Structure , vol.18 , pp. 1094-1103
    • Marsh, J.A.1    Dancheck, B.2    Ragusa, M.J.3    Allaire, M.4    Forman-Kay, J.D.5    Peti, W.6
  • 51
    • 76649114676 scopus 로고    scopus 로고
    • Protein dynamics and conformational disorder in molecular recognition
    • Mittag T, Kay LE, Forman-Kay JD. Protein dynamics and conformational disorder in molecular recognition. J Mol Recognit 2010, 23:105-116.
    • (2010) J Mol Recognit , vol.23 , pp. 105-116
    • Mittag, T.1    Kay, L.E.2    Forman-Kay, J.D.3
  • 52
    • 33846671062 scopus 로고    scopus 로고
    • Tuning bulk electrostatics to regulate protein function
    • 10.1016/j.cell.2007.01.018, 17289565
    • Serber Z, Ferrell JE. Tuning bulk electrostatics to regulate protein function. Cell 2007, 128:441-444. 10.1016/j.cell.2007.01.018, 17289565.
    • (2007) Cell , vol.128 , pp. 441-444
    • Serber, Z.1    Ferrell, J.E.2
  • 53
    • 0034657187 scopus 로고    scopus 로고
    • Structural basis of the Axin-adenomatous polyposis coli interaction
    • 10.1093/emboj/19.10.2270, 384355, 10811618
    • Spink KE, Polakis P, Weis WI. Structural basis of the Axin-adenomatous polyposis coli interaction. EMBO Journal 2000, 19:2270-2279. 10.1093/emboj/19.10.2270, 384355, 10811618.
    • (2000) EMBO Journal , vol.19 , pp. 2270-2279
    • Spink, K.E.1    Polakis, P.2    Weis, W.I.3
  • 55
    • 68049093193 scopus 로고    scopus 로고
    • Direct Observation of the Dynamic Process Underlying Allosteric Signal Transmission
    • 10.1021/ja809947w, 19203263
    • Bruschweiler S, Schanda P, Kloiber K, Brutscher B, Kontaxis G, Konrat R, Tollinger M. Direct Observation of the Dynamic Process Underlying Allosteric Signal Transmission. J Am Chem Soc 2009, 131:3063-3068. 10.1021/ja809947w, 19203263.
    • (2009) J Am Chem Soc , vol.131 , pp. 3063-3068
    • Bruschweiler, S.1    Schanda, P.2    Kloiber, K.3    Brutscher, B.4    Kontaxis, G.5    Konrat, R.6    Tollinger, M.7
  • 56
    • 33845373278 scopus 로고    scopus 로고
    • Colorectal cancer and genetic alterations in the Wnt pathway
    • 10.1038/sj.onc.1210059, 17143297
    • Segditsas S, Tomlinson I. Colorectal cancer and genetic alterations in the Wnt pathway. Oncogene 2006, 25:7531-7537. 10.1038/sj.onc.1210059, 17143297.
    • (2006) Oncogene , vol.25 , pp. 7531-7537
    • Segditsas, S.1    Tomlinson, I.2
  • 57
    • 0025938038 scopus 로고
    • Identification and characterization of the familial adenomatous polyposis coli gene
    • 10.1016/0092-8674(81)90021-0, 1651174
    • Groden J. Identification and characterization of the familial adenomatous polyposis coli gene. Cell 1991, 66:589-600. 10.1016/0092-8674(81)90021-0, 1651174.
    • (1991) Cell , vol.66 , pp. 589-600
    • Groden, J.1
  • 59
    • 25444443671 scopus 로고    scopus 로고
    • Rare Variant Hypothesis for Multifactorial Inheritance: Susceptibility to Colorectal Adenomas as a Model
    • 10.4161/cc.4.4.1591, 15753653
    • Fearnhead NS, Winney B, Bodmer WF. Rare Variant Hypothesis for Multifactorial Inheritance: Susceptibility to Colorectal Adenomas as a Model. Cell Cycle 2005, 4:521-525. 10.4161/cc.4.4.1591, 15753653.
    • (2005) Cell Cycle , vol.4 , pp. 521-525
    • Fearnhead, N.S.1    Winney, B.2    Bodmer, W.F.3
  • 60
    • 0030592517 scopus 로고    scopus 로고
    • Lessons from hereditary colorectal cancer
    • 10.1016/S0092-8674(00)81333-1, 8861899
    • Kinzler KW, Vogelstein B. Lessons from hereditary colorectal cancer. Cell 1996, 87:159-170. 10.1016/S0092-8674(00)81333-1, 8861899.
    • (1996) Cell , vol.87 , pp. 159-170
    • Kinzler, K.W.1    Vogelstein, B.2
  • 62
    • 0034902674 scopus 로고    scopus 로고
    • Disease model: familial adenomatous polyposis
    • 10.1016/S1471-4914(01)02050-0, 11516998
    • Fodde R, Smits R. Disease model: familial adenomatous polyposis. Trends in Molecular Medicine 2001, 7:369-373. 10.1016/S1471-4914(01)02050-0, 11516998.
    • (2001) Trends in Molecular Medicine , vol.7 , pp. 369-373
    • Fodde, R.1    Smits, R.2
  • 63
    • 5444233462 scopus 로고    scopus 로고
    • APC dosage effects in tumorigenesis and stem cell differentiation
    • 10.1387/ijdb.041807cg, 15349813
    • Gaspar C, Fodde R. APC dosage effects in tumorigenesis and stem cell differentiation. Int J Dev Biol 2004, 48:377-386. 10.1387/ijdb.041807cg, 15349813.
    • (2004) Int J Dev Biol , vol.48 , pp. 377-386
    • Gaspar, C.1    Fodde, R.2
  • 65
    • 58149383087 scopus 로고    scopus 로고
    • Somatic mutations of adenomatous polyposis coli gene and nuclear b-catenin accumulation have prognostic significance in invasive urothelial carcinomas: evidence for Wnt pathway implication
    • 10.1002/ijc.23917, 18844223
    • Kastritis E, Murray S, Kyriakou F, Horti M, Tamvakis N, Kavantzas N, Patsouris ES, Noni A, Legaki S, Dimopoulos MA, Bamias A. Somatic mutations of adenomatous polyposis coli gene and nuclear b-catenin accumulation have prognostic significance in invasive urothelial carcinomas: evidence for Wnt pathway implication. Int J Cancer 2009, 124:103-108. 10.1002/ijc.23917, 18844223.
    • (2009) Int J Cancer , vol.124 , pp. 103-108
    • Kastritis, E.1    Murray, S.2    Kyriakou, F.3    Horti, M.4    Tamvakis, N.5    Kavantzas, N.6    Patsouris, E.S.7    Noni, A.8    Legaki, S.9    Dimopoulos, M.A.10    Bamias, A.11
  • 68
    • 0029155035 scopus 로고
    • Helix design, prediction and stability
    • 10.1016/0958-1669(95)80066-2, 7579647
    • Munoz V, Serrano L. Helix design, prediction and stability. Curr Opin Biotechnol 1995, 6:382-386. 10.1016/0958-1669(95)80066-2, 7579647.
    • (1995) Curr Opin Biotechnol , vol.6 , pp. 382-386
    • Munoz, V.1    Serrano, L.2
  • 69
    • 35448947338 scopus 로고    scopus 로고
    • Chemical dissection of the APC Repeat 3 multistep phosphorylation by the concerted action of protein kinases CK1 and GSK3
    • 10.1021/bi701674z, 17910481
    • Ferrarese A, Marin O, Bustos VH, Venerando A, Antonelli M, Allende JE, Pinna LA. Chemical dissection of the APC Repeat 3 multistep phosphorylation by the concerted action of protein kinases CK1 and GSK3. Biochemistry 2007, 46:11902-11910. 10.1021/bi701674z, 17910481.
    • (2007) Biochemistry , vol.46 , pp. 11902-11910
    • Ferrarese, A.1    Marin, O.2    Bustos, V.H.3    Venerando, A.4    Antonelli, M.5    Allende, J.E.6    Pinna, L.A.7
  • 70
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • 10.1038/nature05858, 17522630
    • Sugase K, Dyson HJ, Wright PE. Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 2007, 447:1021-1025. 10.1038/nature05858, 17522630.
    • (2007) Nature , vol.447 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 71
    • 60649109828 scopus 로고    scopus 로고
    • Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms
    • 10.1039/b819720b, 19225609
    • Tsai CJ, Del Sol A, Nussinov R. Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms. Mol Biosyst 2009, 5:207-216. 10.1039/b819720b, 19225609.
    • (2009) Mol Biosyst , vol.5 , pp. 207-216
    • Tsai, C.J.1    Del Sol, A.2    Nussinov, R.3


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