메뉴 건너뛰기




Volumn 50, Issue 5, 2011, Pages 715-726

Structural characterization of partially disordered human Chibby: Insights into its function in the Wnt-signaling pathway

Author keywords

[No Author keywords available]

Indexed keywords

14-3-3 PROTEINS; BINDING STUDIES; CATENIN SIGNALING; COILED COIL; COILED-COIL STRUCTURE; CONSERVED PROTEINS; DIFFERENT MODES; DISORDERED PROTEINS; DISTINCT STRUCTURAL MODULES; EMBRYONIC DEVELOPMENT; HUMAN DISEASE; INTRACELLULAR DISTRIBUTION; ISOFORMS; LARGE-SCALE ANALYSIS; N-TERMINALS; NMR SPECTROSCOPY; PROTEIN COMPLEXES; PROTEIN INTERACTION; PROTEOMES; SELF-ASSOCIATIONS; SIGNALING PATHWAYS; STRUCTURAL CHARACTERIZATION; STRUCTURE-FUNCTION RELATIONSHIP; TARGET GENES; TERNARY COMPLEX; THYROID CANCERS; TISSUE REGENERATION; TRANSCRIPTIONAL ACTIVATIONS; WNT SIGNALING;

EID: 79952095538     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101236z     Document Type: Article
Times cited : (21)

References (80)
  • 1
    • 33746808398 scopus 로고    scopus 로고
    • Wnt/β-catenin signaling in development and disease
    • Clevers, H. (2006) Wnt/β-catenin signaling in development and disease. Cell 127, 469-480.
    • (2006) Cell , vol.127 , pp. 469-480
    • Clevers, H.1
  • 2
    • 8444251784 scopus 로고    scopus 로고
    • The Wnt signaling pathway in development and disease
    • DOI 10.1146/annurev.cellbio.20.010403.113126
    • Logan, C. Y., and Nusse, R. (2004) The Wnt signaling pathway in development and disease. Annu. Rev. Cell. Dev. Biol. 20, 781-810. (Pubitemid 39488658)
    • (2004) Annual Review of Cell and Developmental Biology , vol.20 , pp. 781-810
    • Logan, C.Y.1    Nusse, R.2
  • 3
    • 4344584730 scopus 로고    scopus 로고
    • WNT and β-catenin signalling: Diseases and therapies
    • DOI 10.1038/nrg1427
    • Moon, R. T., Kohn, A. D., De Ferrari, G. V., and Kaykas, A. (2004) WNT and β-catenin signalling: diseases and therapies. Nat. Rev. Genet. 5, 691-701. (Pubitemid 39150127)
    • (2004) Nature Reviews Genetics , vol.5 , Issue.9 , pp. 691-701
    • Moon, R.T.1    Kohn, A.D.2    De Ferrari, G.V.3    Kaykas, A.4
  • 4
    • 0033895709 scopus 로고    scopus 로고
    • Wnt signaling and cancer
    • Polakis, P. (2000) Wnt signaling and cancer. Genes Dev. 14, 1837-1851. (Pubitemid 30639518)
    • (2000) Genes and Development , vol.14 , Issue.15 , pp. 1837-1851
    • Polakis, P.1
  • 5
    • 33845351956 scopus 로고    scopus 로고
    • β-Catenin destruction complex: Insights and questions from a structural perspective
    • DOI 10.1038/sj.onc.1210055, PII 1210055
    • Kimelman, D., and Xu, W. (2006) β-catenin destruction complex: insights and questions from a structural perspective. Oncogene 25, 7482-7491. (Pubitemid 44885747)
    • (2006) Oncogene , vol.25 , Issue.57 , pp. 7482-7491
    • Kimelman, D.1    Xu, W.2
  • 6
    • 0030978351 scopus 로고    scopus 로고
    • β-catenin is a target for the ubiquitin-proteasome pathway
    • Aberle, H., Bauer, A., Stappert, J., Kispert, A., and Kemler, R. (1997) β-catenin is a target for the ubiquitin-proteasome pathway. EMBO J. 16, 3797-3804.
    • (1997) EMBO J. , vol.16 , pp. 3797-3804
    • Aberle, H.1    Bauer, A.2    Stappert, J.3    Kispert, A.4    Kemler, R.5
  • 7
    • 0029781509 scopus 로고    scopus 로고
    • Functional interaction of β-catenin with the transcription factor LEF- 1
    • DOI 10.1038/382638a0
    • Behrens, J., von Kries, J. P., Kuhl, M., Bruhn, L., Wedlich, D., Grosschedl, R., and Birchmeier, W. (1996) Functional interaction of β-catenin with the transcription factor LEF-1. Nature 382, 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
  • 8
    • 34447646653 scopus 로고    scopus 로고
    • Wnt signaling as a therapeutic target for cancer
    • DOI 10.1385/1-59745-208-4:63, Target Discovery and Validation Reviews and Protocols: Volume 2 Emerging Molecular Targetsand Treatment Options
    • Herbst, A., and Kolligs, F. T. (2007) Wnt signaling as a therapeutic target for cancer. Methods Mol. Biol. 361, 63-91. (Pubitemid 350183202)
    • (2007) Methods in Molecular Biology , vol.361 , pp. 63-91
    • Herbst, A.1    Kolligs, F.T.2
  • 9
    • 0242515751 scopus 로고    scopus 로고
    • Chibby, a nuclear β-catenin-associated antagonist of the Wnt/Wingless pathway
    • DOI 10.1038/nature01570
    • Takemaru, K., Yamaguchi, S., Lee, Y. S., Zhang, Y., Carthew, R. W., and Moon, R. T. (2003) Chibby, a nuclear β-catenin-associated antagonist of the Wnt/Wingless pathway. Nature 422, 905-909. (Pubitemid 36520044)
    • (2003) Nature , vol.422 , Issue.6934 , pp. 905-909
    • Takemaru, K.-I.1    Yamaguchi, S.2    Sik Lee, Y.3    Zhang, Y.4    Carthew, R.W.5    Moon, R.T.6
  • 10
    • 46449112475 scopus 로고    scopus 로고
    • Chibby cooperates with 14-3-3 to regulate β-catenin subcellular distribution and signaling activity
    • DOI 10.1083/jcb.200709091
    • Li, F. Q., Mofunanya, A., Harris, K., and Takemaru, K. (2008) Chibby cooperates with 14-3-3 to regulate β-catenin subcellular distribution and signaling activity. J. Cell Biol. 181, 1141-1154. (Pubitemid 351923062)
    • (2008) Journal of Cell Biology , vol.181 , Issue.7 , pp. 1141-1154
    • Li, F.-Q.1    Mofunanya, A.2    Harris, K.3    Takemaru, K.-I.4
  • 11
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • DOI 10.1016/S0092-8674(00)81067-3
    • Muslin, A. J., Tanner, J. W., Allen, P. M., and Shaw, A. S. (1996) Interaction of 14-3-3 with signaling proteins is MEDiated by the recognition of phosphoserine. Cell 84, 889-897. (Pubitemid 26106858)
    • (1996) Cell , vol.84 , Issue.6 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 14
    • 58549108026 scopus 로고    scopus 로고
    • Fine-tuning of nuclear-catenin by Chibby and 14-3-3
    • Takemaru, K., Fischer, V., and Li, F. Q. (2009) Fine-tuning of nuclear-catenin by Chibby and 14-3-3. Cell Cycle 8, 210-213.
    • (2009) Cell Cycle , vol.8 , pp. 210-213
    • Takemaru, K.1    Fischer, V.2    Li, F.Q.3
  • 15
    • 0034329424 scopus 로고    scopus 로고
    • Cloning of TC-1 (C8orf4), a novel gene found to be overexpressed in thyroid cancer
    • Chua, E. L., Young, L., Wu, W. M., Turtle, J. R., and Dong, Q. (2000) Cloning of TC-1 (C8orf4), a novel gene found to be overexpressed in thyroid cancer. Genomics 69, 342-347.
    • (2000) Genomics , vol.69 , pp. 342-347
    • Chua, E.L.1    Young, L.2    Wu, W.M.3    Turtle, J.R.4    Dong, Q.5
  • 16
    • 13844261745 scopus 로고    scopus 로고
    • TC-1 Is a Novel Tumorigenic and Natively Disordered Protein Associated with Thyroid Cancer
    • DOI 10.1158/0008-5472.CAN-03-2093
    • Sunde, M., McGrath, K. C., Young, L., Matthews, J. M., Chua, E. L., Mackay, J. P., and Death, A. K. (2004) TC-1 is a novel tumorigenic and natively disordered protein associated with thyroid cancer. Cancer Res. 64, 2766-2773. (Pubitemid 38500614)
    • (2004) Cancer Research , vol.64 , Issue.8 , pp. 2766-2773
    • Sunde, M.1    McGrath, K.C.Y.2    Young, L.3    Matthews, J.M.4    Chua, E.L.5    Mackay, J.P.6    Death, A.K.7
  • 17
    • 31544462050 scopus 로고    scopus 로고
    • TC1 (C8orf4) enhances the Wnt/β-catenin pathway by relieving antagonistic activity of Chibby
    • DOI 10.1158/0008-5472.CAN-05-3124
    • Jung, Y., Bang, S., Choi, K., Kim, E., Kim, Y., Kim, J., Park, J., Koo, H., Moon, R. T., Song, K., and Lee, I. (2006) TC1 (C8orf4) enhances the Wnt/β-catenin pathway by relieving antagonistic activity of Chibby. Cancer Res. 66, 723-728. (Pubitemid 43165934)
    • (2006) Cancer Research , vol.66 , Issue.2 , pp. 723-728
    • Jung, Y.1    Bang, S.2    Choi, K.3    Kim, E.4    Kim, Y.5    Kim, J.6    Park, J.7    Koo, H.8    Moon, R.T.9    Song, K.10    Lee, I.11
  • 18
    • 35648982507 scopus 로고    scopus 로고
    • The intrinsically disordered TC-1 interacts with Chibby via regions with high helical propensity
    • DOI 10.1110/ps.073062707
    • Gall, C., Xu, H., Brickenden, A., Ai, X., and Choy, W. Y. (2007) The intrinsically disordered TC-1 interacts with Chibby via regions with high helical propensity. Protein Sci. 16, 2510-2518. (Pubitemid 350036756)
    • (2007) Protein Science , vol.16 , Issue.11 , pp. 2510-2518
    • Gall, C.1    Xu, H.2    Brickenden, A.3    Ai, X.4    Wing, Y.C.5
  • 21
    • 33846852450 scopus 로고    scopus 로고
    • Chibby, an antagonist of the Wnt/β-catenin pathway, facilitates cardiomyocyte differentiation of murine embryonic stem cells
    • DOI 10.1161/CIRCULATIONAHA.106.642298, PII 0000301720070206000013
    • Singh, A. M., Li, F. Q., Hamazaki, T., Kasahara, H., Takemaru, K., and Terada, N. (2007) Chibby, an antagonist of the Wnt/β-catenin pathway, facilitates cardiomyocyte differentiation of murine embryonic stem cells. Circulation 115, 617-626. (Pubitemid 46226172)
    • (2007) Circulation , vol.115 , Issue.5 , pp. 617-626
    • Singh, A.M.1    Li, F.-Q.2    Hamazaki, T.3    Kasahara, H.4    Takemaru, K.-I.5    Terada, N.6
  • 23
    • 4544321242 scopus 로고    scopus 로고
    • PIGEA-14, a novel coiled-coil protein affecting the intracellular distribution of polycystin-2
    • DOI 10.1074/jbc.M314206200
    • Hidaka, S., Konecke, V., Osten, L., andWitzgall, R. (2004) PIGEA-14, a novel coiled-coil protein affecting the intracellular distribution of polycystin-2. J. Biol. Chem. 279, 35009-35016. (Pubitemid 39318137)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 35009-35016
    • Hidaka, S.1    Konecke, V.2    Osten, L.3    Witzgall, R.4
  • 24
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the armadillo repeat region of β-catenin
    • Huber, A. H., Nelson, W. J., and Weis, W. I. (1997) Three-dimensional structure of the armadillo repeat region of β-catenin. Cell 90, 871-882.
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.H.1    Nelson, W.J.2    Weis, W.I.3
  • 26
    • 0035180690 scopus 로고    scopus 로고
    • Tcf4 can specifically recognize β-catenin using alternative conformations
    • DOI 10.1038/nsb718
    • Graham, T. A., Ferkey, D. M., Mao, F., Kimelman, D., and Xu, W. (2001) Tcf4 can specifically recognize β-catenin using alternative conformations. Nat. Struct. Biol. 8, 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
  • 27
    • 0033635606 scopus 로고    scopus 로고
    • Crystal structure of a β-catenin/Tcf complex
    • Graham, T. A., Weaver, C., Mao, F., Kimelman, D., and Xu, W. (2000) Crystal structure of a β-catenin/Tcf complex. Cell 103, 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
  • 29
    • 66449119374 scopus 로고    scopus 로고
    • Chibby forms a homodimer through a heptad repeat of leucine residues in its C-terminal coiled-coil motif
    • Mofunanya, A., Li, F. Q., Hsieh, J. C., and Takemaru, K. (2009) Chibby forms a homodimer through a heptad repeat of leucine residues in its C-terminal coiled-coil motif. BMC Mol. Biol. 10, 41.
    • (2009) BMC Mol. Biol. , vol.10 , pp. 41
    • Mofunanya, A.1    Li, F.Q.2    Hsieh, J.C.3    Takemaru, K.4
  • 30
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • DOI 10.1006/abio.2000.4880
    • Sreerama, N., and Woody, R.W. (2000) Estimation of protein secondary structure from CD spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set. Anal. Biochem. 282, 252-260. (Pubitemid 32006234)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 31
    • 34247207152 scopus 로고    scopus 로고
    • Crystallization conditions of membrane protein CLC-ec1: An example outside the crystallization slot
    • DOI 10.1016/j.jcrysgro.2007.01.028, PII S0022024807001029
    • Blouwolff, J., and Fraden, S. (2007) Crystallization conditions of membrane protein CLC-ec1: an example outside the crystallization slot. J. Cryst. Growth 303, 546-553. (Pubitemid 46617581)
    • (2007) Journal of Crystal Growth , vol.303 , Issue.2 , pp. 546-553
    • Blouwolff, J.1    Fraden, S.2
  • 32
    • 36849103950 scopus 로고
    • Analysis of macromolecular polydispersity in intensity correlation spectroscopy: The method of cumulants
    • Koppel, D. E. (1972) Analysis of macromolecular polydispersity in intensity correlation spectroscopy: the method of cumulants. J. Chem. Phys. 57, 4814-4820.
    • (1972) J. Chem. Phys. , vol.57 , pp. 4814-4820
    • Koppel, D.E.1
  • 35
    • 0001689741 scopus 로고
    • Gradient-enhanced tripleresonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram, D. R., and Kay, L. E. (1994) Gradient-enhanced tripleresonance three-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. B 103, 203-216.
    • (1994) J. Magn. Reson. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 36
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 37
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson, B. A. (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 278, 313-352.
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 38
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed field gradient NRM self-diffusion measurements
    • Altieri, A. S., Hinton, D. P., and Byrd, R. A. (1995) Association of biomolecular systems via pulsed field gradient NRM self-diffusion measurements. J. Am. Chem. Soc. 117, 7566-7567.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7566-7567
    • Altieri, A.S.1    Hinton, D.P.2    Byrd, R.A.3
  • 39
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins, D. K., Grimshaw, S. B., Receveur, V., Dobson, C. M., Jones, J. A., and Smith, L. J. (1999) Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry 38, 16424-16431.
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 40
    • 0001144784 scopus 로고    scopus 로고
    • 1 constant relaxation time NMR spectroscopy
    • Akke, M., and Palmer, A. G. (1996) Monitoring macromolecular motions on microsecond-millisecond time scales byR1F andR1 constant relaxation time NMR spectroscopy. J. Am. Chem. Soc. 118, 911-912. (Pubitemid 126528353)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.4 , pp. 911-912
    • Akke, M.1    Palmer III, A.G.2
  • 42
    • 0028472289 scopus 로고
    • Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1 rho and T2 (CPMG) methods
    • Davis, D. G., Perlman, M. E., and London, R. E. (1994) Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1 rho and T2 (CPMG) methods. J. Magn. Reson.B 104, 266-275.
    • (1994) J. Magn. Reson.B , vol.104 , pp. 266-275
    • Davis, D.G.1    Perlman, M.E.2    London, R.E.3
  • 43
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiled-coil structures
    • DOI 10.1016/S0076-6879(96)66032-7
    • Lupas, A. (1996) Prediction and analysis of coiled-coil structures. Methods Enzymol. 266, 513-525. (Pubitemid 26165886)
    • (1996) Methods in Enzymology , vol.266 , pp. 513-525
    • Lupas, A.1
  • 44
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky, V. N., Gillespie, J. R., and Fink, A. L. (2000) Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 41, 415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 48
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • DOI 10.1110/ps.4210102
    • Uversky, V. N. (2002) Natively unfolded proteins: a point where biology waits for physics. Protein Sci. 11, 739-756. (Pubitemid 34241284)
    • (2002) Protein Science , vol.11 , Issue.4 , pp. 739-756
    • Uversky, V.N.1
  • 49
    • 33751552347 scopus 로고    scopus 로고
    • Sensitivity of secondary structure propensities to sequence differences between R- and γ-synuclein: Implications for fibrillation
    • DOI 10.1110/ps.062465306
    • Marsh, J. A., Singh, V. K., Jia, Z., and Forman-Kay, J. D. (2006) Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation. Protein Sci. 15, 2795-2804. (Pubitemid 44833760)
    • (2006) Protein Science , vol.15 , Issue.12 , pp. 2795-2804
    • Marsh, J.A.1    Singh, V.K.2    Jia, Z.3    Forman-Kay, J.D.4
  • 50
    • 0036129107 scopus 로고    scopus 로고
    • Probability-based protein secondary structure identification using combined NMR chemical-shift data
    • DOI 10.1110/ps.3180102
    • Wang, Y., and Jardetzky, O. (2002) Probability-based protein secondary structure identification using combined NMR chemical-shift data. Protein Sci. 11, 852-861. (Pubitemid 34241293)
    • (2002) Protein Science , vol.11 , Issue.4 , pp. 852-861
    • Wang, Y.1    Jardetzky, O.2
  • 51
    • 0028673594 scopus 로고
    • Chemical shifts as a tool for structure determination
    • Wishart, D. S., and Sykes, B. D. (1994) Chemical shifts as a tool for structure determination. Methods Enzymol. 239, 363-392.
    • (1994) Methods Enzymol. , vol.239 , pp. 363-392
    • Wishart, D.S.1    Sykes, B.D.2
  • 53
    • 0021719074 scopus 로고
    • Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded R-helical coiled-coils
    • Lau, S. Y., Taneja, A. K., and Hodges, R. S. (1984) Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded alpha-helical coiled-coils. J. Biol. Chem. 259, 13253-13261. (Pubitemid 15223850)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.21 , pp. 13253-13261
    • Lau, S.Y.M.1    Taneja, A.K.2    Hodges, R.S.3
  • 54
    • 0035497781 scopus 로고    scopus 로고
    • Practical implication of some recent studies in electrospray ionization fundamentals
    • Cech, N. B., and Enke, C. G. (2001) Practical implication of some recent studies in electrospray ionization fundamentals. Mass Spectrom. Rev. 20, 362-387.
    • (2001) Mass Spectrom. Rev. , vol.20 , pp. 362-387
    • Cech, N.B.1    Enke, C.G.2
  • 55
    • 33947377924 scopus 로고    scopus 로고
    • Signal response of coexisting protein conformers in electrospray mass spectrometry
    • DOI 10.1021/ac0620056
    • Kuprowski, M. C., and Konermann, L. (2007) Signal response of co-existing protein conformers in electrospray mass spectrometry. Anal. Biochem. 79, 2499-2506. (Pubitemid 46449032)
    • (2007) Analytical Chemistry , vol.79 , Issue.6 , pp. 2499-2506
    • Kuprowski, M.C.1    Konermann, L.2
  • 56
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anistropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin, K., Riek, R., Wider, G., and Wuthrich, K. (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anistropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. U.S.A. 94, 12366-12371.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 58
    • 17444433002 scopus 로고    scopus 로고
    • The design of coiled-coil structure and assemblies
    • Woolfson, D. N. (2005) The design of coiled-coil structure and assemblies. Adv. Protein Chem. 70, 79-112.
    • (2005) Adv. Protein Chem. , vol.70 , pp. 79-112
    • Woolfson, D.N.1
  • 59
    • 75649124555 scopus 로고    scopus 로고
    • Nuclear-cytoplasmic shuttling of Chibby controls beta-catenin signaling
    • Li, F. Q., Mofunanya, A., Fischer, V., Hall, J., and Takemaru, K. I. (2010) Nuclear-cytoplasmic shuttling of Chibby controls beta-catenin signaling. Mol. Biol. Cell 21, 311-322.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 311-322
    • Li, F.Q.1    Mofunanya, A.2    Fischer, V.3    Hall, J.4    Takemaru, K.I.5
  • 60
    • 77950629383 scopus 로고    scopus 로고
    • Chibby interacts with NBPF1 and clusterin, two candidate tumor suppressors linked to neuroblastoma
    • Vandepoele, K., Staes, K., Andries, V., and van Roy, F. (2010) Chibby interacts with NBPF1 and clusterin, two candidate tumor suppressors linked to neuroblastoma. Exp. Cell Res. 316, 1225-1233.
    • (2010) Exp. Cell Res. , vol.316 , pp. 1225-1233
    • Vandepoele, K.1    Staes, K.2    Andries, V.3    Van Roy, F.4
  • 61
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • DOI 10.1016/j.jmb.2004.03.017, PII S0022283604003079
    • Fuxreiter, M., Simon, I., Friedrich, P., and Tompa, P. (2004) PreforMED structural elements feature in partner recognition by intrinsically unstructured proteins. J. Mol. Biol. 338, 1015-1026. (Pubitemid 38542830)
    • (2004) Journal of Molecular Biology , vol.338 , Issue.5 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 62
    • 24944546549 scopus 로고    scopus 로고
    • Coupled folding and binding with R-helix-forming molecular recognition elements
    • DOI 10.1021/bi050736e
    • Oldfield, C. J., Cheng, Y., Cortese, M. S., Romero, P., Uversky, V. N., and Dunker, A. K. (2005) Coupled folding and binding with R-helixforming molecular recognition elements. Biochemistry 44, 12454-12470. (Pubitemid 41324337)
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12454-12470
    • Oldfield, C.J.1    Cheng, Y.2    Cortese, M.S.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 63
    • 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
    • Daniels, D. L., and Weis, W. I. (2002) ICAT inhibits β-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules. Mol. Cell 10, 573-584. (Pubitemid 35291069)
    • (2002) Molecular Cell , vol.10 , Issue.3 , pp. 573-584
    • Daniels, D.L.1    Weis, W.I.2
  • 64
    • 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
    • Graham, T. A., Clements, W. K., Kimelman, D., and Xu, W. (2002) The crystal structure of the β-catenin/ICAT complex reveals the inhibitory mechanism of ICAT. Mol. Cell 10, 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
  • 65
    • 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
    • Huber, A. H., and Weis, W. I. (2001) The structure of the β-catenin/ E-cadherin complex and the molecular basis of diverse ligand recognition by β-catenin. Cell 105, 391-402. (Pubitemid 32455345)
    • (2001) Cell , vol.105 , Issue.3 , pp. 391-402
    • Huber, A.H.1    Weis, W.I.2
  • 66
    • 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
    • Spink, K. E., Fridman, S. G., and Weis, W. I. (2001) Molecular mechanisms of β-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-β-catenin complex. EMBO J. 20, 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
  • 68
    • 38849199178 scopus 로고    scopus 로고
    • Dynein light chain LC8 is a dimerization hub essential in diverse protein networks
    • DOI 10.1021/bi701995m
    • Barbar, E. (2008) Dynein light chain LC8 is a dimerization hub essential in diverse protein networks. Biochemistry 47, 503-508. (Pubitemid 351195422)
    • (2008) Biochemistry , vol.47 , Issue.2 , pp. 503-508
    • Barbar, E.1
  • 69
    • 33748460073 scopus 로고    scopus 로고
    • Heteronuclear NMR Identifies a Nascent Helix in Intrinsically Disordered Dynein Intermediate Chain: Implications for Folding and Dimerization
    • DOI 10.1016/j.jmb.2006.08.006, PII S0022283606009946
    • Benison, G., Nyarko, A., and Barbar, E. (2006) Heteronuclear NMR identifies a nascent helix in intrinsically disordered dynein interMEDiate chain: implications for folding and dimerization. J. Mol. Biol. 362, 1082-1093. (Pubitemid 44353526)
    • (2006) Journal of Molecular Biology , vol.362 , Issue.5 , pp. 1082-1093
    • Benison, G.1    Nyarko, A.2    Barbar, E.3
  • 70
    • 48649084513 scopus 로고    scopus 로고
    • Brucella abortus MFP: A trimeric coiled-coil protein with membrane fusogenic activity
    • Carrica, M. C., Craig, P. O., Alonso, S. V., Goldbaum, F. A., and Cravero, S. L. (2008) Brucella abortus MFP: a trimeric coiled-coil protein with membrane fusogenic activity. Biochemistry 47, 8165-8175.
    • (2008) Biochemistry , vol.47 , pp. 8165-8175
    • Carrica, M.C.1    Craig, P.O.2    Alonso, S.V.3    Goldbaum, F.A.4    Cravero, S.L.5
  • 73
    • 46549086366 scopus 로고    scopus 로고
    • Intrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stress
    • Singh, V. K., Pacheco, I., Uversky, V. N., Smith, S. P., MacLeod, R. J., and Jia, Z. (2008) Intrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stress. J. Mol. Biol. 380, 313-326.
    • (2008) J. Mol. Biol. , vol.380 , pp. 313-326
    • Singh, V.K.1    Pacheco, I.2    Uversky, V.N.3    Smith, S.P.4    MacLeod, R.J.5    Jia, Z.6
  • 74
    • 33744942206 scopus 로고    scopus 로고
    • The C/EBP homologous protein CHOP (GADD153) is an inhibitor of Wnt/TCF signals
    • DOI 10.1038/sj.onc.1209380, PII 1209380
    • Horndasch, M., Lienkamp, S., Springer, E., Schmitt, A., Pavenstadt, H., Walz, G., and Gloy, J. (2006) The C/EBP homologous protein CHOP (GADD153) is an inhibitor of Wnt/TCF signals. Oncogene 25, 3397-3407. (Pubitemid 43877043)
    • (2006) Oncogene , vol.25 , Issue.24 , pp. 3397-3407
    • Horndasch, M.1    Lienkamp, S.2    Springer, E.3    Schmitt, A.4    Pavenstadt, H.5    Walz, G.6    Gloy, J.7
  • 76
    • 76649114676 scopus 로고    scopus 로고
    • Protein dynamics and conformational disorder in molecular recognition
    • Mittag, T., Kay, L. E., and Forman-Kay, J. D. (2010) Protein dynamics and conformational disorder in molecular recognition. J. Mol. Recognit. 23, 105-116.
    • (2010) J. Mol. Recognit. , vol.23 , pp. 105-116
    • Mittag, T.1    Kay, L.E.2    Forman-Kay, J.D.3
  • 79
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • DOI 10.1016/S0959-440X(02)00289-0
    • Dyson, H. J., and Wright, P. E. (2002) Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 12, 54-60. (Pubitemid 34142721)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.1 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 80
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • Dyson, H. J., and Wright, P. E. (2005) Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell. Biol. 6, 197-208. (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.