Dipartimento di Chimica, Università Federico II, Complesso Universitario MSA, via Cintia 45, 80126 Napoli, Italy
Istituto di Biostrutture e Bioimmagini del CNR, via Mezzocannone, 16, 80134 Napoli, Italy
Istituto di Genetica e Biofisica Adriano B. Traverso del CNR, via P. Castellino, 111, 80126 Napoli, Italy
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Xing, P. X., Hu, X. F., Pietersz, G. A., Hosick, H. L., McKenzie, I. F., Cripto: A novel target for antibody-based cancer immunotherapy (2004) Cancer Res., 64, pp. 4018-4023
Hu, X. F., Xing, P. X., Cripto as a target for cancer immunotherapy (2005) Expert Opin. Ther. Targets, 9, pp. 383-394
Niemeyer, C. C., Persico, M. G., Adamson, E. D., Cripto: Roles in mammary cell growth, survival, differentiation and transformation (1998) Cell Death Differ., 5, pp. 440-449
Salomon, D. S., Bianco, C., Ebert, A. D., Khan, N. I., De Santis, M., The EGF-CFC family: Novel epidermal growth factor-related proteins in development and cancer (2000) Endocr. -Relat. Cancer, 7, pp. 199-226
Sonntag, K. C., Simantov, R., Bjorklund, L., Cooper, O., Pruszak, J., Context-dependent neuronal differentiation and germ layer induction of Smad4-/- and Cripto-/- embryonic stem cells (2005) Mol. Cell Neurosci., 28, pp. 417-429
Kenney, N. J., Adkins, H. B., Sanicola, M., Nodal and Cripto-1: Embryonic pattern formation genes involved in mammary gland development and tumorigenesis (2004) J. Mammary Gland Biol. Neoplasia, 9, pp. 133-144
Adamson, E. D., Minchiotti, G., Salomon, D. S., Cripto: A tumor growth factor and more (2002) J. Cell. Physiol., 190, pp. 267-278
Yan, Y. T., Liu, J. J., Luo, Y., C., E., Haltiwanger, R. S., Dual roles of Cripto as a ligand and coreceptor in the nodal signaling pathway (2002) Mol. Cell Biol., 22, pp. 4439-4449
Schier, A. F., Nodal signaling in vertebrate development (2003) Annu. Rev. Cell Dev. Biol., 19, pp. 589-621
Chen, C., Ware, S. M., Sato, A., Houston-Hawkins, D. E., Habas, R., The Vg1-related protein Gdf3 acts in a Nodal signaling pathway in the pre-gastrulation mouse embryo (2006) Development, 133, pp. 319-329
Cheng, S. K., Olale, F., Bennett, J. T., Brivanlou, A. H., Schier, A. F., EGF-CFC proteins are essential coreceptors for the TGF-beta signals Vg1 and GDF1 (2003) Genes Dev., 17, pp. 31-36
Gray, P. C., Harrison, C. A., Vale, W., Cripto forms a complex with activin and type II activin receptors and can block activin signaling (2003) Proc. Natl. Acad. Sci. U. S. A., 100, pp. 5193-5198
Foley, S. F., Van Vlijmen, H. W., Boynton, R. E., Adkins, H. B., Cheung, A. E., The CRIPTO/FRL-1/CRYPTIC (CFC) domain of human Cripto. Functional and structural insights through disulfide structure analysis (2003) Eur. J. Biochem., 270, pp. 3610-3618
Risbridger, G. P., Schmitt, J. F., Robertson, D. M., Activins and inhibins in endocrine and other tumors (2001) Endocr. Rev., 22, pp. 836-858
Shen, M. M., Decrypting the role of Cripto in tumorigenesis (2003) J. Clin. Invest., 112, pp. 500-502
Shen, M. M., Schier, A. F., The EGF-CFC gene family in vertebrate development (2000) Trends Genet., 16, pp. 303-309
Persico, M. G., Liguori, G. L., Parisi, S., D'Andrea, D., Salomon, D. S., Cripto in tumors and embryo development (2001) Biochim. Biophys. Acta, 1552, pp. 87-93
Wishart, D. S., Sykes, B. D., Richards, F. M., Relationship between nuclear magnetic resonance chemical shift and protein secondary structure (1991) J. Mol. Biol., 222, pp. 311-333
Harrison, P. M., Sternberg, M. J. E., The disulphide beta-cross: From cystine geometry and clustering to classification of small disulphide-rich protein folds (1996) J. Mol. Biol., 264, pp. 603-623
Schiffer, S. G., Foley, S., Kaffashan, A., Hronowski, X., Zichittella, A. E., Fucosylation of Cripto is required for its ability to facilitate nodal signaling (2001) J. Biol. Chem., 276, pp. 37769-37778
Bax, A., Davis, D. G., MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy (1985) J. Magn. Res., 65, pp. 355-360
States, D. J., Haberhorn, R. A., Ruben, D. J., A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants (1982) J. Magn. Res., 48, pp. 286-292
Johnson, B. A., Blevins, R. A., NMRView: A computer program for the visualization and analysis of NMR data (1994) J. Biomol. NMR, 4, pp. 603-614
Case, D. A., Pearlman, D. A., Caldwell, J. W., Cheatham, I. T. E., Ross, W. S., (1999) AMBER 6, , University of California: San Francisco, CA
Pearlman, D. A., Case, D. A., Caldwell, J. W., Ross, W. S., Cheatham, I. T. E., AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to stimulate the structural and energetic properties of molecules (1996) Proteins, 26, pp. 304-313
Weiner, S. J., Kollmann, P. A., Nguyen, D. T., Case, D. A., An all atom force field for simulations of proteins and nucleic acids (1986) J. Comput. Chem., 7, pp. 230-238
Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala
We report here for the first time the solution structures at pH 3 and pH 6 of the synthetic CFC domain of mouse Cripto and of the point mutated variant W107A that is unable to bind to the Alk4 Cripto receptor. NMR data confirm that the CFC domain has a C1-C4, C2-C6, C3-C5 disulfide pattern and show that structures are rather flexible and globally extended, with three noncanonical antiparallel strands. His104 and Trp107 side chains protrude from a protein edge and are strongly exposed to solvent, supporting previous evidence of direct involvement in receptor binding. On the opposite molecule side, several nonpolar residues are gathered, forming a large hydrophobic patch that supposedly acts as interface with the cell membrane or the adjacent EGF-like domain. A second hydrophilic patch surrounding His104 and Trp107 is present only in the wild type variant, suggesting a possible involvement in modulating Alk4 recognition.
Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala
Kim YH, Shin SW, Pellicano R, Fagoonee S, Choi IJ, Kim YI, Park B, Choi JM, Kim SG, Choi J, Park JY, Oh S, Yang HJ, Lim JH, Im JP, Kim JS, Jung HC, Ponzetto A, Figura N, Malfertheiner P, Choi IJ, Kook MC, Kim YI, Cho SJ, Lee JY, Kim CG, Park B, Nam BH, Bae SE, Choi KD, Choe J, Kim SO, Na HK, Choi JY, Ahn JY, Jung KW, Lee J, Kim DH, Chang HS, Song HJ, Lee GH, Jung HY, Seta T, Takahashi Y, Noguchi Y, Shikata S, Sakai T, Sakai K, Yamashita Y, Nakayama T, Leja M, Park JY, Murillo R, Liepniece-karele I, Isajevs S, Kikuste I, Rudzite D, Krike P, Parshutin S, Polaka I, Kirsners A, Santare D, Folkmanis V, Daugule I, Plummer M, Herrero R, Tsukamoto T, Nakagawa M, Kiriyama Y, Toyoda T, Cao X, Corral JE, Mera R, Dye CW, Morgan DR, Lee YC, Lin JT, Garcia Martin R, Matia Cubillo A, Lee SH, Park JM, Han YM, Ko WJ, Hahm KB, Leontiadis GI, Ford AC, Ichinose M, Sugano K, Jeong M, Park JM, Han YM, Park KY, Lee DH, Yoo JH, Cho JY, Hahm KB, Bang CS, Baik GH, Shin IS, Kim JB, Suk KT, Yoon JH, Kim YS, Kim DJ * Helicobacter pylori Eradication for Prevention of Metachronous Recurrence after Endoscopic Resection of Early Gastric Cancer(297 views) N Engl J Med (ISSN: 0028-4793, 0028-4793linking, 1533-4406electronic), 2015 Jun; 30642104201566393291: 749-756. Impact Factor:59.558 ViewExport to BibTeXExport to EndNote