Structure-based design of a potent artificial transactivation domain based on p53 (425 views)
J Am Chem Soc (ISSN: 1520-5126, 0002-2786, 0002-7863), 2012 Jan 25; 134(3): 1715-1723.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 5.65, 5-year impact factor: 7.873
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84856247693&partnerID=40&md5=08049918ab7aa82cf4afbeb870183810
Keywords: Dna-Binding Domain, Human Disease, In-Vitro Analysis, Model System, N-Capping Motif, Natural Amino Acids, Structure-Based, Target Proteins, Transactivation Domain, Transcription Activators, Transcriptional Activators, Transcriptional Regulation, Disease Control, Genes, Peptides, Structural Design, Protein P53, Article, Capping Phenomenon, Controlled Study, Nonhuman, Protein Modification, Protein Motif, Protein Structure, Yeast, Amino Acid Motifs, Amino Acid Sequence, Gene Expression Regulation, Fungal, Leucine, Molecular, Molecular Sequence Data, Tertiary, Transcriptional Activation, Tumor Suppressor Protein P53, Chemistry, Chemical Synthesis, Metabolism, Genetics,
Affiliations:
*** IBB - CNR ***
D partement de Biochimie, Universit de Montr al, C. P. 6128 Succursale, Centre-Ville, Montr al, QC H3C 3J7, Canada
Institute of Biostructures and Bioimaging, Department of Biological Sciences, University of Naples Federico II, via Mezzocannone 16, 80134 Napoli, Italy
Departement de Biochimie, Universite de Montreal, C. P. 6128 Succursale, Centre-Ville, Montreal, Quebec H3C 3J7, Canada.
References:
Ptashne, M., Gann, A. A. F., (1997) Nature, 386, p. 56
Giniger, E., Ptashne, M., (1987) Nature, 330, p. 670
Sadowski, I., Ma, J., Triezenberg, S., Ptashne, M., (1988) Nature, 335, p. 563
Goodrich, J. A., Hoey, T., Thut, C. J., Admon, A., Tjian, R., (1993) Cell, 75, p. 519
Brown, C. E., Howe, L., Sousa, K., Alley, S. C., Carrozza, M. J., Tan, S., Workman, J. L., (2001) Science, 292, p. 2333
Prochasson, P., Neely, K. E., Hassan, A. H., Li, B., Workman, J. L., (2003) Mol. Cell, 12, p. 983
Yang, F., Debeaumont, R., Zhou, S., Naar, A. M., (2004) Proc. Natl. Acad. Sci. U. S. A., 101, p. 2339
Blau, J., Xiao, H., McCracken, S., O'Hare, P., Greenblatt, J., Bentley, D., (1996) Mol. Cell. Biol., 16, p. 2044
Tansey, W. P., Ruppert, S., Tjian, R., Herr, W., (1994) Genes Dev., 8, p. 2756
Black, J. C., Choi, J. E., Lombardo, S. R., Carey, M., (2006) Mol. Cell, 23, p. 809
Gutierrez, J. L., Chandy, M., Carrozza, M. J., Workman, J. L., (2007) EMBO J., 26, p. 730
Brown, S. A., Weirich, C. S., Newton, E. M., Kingston, R. E., (1998) EMBO J., 17, p. 3146
Lee, L. W., Mapp, A. K., (2010) J. Biol. Chem., 285, p. 11033
Graslund, T., Li, X., Magnenat, L., Popkov, M., (2005) J. Biol. Chem., 280, p. 3707
Rodriguez-Martinez, J. A., Peterson-Kaufman, K. J., Ansari, A. Z., (2010) Biochim. Biophys. Acta Gene Reg. Mech., 1799, p. 768
Sera, T., (2009) Adv. Drug Delivery Rev., 61, p. 513
Visser, A. E., Verschure, P. J., Gommans, W. M., Haisma, H. J., Rots, M. G., (2006) Adv. Genet., 56, p. 131
Verschure, P. J., Visser, A. E., Rots, M. G., (2006) Adv. Genet., 56, p. 163
Hannon, G. J., (2002) Nature, 418, p. 244
Rana, T. M., (2007) Nat. Rev. Mol. Cell Biol., 8, p. 23
Kim, D. H., Rossi, J. J., (2007) Nat. Rev. Genet., 8, p. 173
Dervan, P. B., Doss, R. M., Marques, M. A., (2005) Curr. Med. Chem. Anticancer Agents, 5, p. 373
Nickols, N. G., Jacobs, C. S., Farkas, M. E., Dervan, P. B., (2007) Nucleic Acids Res., 35, p. 363
Muzikar, K. A., Nickols, N. G., Dervan, P. B., (2009) Proc. Natl. Acad. Sci. U. S. A., 106, p. 16598
Nielsen, P. E., (2005) Q. Rev. Biophys., 38, p. 345
Chen, J., Peterson, K. R., Iancu-Rubin, C., Bieker, J. J., (2010) Proc. Natl. Acad. Sci. U. S. A., 107, p. 16846
Liu, B., Han, Y., Corey, D. R., Kodadek, T., (2002) J. Am. Chem. Soc., 124, p. 1838
Nielsen, P. E., Egholm, M., Berg, R. H., Buchardt, O., (1991) Science, 254, p. 1497
Beerli, R. R., (2002) Nat. Biotechnol., 20, p. 135
Beerli, R. R., Dreier, B., (2000) Proc. Natl. Acad. Sci. U. S. A., 97, p. 1495
Beerli, R. R., Schopfer, U., Dreier, B., (2000) J. Biol. Chem., 275, p. 32617
Di Lello, P., Jenkins, L. M. M., Jones, T. N., Nguyen, B. D., Hara, T., Yamaguchi, H., Dikeakos, J. D., Omichinski, J. G., (2006) Mol. Cell, 22, p. 731
Langlois, C., Mas, C., Di Lello, P., Jenkins, L. M. M., Legault, P., Omichinski, J. G., (2008) J. Am. Chem. Soc., 130, p. 10596
Uesugi, M., Nyanguile, O., Lu, H., Levine, A. J., Verdine, G. L., (1997) Science, 277, p. 1310
Radhakrishnan, I., Perezalvarado, G. C., Parker, D., Dyson, H. J., Montminy, M. R., Wright, P. E., (1997) Cell, 91, p. 741
Dames, S. A., Martinez-Yamount, M., Guzman, R. N. D., Dyson, H. J., Wright, P. E., (2002) Proc. Natl. Acad. Sci. U. S. A., 99, p. 5271
Wojciak, J. M., Martinez-Yamout, M. A., Dyson, H. J., Wright, P. E., (2009) EMBO J., 28, p. 948
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., Pavletich, N. P., (1996) Science, 274, p. 948
Mattei, E., Corbi, N., Di Certo, M. G., Strimpakos, G., Severini, C., Onori, A., Desantis, A., Passananti, C., (2007) PLoS One, 2, p. 774
Lu, Y., Tian, C., Danialou, G., Gilbert, R., Petrof, B. J., Karpati, G., Nalbantoglu, J., (2008) J. Biol. Chem., 283, p. 34720
Stanojevic, D., Young, R. A., (2002) Biochemistry, 41, p. 7209
Di Certo, M. G., Corbi, N., Strimpakos, G., Onori, A., Luvisetto, S., Severini, C., Guglielmotti, A., Passananti, C., (2010) Hum. Mol. Genet., 19, p. 752
Wilber, A., Tschulena, U., Hargrove, P. W., Kim, Y. S., Persons, D. A., Nienhuis, A. W., (2010) Blood, 115, p. 3033
Rowe, S. P., Casey, R. J., Brennan, B. B., Buhrlage, S. J., Mapp, A. K., (2007) J. Am. Chem. Soc., 129, p. 10654
Ansari, A. Z., Mapp, A. K., Nguyen, D. H., Dervan, P. B., Ptashne, M., (2001) Chem. Biol., 8, p. 583
Beltran, A. S., Sun, X., Lizardi, P. M., Blancafort, P., (2008) Mol. Cancer Ther., 7, p. 1080
Ma, J., Ptashne, M., (1987) Cell, 51, p. 113
Xiao, X., Yu, P., Lim, H. S., Sikder, D., Kodadek, T., (2007) Angew. Chem., Int. Ed., 46, p. 2865
Liu, B., Alluri, P. G., Yu, P., Kodadek, T., (2005) J. Am. Chem. Soc., 127, p. 8254
Jung, D. J., Shimogawa, H., Kwon, Y., Mao, Q., Sato, S., Kamisuki, S., Kigoshi, H., Uesugi, M., (2009) J. Am. Chem. Soc., 131, p. 4774
Jung, D. J., Choi, Y. M., Uesugi, M., (2006) Drug Discovery Today, 11, p. 452
Minter, A. R., Brennan, B. B., Mapp, A. K., (2004) J. Am. Chem. Soc., 126, p. 10504
Candau, R., Scolnick, D. M., Darpino, P., Ying, C. Y., Halazonetis, T. D., Berger, S. L., (1997) Oncogene, 12, p. 807
Triezenberg, S. J., Kingsbury, R. C., McKnight, S. L., (1988) Genes Dev., 2, p. 718
Unger, T., Nau, M. M., Segal, S., Minna, J. D., (1992) EMBO J., 11, p. 1383
Sullivan, S. M., Horn, P. J., Olson, V. A., Koop, A. H., Niu, W., Ebright, R. H., Triezenberg, S. J., (1998) Nucleic Acid Res., 26, p. 4487
Marion, D., Kay, L., Sparks, S. W., Torchia, D., Bax, A., (1989) J. Am. Chem. Soc., 111, p. 1515
Ikura, M., Bax, A., (1992) J. Am. Chem. Soc., 114, p. 2433
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., Bax, A., (1995) J. Biomol. NMR, 6, p. 277
Vranken, W. F., Boucher, W., Stevens, T. J., Fogh, R. H., Pajon, A., Llinas, P., Ulrich, E. L., Laue, E. D., (2005) Proteins, 59, p. 687
Cornilescu, G., Delaglio, F., Bax, A., (1999) J. Biomol. NMR, 13, p. 289
Brunger, A. T., Adams, P. D., Clore, G. M., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. -S., Kuszewski, J., Warren, G. L., (1998) Acta Crystallogr., 54, p. 905
Choy, W. -Y., Tollinger, M., Mueller, G. A., Kay, L. E., (2001) J. Biomol. NMR, 21, p. 31
Laskowski, R. A., Antoon, J., Rullmann, C., MacArthur, M. W., Kaptein, R., Thornton, J. M., (1996) J. Biomol. NMR, 8, p. 477
D'Andrea, L. D., Iaccarino, G., Fattorusso, R., Sorriento, D., Carannante, C., Capasso, D., Trimarco, B., Pedone, C., (2005) Proc. Natl. Acad. Sci. U. S. A., 102, p. 14215
Aurora, R., Rose, G. D., (1998) Protein Sci., 7, p. 21
Diana, D., Ziaco, B., Colombo, G., Scarabelli, G., Romanelli, A., Fedone, C., Fattorusso, R., D'Andrea, L. D., (2008) Chem. -Eur. J., 14, p. 4164
Gu, W., Roeder, R. G., (1997) Cell, 90, p. 595
Avantaggiati, M. L., Ogryzko, V., Gardner, K., Giordano, A., Levine, A. S., Kelly, K., (1997) Cell, 89, p. 1175
Ferreon, J. C., Lee, C. W., Arai, M., Martinez-Yamout, M. A., Dyson, H. J., Wright, P. E., (2009) Proc. Natl. Acad. Sci. U. S. A., 106, p. 6591
Teufel, D. P., Freund, S. M., Bycroft, M., Fersht, A. R., (2007) Proc. Natl. Acad. Sci. U. S. A., 104, p. 7009
Padmanabhan, S., Baldwin, R. L., (1994) Protein Sci., 3, p. 1992
Luo, P., Baldwin, R. L., (2002) Biophys. Chem., 96, p. 103
Munoz, V., Serrano, L., (1994) Nat. Struct. Biol., 1, p. 399
Creamer, T. P., Rose, G. D., (1995) Protein Sci., 4, p. 1305
Kutchukian, P. S., Yang, J. S., Verdine, G. L., Shakhnovich, E. I., (2009) J. Am. Chem. Soc., 131, p. 4622
Bautista, A. D., Appelbaum, J. S., Craig, C. J., Michel, J., Schepartz, A., (2010) J. Am. Chem. Soc., 132, p. 2904
Kim, Y. W., Kutchukian, P. S., Verdine, G. L., (2010) Org. Lett., 12, p. 3046
Shoemaker, B. A., Portman, J. J., Wolynes, P. G., (2000) Proc. Natl. Acad. Sci. U. S. A., 97, p. 8868
J Am Chem Soc (ISSN: 1520-5126, 0002-2786, 0002-7863), 2012 Jan 25; 134(3): 1715-1723.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 5.65, 5-year impact factor: 7.873
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84856247693&partnerID=40&md5=08049918ab7aa82cf4afbeb870183810
Keywords: Dna-Binding Domain, Human Disease, In-Vitro Analysis, Model System, N-Capping Motif, Natural Amino Acids, Structure-Based, Target Proteins, Transactivation Domain, Transcription Activators, Transcriptional Activators, Transcriptional Regulation, Disease Control, Genes, Peptides, Structural Design, Protein P53, Article, Capping Phenomenon, Controlled Study, Nonhuman, Protein Modification, Protein Motif, Protein Structure, Yeast, Amino Acid Motifs, Amino Acid Sequence, Gene Expression Regulation, Fungal, Leucine, Molecular, Molecular Sequence Data, Tertiary, Transcriptional Activation, Tumor Suppressor Protein P53, Chemistry, Chemical Synthesis, Metabolism, Genetics,
Affiliations:
*** IBB - CNR ***
D partement de Biochimie, Universit de Montr al, C. P. 6128 Succursale, Centre-Ville, Montr al, QC H3C 3J7, Canada
Institute of Biostructures and Bioimaging, Department of Biological Sciences, University of Naples Federico II, via Mezzocannone 16, 80134 Napoli, Italy
Departement de Biochimie, Universite de Montreal, C. P. 6128 Succursale, Centre-Ville, Montreal, Quebec H3C 3J7, Canada.
References:
Ptashne, M., Gann, A. A. F., (1997) Nature, 386, p. 56
Giniger, E., Ptashne, M., (1987) Nature, 330, p. 670
Sadowski, I., Ma, J., Triezenberg, S., Ptashne, M., (1988) Nature, 335, p. 563
Goodrich, J. A., Hoey, T., Thut, C. J., Admon, A., Tjian, R., (1993) Cell, 75, p. 519
Brown, C. E., Howe, L., Sousa, K., Alley, S. C., Carrozza, M. J., Tan, S., Workman, J. L., (2001) Science, 292, p. 2333
Prochasson, P., Neely, K. E., Hassan, A. H., Li, B., Workman, J. L., (2003) Mol. Cell, 12, p. 983
Yang, F., Debeaumont, R., Zhou, S., Naar, A. M., (2004) Proc. Natl. Acad. Sci. U. S. A., 101, p. 2339
Blau, J., Xiao, H., McCracken, S., O'Hare, P., Greenblatt, J., Bentley, D., (1996) Mol. Cell. Biol., 16, p. 2044
Tansey, W. P., Ruppert, S., Tjian, R., Herr, W., (1994) Genes Dev., 8, p. 2756
Black, J. C., Choi, J. E., Lombardo, S. R., Carey, M., (2006) Mol. Cell, 23, p. 809
Gutierrez, J. L., Chandy, M., Carrozza, M. J., Workman, J. L., (2007) EMBO J., 26, p. 730
Brown, S. A., Weirich, C. S., Newton, E. M., Kingston, R. E., (1998) EMBO J., 17, p. 3146
Lee, L. W., Mapp, A. K., (2010) J. Biol. Chem., 285, p. 11033
Graslund, T., Li, X., Magnenat, L., Popkov, M., (2005) J. Biol. Chem., 280, p. 3707
Rodriguez-Martinez, J. A., Peterson-Kaufman, K. J., Ansari, A. Z., (2010) Biochim. Biophys. Acta Gene Reg. Mech., 1799, p. 768
Sera, T., (2009) Adv. Drug Delivery Rev., 61, p. 513
Visser, A. E., Verschure, P. J., Gommans, W. M., Haisma, H. J., Rots, M. G., (2006) Adv. Genet., 56, p. 131
Verschure, P. J., Visser, A. E., Rots, M. G., (2006) Adv. Genet., 56, p. 163
Hannon, G. J., (2002) Nature, 418, p. 244
Rana, T. M., (2007) Nat. Rev. Mol. Cell Biol., 8, p. 23
Kim, D. H., Rossi, J. J., (2007) Nat. Rev. Genet., 8, p. 173
Dervan, P. B., Doss, R. M., Marques, M. A., (2005) Curr. Med. Chem. Anticancer Agents, 5, p. 373
Nickols, N. G., Jacobs, C. S., Farkas, M. E., Dervan, P. B., (2007) Nucleic Acids Res., 35, p. 363
Muzikar, K. A., Nickols, N. G., Dervan, P. B., (2009) Proc. Natl. Acad. Sci. U. S. A., 106, p. 16598
Nielsen, P. E., (2005) Q. Rev. Biophys., 38, p. 345
Chen, J., Peterson, K. R., Iancu-Rubin, C., Bieker, J. J., (2010) Proc. Natl. Acad. Sci. U. S. A., 107, p. 16846
Liu, B., Han, Y., Corey, D. R., Kodadek, T., (2002) J. Am. Chem. Soc., 124, p. 1838
Nielsen, P. E., Egholm, M., Berg, R. H., Buchardt, O., (1991) Science, 254, p. 1497
Beerli, R. R., (2002) Nat. Biotechnol., 20, p. 135
Beerli, R. R., Dreier, B., (2000) Proc. Natl. Acad. Sci. U. S. A., 97, p. 1495
Beerli, R. R., Schopfer, U., Dreier, B., (2000) J. Biol. Chem., 275, p. 32617
Di Lello, P., Jenkins, L. M. M., Jones, T. N., Nguyen, B. D., Hara, T., Yamaguchi, H., Dikeakos, J. D., Omichinski, J. G., (2006) Mol. Cell, 22, p. 731
Langlois, C., Mas, C., Di Lello, P., Jenkins, L. M. M., Legault, P., Omichinski, J. G., (2008) J. Am. Chem. Soc., 130, p. 10596
Uesugi, M., Nyanguile, O., Lu, H., Levine, A. J., Verdine, G. L., (1997) Science, 277, p. 1310
Radhakrishnan, I., Perezalvarado, G. C., Parker, D., Dyson, H. J., Montminy, M. R., Wright, P. E., (1997) Cell, 91, p. 741
Dames, S. A., Martinez-Yamount, M., Guzman, R. N. D., Dyson, H. J., Wright, P. E., (2002) Proc. Natl. Acad. Sci. U. S. A., 99, p. 5271
Wojciak, J. M., Martinez-Yamout, M. A., Dyson, H. J., Wright, P. E., (2009) EMBO J., 28, p. 948
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., Pavletich, N. P., (1996) Science, 274, p. 948
Mattei, E., Corbi, N., Di Certo, M. G., Strimpakos, G., Severini, C., Onori, A., Desantis, A., Passananti, C., (2007) PLoS One, 2, p. 774
Lu, Y., Tian, C., Danialou, G., Gilbert, R., Petrof, B. J., Karpati, G., Nalbantoglu, J., (2008) J. Biol. Chem., 283, p. 34720
Stanojevic, D., Young, R. A., (2002) Biochemistry, 41, p. 7209
Di Certo, M. G., Corbi, N., Strimpakos, G., Onori, A., Luvisetto, S., Severini, C., Guglielmotti, A., Passananti, C., (2010) Hum. Mol. Genet., 19, p. 752
Wilber, A., Tschulena, U., Hargrove, P. W., Kim, Y. S., Persons, D. A., Nienhuis, A. W., (2010) Blood, 115, p. 3033
Rowe, S. P., Casey, R. J., Brennan, B. B., Buhrlage, S. J., Mapp, A. K., (2007) J. Am. Chem. Soc., 129, p. 10654
Ansari, A. Z., Mapp, A. K., Nguyen, D. H., Dervan, P. B., Ptashne, M., (2001) Chem. Biol., 8, p. 583
Beltran, A. S., Sun, X., Lizardi, P. M., Blancafort, P., (2008) Mol. Cancer Ther., 7, p. 1080
Ma, J., Ptashne, M., (1987) Cell, 51, p. 113
Xiao, X., Yu, P., Lim, H. S., Sikder, D., Kodadek, T., (2007) Angew. Chem., Int. Ed., 46, p. 2865
Liu, B., Alluri, P. G., Yu, P., Kodadek, T., (2005) J. Am. Chem. Soc., 127, p. 8254
Jung, D. J., Shimogawa, H., Kwon, Y., Mao, Q., Sato, S., Kamisuki, S., Kigoshi, H., Uesugi, M., (2009) J. Am. Chem. Soc., 131, p. 4774
Jung, D. J., Choi, Y. M., Uesugi, M., (2006) Drug Discovery Today, 11, p. 452
Minter, A. R., Brennan, B. B., Mapp, A. K., (2004) J. Am. Chem. Soc., 126, p. 10504
Candau, R., Scolnick, D. M., Darpino, P., Ying, C. Y., Halazonetis, T. D., Berger, S. L., (1997) Oncogene, 12, p. 807
Triezenberg, S. J., Kingsbury, R. C., McKnight, S. L., (1988) Genes Dev., 2, p. 718
Unger, T., Nau, M. M., Segal, S., Minna, J. D., (1992) EMBO J., 11, p. 1383
Sullivan, S. M., Horn, P. J., Olson, V. A., Koop, A. H., Niu, W., Ebright, R. H., Triezenberg, S. J., (1998) Nucleic Acid Res., 26, p. 4487
Marion, D., Kay, L., Sparks, S. W., Torchia, D., Bax, A., (1989) J. Am. Chem. Soc., 111, p. 1515
Ikura, M., Bax, A., (1992) J. Am. Chem. Soc., 114, p. 2433
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., Bax, A., (1995) J. Biomol. NMR, 6, p. 277
Vranken, W. F., Boucher, W., Stevens, T. J., Fogh, R. H., Pajon, A., Llinas, P., Ulrich, E. L., Laue, E. D., (2005) Proteins, 59, p. 687
Cornilescu, G., Delaglio, F., Bax, A., (1999) J. Biomol. NMR, 13, p. 289
Brunger, A. T., Adams, P. D., Clore, G. M., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. -S., Kuszewski, J., Warren, G. L., (1998) Acta Crystallogr., 54, p. 905
Choy, W. -Y., Tollinger, M., Mueller, G. A., Kay, L. E., (2001) J. Biomol. NMR, 21, p. 31
Laskowski, R. A., Antoon, J., Rullmann, C., MacArthur, M. W., Kaptein, R., Thornton, J. M., (1996) J. Biomol. NMR, 8, p. 477
D'Andrea, L. D., Iaccarino, G., Fattorusso, R., Sorriento, D., Carannante, C., Capasso, D., Trimarco, B., Pedone, C., (2005) Proc. Natl. Acad. Sci. U. S. A., 102, p. 14215
Aurora, R., Rose, G. D., (1998) Protein Sci., 7, p. 21
Diana, D., Ziaco, B., Colombo, G., Scarabelli, G., Romanelli, A., Fedone, C., Fattorusso, R., D'Andrea, L. D., (2008) Chem. -Eur. J., 14, p. 4164
Gu, W., Roeder, R. G., (1997) Cell, 90, p. 595
Avantaggiati, M. L., Ogryzko, V., Gardner, K., Giordano, A., Levine, A. S., Kelly, K., (1997) Cell, 89, p. 1175
Ferreon, J. C., Lee, C. W., Arai, M., Martinez-Yamout, M. A., Dyson, H. J., Wright, P. E., (2009) Proc. Natl. Acad. Sci. U. S. A., 106, p. 6591
Teufel, D. P., Freund, S. M., Bycroft, M., Fersht, A. R., (2007) Proc. Natl. Acad. Sci. U. S. A., 104, p. 7009
Padmanabhan, S., Baldwin, R. L., (1994) Protein Sci., 3, p. 1992
Luo, P., Baldwin, R. L., (2002) Biophys. Chem., 96, p. 103
Munoz, V., Serrano, L., (1994) Nat. Struct. Biol., 1, p. 399
Creamer, T. P., Rose, G. D., (1995) Protein Sci., 4, p. 1305
Kutchukian, P. S., Yang, J. S., Verdine, G. L., Shakhnovich, E. I., (2009) J. Am. Chem. Soc., 131, p. 4622
Bautista, A. D., Appelbaum, J. S., Craig, C. J., Michel, J., Schepartz, A., (2010) J. Am. Chem. Soc., 132, p. 2904
Kim, Y. W., Kutchukian, P. S., Verdine, G. L., (2010) Org. Lett., 12, p. 3046
Shoemaker, B. A., Portman, J. J., Wolynes, P. G., (2000) Proc. Natl. Acad. Sci. U. S. A., 97, p. 8868
Structure-based design of a potent artificial transactivation domain based on p53
Malfunctions in transcriptional regulation are associated with a number of critical human diseases. As a result, there is considerable interest in designing artificial transcription activators (ATAs) that specifically control genes linked to human diseases. Like native transcriptional activator proteins, an ATA must minimally contain a DNA-binding domain (DBD) and a transactivation domain (TAD) and, although there are several reliable methods for designing artificial DBDs, designing artificial TADs has proven difficult. In this manuscript, we present a structure-based strategy for designing short peptides containing natural amino acids that function as artificial TADs. Using a segment of the TAD of p53 as the scaffolding, modifications are introduced to increase the helical propensity of the peptides. The most active artificial TAD, termed E-Cap- (LL), is a 13-mer peptide that contains four key residues from p53, an N-capping motif and a dileucine hydrophobic bridge. In vitro analysis demonstrates that E-Cap- (LL) interacts with several known p53 target proteins, while in vivo studies in a yeast model system show that it is a 20-fold more potent transcriptional activator than the native p53-13 peptide. These results demonstrate that structure-based design represents a promising approach for developing artificial TADs that can be combined with artificial DBDs to create potent and specific ATAs. 2011 American Chemical Society
Malfunctions in transcriptional regulation are associated with a number of critical human diseases. As a result, there is considerable interest in designing artificial transcription activators (ATAs) that specifically control genes linked to human diseases. Like native transcriptional activator proteins, an ATA must minimally contain a DNA-binding domain (DBD) and a transactivation domain (TAD) and, although there are several reliable methods for designing artificial DBDs, designing artificial TADs has proven difficult. In this manuscript, we present a structure-based strategy for designing short peptides containing natural amino acids that function as artificial TADs. Using a segment of the TAD of p53 as the scaffolding, modifications are introduced to increase the helical propensity of the peptides. The most active artificial TAD, termed E-Cap- (LL), is a 13-mer peptide that contains four key residues from p53, an N-capping motif and a dileucine hydrophobic bridge. In vitro analysis demonstrates that E-Cap- (LL) interacts with several known p53 target proteins, while in vivo studies in a yeast model system show that it is a 20-fold more potent transcriptional activator than the native p53-13 peptide. These results demonstrate that structure-based design represents a promising approach for developing artificial TADs that can be combined with artificial DBDs to create potent and specific ATAs. 2011 American Chemical Society
Structure-based design of a potent artificial transactivation domain based on p53
Structure-based design of a potent artificial transactivation domain based on p53
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Fogliano V, Monti SM, Musella T, Randazzo G, Ritieni A
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Journal Of Agricultural And Food Chemistry, 1999; 66: 293-299.
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Bailey RG, Ames JM, Monti SM
An analysis of the non-volatile reaction products of aqueous Maillard model systems at pH 5, using reversed-phase HPLC with diode-array detection (340 views)
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Impact Factor: 0.895
View Export to BibTeX Export to EndNote
* The Amazing World of IDPs in Human Diseases II (13 views)
Biomolecules, 2022 Feb 25; 1211(2): 369-369.
Impact Factor: 6.064
View Export to BibTeX Export to EndNote
Ayoub J, Buonanno M, Di Fiore A, De Simone G, Monti SM
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Impact Factor: 6.208
View Export to BibTeX Export to EndNote
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Impact Factor:
View Export to BibTeX Export to EndNote
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* The Amazing World of IDPs in Human Diseases (32 views)
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Impact Factor: 4.879
View Export to BibTeX Export to EndNote
De Luca S, Verdoliva V, Saviano M
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Impact Factor: 6.205
View Export to BibTeX Export to EndNote
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* SPR and NMR characterization of the molecular interaction between A9 peptide and a model system of HER2 receptor: A fragment approach for selecting peptide structures specific for their target (135 views)
J Pept Sci (ISSN: 1075-2617linking, 1099-1387electronic), 2020 Feb; 26(2): e3231-e3231.
Impact Factor: 1.877
View Export to BibTeX Export to EndNote
Musumeci D, Rozza L, Merlino A, Paduano L, Marzo T, Massai L, Messori L, Montesarchio D
* Interaction of anticancer Ru(III) complexes with single stranded and duplex DNA model systems (568 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9226linking), 2015; 44(31): 13914-13925.
Impact Factor: 4.177
View Export to BibTeX Export to EndNote
Troise AD, Dathan NA, Fiore A, Roviello G, Di Fiore A, Caira S, Cuollo M, De Simone G, Fogliano V, Monti SM
* Faox enzymes inhibited Maillard reaction development during storage both in protein glucose model system and low lactose UHT milk (230 views)
Amino Acids (ISSN: 0939-4451, 1438-2199, 1438-2199electronic), 2014 Feb; 46(2): 279-288.
Impact Factor: 3.293
View Export to BibTeX Export to EndNote
Calce E, Sandomenico A, Saviano M, Ruvo M, De Luca S
* Cysteine Co-Oxidation Process Driven By Native Peptide Folding: An Example On Her2 Receptor Model System (371 views)
Amino Acids (ISSN: 0939-4451, 1438-2199, 1438-2199electronic), 2014; 46(5): 1197-1206.
Impact Factor: 3.293
View Export to BibTeX Export to EndNote
Banyasz A, Gustavsson T, Onidas D, Changenet-Barret P, Markovitsi D, Improta R
* Multi-pathway excited state relaxation of adenine oligomers in aqueous solution: A joint theoretical and experimental study (306 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2013 Mar; 19(11): 3762-3774.
Impact Factor: 5.696
View Export to BibTeX Export to EndNote
D'Andrea LD, Romanelli A, Di Stasi R, Pedone C
* Bioinorganic aspects of angiogenesis (543 views)
Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2010 Sep 7; 39(33): 7625-7636.
Impact Factor: 3.647
View Export to BibTeX Export to EndNote
Pensato S, Renda M, Leccia F, Saviano M, D'Andrea LD, Pedone C, Pedone PV, Romanelli A
* PNA zipper as a dimerization tool: development of a bZip mimic (597 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2010 May; 93(5): 434-441.
Impact Factor: 2.572
View Export to BibTeX Export to EndNote
Borrelli RC, Fogliano V, Monti SM, Ames JM
* Characterization of melanoidins from a glucose-glycine model system (243 views)
Eur Food Res Technol (ISSN: 1438-2377), 2002 Sep; 215(3): 210-215.
Impact Factor: 1.021
View Export to BibTeX Export to EndNote
Monti SM, Ritieni A, Sacchi R, Skog K, Borgen E, Fogliano V
* Characterization of phenolic compounds in virgin olive oil and their effect on the formation of carcinogenic/mutagenic heterocyclic amines in a model system (644 views)
J Agric Food Chem (ISSN: 0021-8561), 2001 Sep; 49(8): 3969-3975.
Impact Factor: 1.576
View Export to BibTeX Export to EndNote
Monti SM, Borrelli RC, Ritieni A, Fogliano V
A comparison of color formation and Maillard reaction products of a lactose-lysine and lactose-N(α)-acetyllysine model system (506 views)
J Agric Food Chem (ISSN: 0021-8561), 2000; 48(4): 1041-1046.
Impact Factor: 1.56
View Export to BibTeX Export to EndNote
Vinale F, Monti SM, Panunzi B, Fogliano V
Convenient synthesis of lactuloselysine and its use for LC-MS analysis in milk-like model systems (388 views)
J Agric Food Chem (ISSN: 0021-8561), 1999 Nov; 47(11): 4700-4706.
Impact Factor: 1.453
View Export to BibTeX Export to EndNote
Monti SM, Ritieni A, Graziani G, Randazzo G, Mannina L, Segre AL, Fogliano V
LC/MS analysis and antioxidative efficiency of Maillard reaction products from a lactose-lysine model system (499 views)
J Agric Food Chem (ISSN: 0021-8561), 1999 Apr; 47(4): 1506-1513.
Impact Factor: 1.453
View Export to BibTeX Export to EndNote
Fogliano V, Monti SM, Musella T, Randazzo G, Ritieni A
Formation Of Colored Maillard Reaction Products In A Gluten-Glucose Model System (229 views)
Journal Of Agricultural And Food Chemistry, 1999; 66: 293-299.
Impact Factor: 1.453
View Export to BibTeX Export to EndNote
Monti SM, Bailey RG, Ames JM
The influence of pH on the non-volatile reaction products of aqueous Maillard model systems by HPLC with diode array detection (691 views)
Food Chem (ISSN: 0308-8146, 0308-8146print, 0308-8146linking), 1998 Jul; 62(3): 369-375.
Impact Factor: 0.889
View Export to BibTeX Export to EndNote
Nastri F, Lombardi A, D'Andrea LD, Sanseverino M, Maglio O, Pavone V
Miniaturized hemoproteins (423 views)
Biopolymers (ISSN: 0006-3525print, 0006-3525linking, 1097-0282electronic), 1998; 47(1): 5-22.
Impact Factor: 2.086
View Export to BibTeX Export to EndNote
Fogliano V, Monti SM, Ritieni A, Marchisano C, Peluso G, Randazzo G
An immunological approach to monitor protein lactosylation of heated food model systems (348 views)
Food Chem (ISSN: 0308-8146, 0308-8146print), 1997; 58(1-2): 53-58.
Impact Factor: 0.812
View Export to BibTeX Export to EndNote
Bailey RG, Ames JM, Monti SM
An analysis of the non-volatile reaction products of aqueous Maillard model systems at pH 5, using reversed-phase HPLC with diode-array detection (340 views)
Journal Of The Science Of Food And Agriculture (ISSN: 0022-5142), 1996 Sep; 72(1): 103-103.
Impact Factor: 0.895
View Export to BibTeX Export to EndNote
22 Records (21 excluding Abstracts).
Total impact factor: 61.109 (60.214 excluding Abstracts).
Total 5 year impact factor: 60.491 (58.935 excluding Abstracts).
Total impact factor: 61.109 (60.214 excluding Abstracts).
Total 5 year impact factor: 60.491 (58.935 excluding Abstracts).
425 views. Last view on Thursday 16 February 2023, 22:07:59
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