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1
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0034309931
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See, for example: a
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See, for example: a) D. A. Stetsenko, A. A. Arzumanov, V. A. Korshun, M. A. Gait, Mol. Biol. (Moscow) 2000, 34, 852-859;
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Stetsenko, D.A.1
Arzumanov, A.A.2
Korshun, V.A.3
Gait, M.A.4
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2
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0034012647
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b) A. Austriab-Fisher, D. S. Sergueev, M. Fisher, B. S. Ramsay, R. Juliano, Biochem. Pharmacol. 2000, 60, 83-90;
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Biochem. Pharmacol
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Austriab-Fisher, A.1
Sergueev, D.S.2
Fisher, M.3
Ramsay, B.S.4
Juliano, R.5
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4
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0037345795
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T. Nagasaki, T. Myohoji, T. Tachibana, S. Futaki, S. Tamagaki, Bioconjugate Chem. 2003, 14, 282-286.
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Bioconjugate Chem
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Nagasaki, T.1
Myohoji, T.2
Tachibana, T.3
Futaki, S.4
Tamagaki, S.5
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7
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33749823347
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For a recent comprehensive review, see
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For a recent comprehensive review, see: N. Venkatesan, B. H. Kim, Chem. Rev. 2006, 106, 3712-3761.
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Chem. Rev
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Venkatesan, N.1
Kim, B.H.2
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8
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0005114030
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Eds, S. A. Kates, F. Albericio, Marcel Dekker, New York
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a) R. Eritja, Solid-Phase Synthesis, A Practical Guide (Eds.: S. A. Kates, F. Albericio), Marcel Dekker, New York, 2000, pp. 529-548;
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Solid-Phase Synthesis, A Practical Guide
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Eritja, R.1
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9
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57249083948
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b) E. M. Zubin, E. A. Romanova, T. S. Oretskaya, Russ. Chem. Rev. 2002, 71, 239-264;
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Russ. Chem. Rev
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Zubin, E.M.1
Romanova, E.A.2
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23044529377
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c) C. P. Chen, J. M. Min, L. H. Zhang, Prog. Biochem. Biophys. 2001, 28, 783-787;
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Prog. Biochem. Biophys
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Chen, C.P.1
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b) S. M. Ocampo, F. Albericio, I. Fernández, M. Vilaseca, R. Eritja, Org. Lett. 2005, 7, 4349-4352.
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Org. Lett
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Ocampo, S.M.1
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14
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a) Y. Singh, E. Defranc, P. Dumy, J. Org. Chem. 2004, 69, 8544-8546;
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J. Org. Chem
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b) F. A. Rogers, M. Manoharan, P. Rabinovitch, D. C. Ward, P. M. Glazer, Nucleic Acids Res. 2004, 32, 6595-6604.
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Nucleic Acids Res
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Rogers, F.A.1
Manoharan, M.2
Rabinovitch, P.3
Ward, D.C.4
Glazer, P.M.5
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16
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0003918587
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Many transcription factors bind specific DNA sequences as noncovalent homo- or hetero-oligomers, for reviews see: a, Blackwell, Oxford
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Many transcription factors bind specific DNA sequences as noncovalent homo- or hetero-oligomers, for reviews see: a) R. J. White, Gene Transcription, Mechanism and Control, Blackwell, Oxford, 2001;
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(2001)
Gene Transcription, Mechanism and Control
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White, R.J.1
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21
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0842265974
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f) J. T. Kadonaga, Cell 2004, 116, 247-257.
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Cell
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Kadonaga, J.T.1
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22
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0035971506
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a) P. K. Vogt, Oncogene 2001, 20, 2365-2377;
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Oncogene
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Vogt, P.K.1
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24
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0035971433
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The proto-oncoproteins of the Fos and Jun families are prominent members of the basic-leucine zipper (bZIP) DNA-binding family of proteins: a) Y. Chinenov, T. K. Kerppola, Oncogene 2001, 20, 2438-2452;
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The proto-oncoproteins of the Fos and Jun families are prominent members of the basic-leucine zipper (bZIP) DNA-binding family of proteins: a) Y. Chinenov, T. K. Kerppola, Oncogene 2001, 20, 2438-2452;
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26
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0032422295
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a) S. Yao, M. Brickner, E. I. Pares-Matos, J. Chmielewski, Biopolymers 1998, 47, 277-283;
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Biopolymers
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Yao, S.1
Brickner, M.2
Pares-Matos, E.I.3
Chmielewski, J.4
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27
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0030802419
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Recombinant proteins containing a 30-amino-acid acidic extension at the N terminus of the Fos leucine zipper have been shown to be efficient inhibitors of AP-1 DNA binding. b M. Olive, D. Krylov, D. R. Echlin, K. Gardner, E. Taparowsky, C. Vinson, J. Biol. Chem. 1997, 272, 18586-18594.
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Recombinant proteins containing a 30-amino-acid acidic extension at the N terminus of the Fos leucine zipper have been shown to be efficient inhibitors of AP-1 DNA binding. b) M. Olive, D. Krylov, D. R. Echlin, K. Gardner, E. Taparowsky, C. Vinson, J. Biol. Chem. 1997, 272, 18586-18594.
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28
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D. Gottschling, H. Seliger, G. Tarrasón, J. Piulats, R. Eritja, Bioconjugate Chem. 1998, 9, 831.
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(1998)
Bioconjugate Chem
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Gottschling, D.1
Seliger, H.2
Tarrasón, G.3
Piulats, J.4
Eritja, R.5
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29
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34547577127
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For the synthesis of 3b, two additional equivalents of thiol-oligonucleotide 1 were added portionwise in order to ensure total consumption of peptide 2b, since the HPLC retention times of 2b and 3b are similar.
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For the synthesis of 3b, two additional equivalents of thiol-oligonucleotide 1 were added portionwise in order to ensure total consumption of peptide 2b, since the HPLC retention times of 2b and 3b are similar.
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30
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85123225042
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The synthesis of an oligonucleotide-peptide phosphorothioate conjugate incorporating a peptide with 26 amino acids has been reported: M. Antopolsky, U. Tengvall, S. Auriola, I. Jääskeläinen, S. Rönkkö, P. Honkakoshi, A. Urtti, H. Lönnberg, A. Azhayev, Bioconjugate Chem. 1999, 10, 598-606
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The synthesis of an oligonucleotide-peptide phosphorothioate conjugate incorporating a peptide with 26 amino acids has been reported: M. Antopolsky, U. Tengvall, S. Auriola, I. Jääskeläinen, S. Rönkkö, P. Honkakoshi, A. Urtti, H. Lönnberg, A. Azhayev, Bioconjugate Chem. 1999, 10, 598-606.
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31
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0033524453
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The conjugation between a hairpin oligonucleotide and dodecapeptide has been reported: M. A. Zanta, P. Belguise-Valladier, J. P. Behr, Proc. Natl. Acad. Sci. USA 1999, 96, 91-96.
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The conjugation between a hairpin oligonucleotide and dodecapeptide has been reported: M. A. Zanta, P. Belguise-Valladier, J. P. Behr, Proc. Natl. Acad. Sci. USA 1999, 96, 91-96.
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33
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34547574875
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The sample of c-Jun used for the assays was obtained by recombinant methods and consists of the following sequence amino acids 262-324, MKAERKRMRNRIAASKSRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNH
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The sample of c-Jun used for the assays was obtained by recombinant methods and consists of the following sequence (amino acids 262-324): MKAERKRMRNRIAASKSRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNH.
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34
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34547577439
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This dsDNA-peptide derivative was obtained by annealing the oligonucleotide-peptide hybrid 4 with its complementary strand, with 4 being identical to 3b but featuring a different DNA sequence: 5′-GTACGTCTGCATT-3′. This hybrid was prepared by using a similar conjugation protocol to that used in the case of 3a
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This dsDNA-peptide derivative was obtained by annealing the oligonucleotide-peptide hybrid 4 with its complementary strand, with 4 being identical to 3b but featuring a different DNA sequence: 5′-GTACGTCTGCATT-3′. This hybrid was prepared by using a similar conjugation protocol to that used in the case of 3a.
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35
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Although Jun-binding experiments with FOSIz 35aa can not be analyzed by using standard PAGE experiments, the relatively weak interaction of 3b can be considered as a valid control. Preliminary experiments of inhibition of binding of Jun to its consensus DNA sequence confirm that such a truncated peptide is a considerably weaker Jun-trapping agent than our dsDNA-peptide hybrid
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Although Jun-binding experiments with FOSIz 35aa can not be analyzed by using standard PAGE experiments, the relatively weak interaction of 3b can be considered as a valid control. Preliminary experiments of inhibition of binding of Jun to its consensus DNA sequence confirm that such a truncated peptide is a considerably weaker Jun-trapping agent than our dsDNA-peptide hybrid.
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36
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0034732899
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It has been shown that dimeric bZIP proteins can recognize half-site consensus sequences with relative high affinity; this suggests that one of their basic regions can interact with the phosphodiester surface of the DNA in a nonspecific manner: a J. J. Hollenbeck, M. G. Oakley, Bio chemistry 2000, 39, 6380-6389;
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It has been shown that dimeric bZIP proteins can recognize half-site consensus sequences with relative high affinity; this suggests that one of their basic regions can interact with the phosphodiester surface of the DNA in a nonspecific manner: a) J. J. Hollenbeck, M. G. Oakley, Bio chemistry 2000, 39, 6380-6389;
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38
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34547560093
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A method to diagnose single-base-mismatched sequences that relies on the differences in the recognition properties of ss- and ds-DNA has recently been reported: P. C. Ray, Angew. Chem. 2006, 118, 1169-1172;
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A method to diagnose single-base-mismatched sequences that relies on the differences in the recognition properties of ss- and ds-DNA has recently been reported: P. C. Ray, Angew. Chem. 2006, 118, 1169-1172;
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39
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33746309774
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Angew. Chem. Int. Ed. 2006, 45, 1151-1154.
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(2006)
Chem. Int. Ed
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, pp. 1151-1154
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Angew1
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33745728209
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For recent examples on the use of nucleic acid hybridization to control the conformation and activity of proteins, see: a B. Choi, G. Zocchi, J. Am. Chem. Soc. 2006, 128, 8541-8548;
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For recent examples on the use of nucleic acid hybridization to control the conformation and activity of proteins, see: a) B. Choi, G. Zocchi, J. Am. Chem. Soc. 2006, 128, 8541-8548;
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41
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b) L. Röglin, M. R. Ahmadian, O. Seitz, Angew. Chem. 2007, 119, 2759-2763;
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(2007)
Angew. Chem
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, pp. 2759-2763
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Röglin, L.1
Ahmadian, M.R.2
Seitz, O.3
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34250832742
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Angew. Chem. Int. Ed. 2007, 46, 2704-2707.
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(2007)
Chem. Int. Ed
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Angew1
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