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Volumn 12, Issue 27, 2014, Pages 4890-4904

Enthalpy-driven nuclease-like activity and mechanism of peptide-chlorambucil conjugates

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CHEMICAL ATTACK; DNA; ELECTROPHORESIS; ENTHALPY; MASS SPECTROMETRY; POLYACRYLATES;

EID: 84902804069     PISSN: 14770520     EISSN: None     Source Type: Journal    
DOI: 10.1039/c4ob00123k     Document Type: Article
Times cited : (5)

References (28)
  • 2
    • 0030198135 scopus 로고    scopus 로고
    • Optimizing the targeted chemical nuclease activity of 1,10-phenanthroline-copper by ligand modification
    • J. Gallagher C.-H. B. Chen C. Q. Pan D. M. Perrin Y. M. Cho D. S. Sigman Optimizing the targeted chemical nuclease activity of 1,10-phenanthroline-copper by ligand modification Bioconjugate Chem. 1996 7 413 420
    • (1996) Bioconjugate Chem. , vol.7 , pp. 413-420
    • Gallagher, J.1    Chen, C.-H.B.2    Pan, C.Q.3    Perrin, D.M.4    Cho, Y.M.5    Sigman, D.S.6
  • 3
    • 0022693818 scopus 로고
    • Design of sequence-specific DNA-binding molecules
    • P. B. Dervan Design of sequence-specific DNA-binding molecules Science 1986 232 464 471
    • (1986) Science , vol.232 , pp. 464-471
    • Dervan, P.B.1
  • 4
    • 0021246367 scopus 로고
    • Distamycin and penta-N-methylpyrrolecarboxamide binding sites on native DNA. A comparison of methidiumpropyl-EDTA-Fe(II) footprinting and DNA affinity cleaving
    • P. G. Schultz P. B. Dervan Distamycin and penta-N- methylpyrrolecarboxamide binding sites on native DNA. A comparison of methidiumpropyl-EDTA-Fe(II) footprinting and DNA affinity cleaving J. Biomol. Struct. Dyn. 1984 1 1133 1147
    • (1984) J. Biomol. Struct. Dyn. , vol.1 , pp. 1133-1147
    • Schultz, P.G.1    Dervan, P.B.2
  • 7
    • 80052202732 scopus 로고    scopus 로고
    • DNA cleavage activity of Fe(II)N4Py under photo irradiation in the presence of 1,8-Naphthalimide and 9-Aminoacridine: Unexpected effects of reactive oxygen species scavengers
    • Q. Qian Li W. R. Browne G. Roelfes DNA cleavage activity of Fe(II)N4Py under photo irradiation in the presence of 1,8-Naphthalimide and 9-Aminoacridine: Unexpected effects of reactive oxygen species scavengers Inorg. Chem. 2011 50 8318 8325
    • (2011) Inorg. Chem. , vol.50 , pp. 8318-8325
    • Qian Li, Q.1    Browne, W.R.2    Roelfes, G.3
  • 10
    • 0029111589 scopus 로고
    • Synthesis, DNA binding, and sequence specificity of DNA alkylation by some novel cyclic peptide-chlorambucil conjugates
    • L. Sheh H. W. Chang C. W. Ong S. L. Chen C. Bailly R. C. M. Linssen M. J. Waring Synthesis, DNA binding, and sequence specificity of DNA alkylation by some novel cyclic peptide-chlorambucil conjugates Anti-Cancer Drug Des. 1995 10 373 388
    • (1995) Anti-Cancer Drug Des. , vol.10 , pp. 373-388
    • Sheh, L.1    Chang, H.W.2    Ong, C.W.3    Chen, S.L.4    Bailly, C.5    Linssen, R.C.M.6    Waring, M.J.7
  • 11
    • 0035206945 scopus 로고    scopus 로고
    • Sequence-specific DNA cleavage by dipeptides disubstituted with chlorambucil and 2,6-dimethoxyhydroquinone-3-mercaptoacetic acid
    • A. Minnock L. S. Lin J. Morgan S. D. G. Crow M. J. Waring L. Sheh Sequence-specific DNA cleavage by dipeptides disubstituted with chlorambucil and 2,6-dimethoxyhydroquinone-3-mercaptoacetic acid Bioconjugate Chem. 2001 12 870 882
    • (2001) Bioconjugate Chem. , vol.12 , pp. 870-882
    • Minnock, A.1    Lin, L.S.2    Morgan, J.3    Crow, S.D.G.4    Waring, M.J.5    Sheh, L.6
  • 17
    • 84870512292 scopus 로고    scopus 로고
    • ed. J. A. McEvoy, Nova Science Publishers Inc., New York, ISBN 978-1-61122-734-5, open access available
    • J. T. B. Huang, R. C. K. Yang, W. K. Hung, M. J. Waring and L. Sheh, in Molecular Recognition, ed., J. A. McEvoy, Nova Science Publishers Inc., New York, ISBN 978-1-61122-734-5, 2011, open access available
    • (2011) Molecular Recognition
    • Huang, J.T.B.1    Yang, R.C.K.2    Hung, W.K.3    Waring, M.J.4    Sheh, L.5
  • 20
    • 0024357657 scopus 로고
    • The structure of tumor necrosis factor-α at 2.6 Angstrom resolution
    • reference quoted therein
    • M. J. Eck S. Sprang The structure of tumor necrosis factor-α at 2.6 Angstrom resolution J. Biol. Chem. 1989 264 17595 17605
    • (1989) J. Biol. Chem. , vol.264 , pp. 17595-17605
    • Eck, M.J.1    Sprang, S.2
  • 21
    • 0035393302 scopus 로고    scopus 로고
    • Amino acid-base interactions: A three dimensional analysis of protein-DNA interactions at an atomic level
    • N. M. Luscombe R. A. Laskowski J. M. Thornton Amino acid-base interactions: a three dimensional analysis of protein-DNA interactions at an atomic level Nucleic Acids Res. 2001 29 2860 2874
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2860-2874
    • Luscombe, N.M.1    Laskowski, R.A.2    Thornton, J.M.3
  • 25
    • 79951876264 scopus 로고    scopus 로고
    • Transition state analysis of the arsenolytic depyrimidination of thymidine by human thymidine phosphorylase
    • P. A. Schwartz M. J. Verticatt V. L. Schramm Transition state analysis of the arsenolytic depyrimidination of thymidine by human thymidine phosphorylase Biochemistry 2011 50 1412 1420
    • (2011) Biochemistry , vol.50 , pp. 1412-1420
    • Schwartz, P.A.1    Verticatt, M.J.2    Schramm, V.L.3
  • 27
    • 17844406392 scopus 로고    scopus 로고
    • Induced fit and the entropy of structural adaptation in the complexation of CAP and λ-repressor with cognate DNA sequence
    • S. B. Dixit D. Q. Andrews D. L. Beveridge Induced fit and the entropy of structural adaptation in the complexation of CAP and λ-repressor with cognate DNA sequence Biophys. J. 2005 88 3147 3157
    • (2005) Biophys. J. , vol.88 , pp. 3147-3157
    • Dixit, S.B.1    Andrews, D.Q.2    Beveridge, D.L.3
  • 28
    • 10944261243 scopus 로고    scopus 로고
    • Understanding noncovalent interactions: Ligand binding energy and catalytic efficiency from ligand-induced reductions in motions within receptors and enzymes
    • references cited therein
    • D. H. Williams E. Stephens D. P. O'Brien M. Zhou Understanding noncovalent interactions: ligand binding energy and catalytic efficiency from ligand-induced reductions in motions within receptors and enzymes Angew. Chem., Int. Ed. 2004 43 6596 6616
    • (2004) Angew. Chem., Int. Ed. , vol.43 , pp. 6596-6616
    • Williams, D.H.1    Stephens, E.2    O'Brien, D.P.3    Zhou, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.