메뉴 건너뛰기




Volumn 50, Issue 10, 2011, Pages 1590-1598

Mutations that probe the cooperative assembly of O6- alkylguanine-DNA alkyltransferase complexes

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLATING AGENTS; ALKYLTRANSFERASE; CO-OPERATIVE ASSEMBLY; COOPERATIVITY; DNA BINDING; PROTEIN MOLECULES; PROTEIN-DNA INTERACTIONS; PROTEIN-PROTEIN INTERACTIONS; PROTEIN-PROTEIN INTERFACE; WILD-TYPE CELLS; WILD-TYPE PROTEINS;

EID: 79952408590     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101970d     Document Type: Article
Times cited : (13)

References (47)
  • 1
    • 0014672640 scopus 로고
    • 6 alkylation of dexoyguanosine to the mutagenicity and carcinogenicity of nitrosamines and nitrosamides
    • 6 alkylation of dexoyguanosine to the mutagenicity and carcinogenicity of nitrosamines and nitrosamides Nature 223, 206-207
    • (1969) Nature , vol.223 , pp. 206-207
    • Loveless, A.1
  • 2
    • 0023223806 scopus 로고
    • Do carcinogen-modified deoxynucleotide precursors contribute to cellular mutagenesis?
    • Snow, E. T. and Mitra, S. (1987) Do carcinogen-modified deoxynucleotide precursors contribute to cellular mutagenesis? Cancer Invest. 5, 119-125 (Pubitemid 17124472)
    • (1987) Cancer Investigation , vol.5 , Issue.2 , pp. 119-125
    • Snow, E.T.1    Mitra, S.2
  • 3
    • 0025195404 scopus 로고
    • 6-alkylguanine-DNA alkyltransferase: Regulation and importance in response to alkylating carcinogenic and therapeutic agents
    • 6-alkylguanine-DNA alkyltransferase: Regulation and importance in response to alkylating carcinogens and therapeutic agents Cancer Res. 50, 6119-6129 (Pubitemid 20323662)
    • (1990) Cancer Research , vol.50 , Issue.19 , pp. 6119-6129
    • Pegg, A.E.1
  • 4
    • 0036006173 scopus 로고    scopus 로고
    • 6-alkylguanine-DNA alkyltransferase: Role in carcinogenesis and chemotherapy
    • DOI 10.1002/bies.10063
    • 6-Alkylguanine-DNA alkyltransferase: Role in carcinogenesis and chemotherapy BioEssays 24, 255-266 (Pubitemid 34248691)
    • (2002) BioEssays , vol.24 , Issue.3 , pp. 255-266
    • Margison, G.P.1    Santibanez-Koref, M.F.2
  • 5
    • 0036570062 scopus 로고    scopus 로고
    • Clinical relevance of MGMT in the treatment of cancer
    • DOI 10.1200/JCO.2002.06.110
    • Gerson, S. L. (2002) Clinical relevance of MGMT in the treatment of cancer J. Clin. Oncol. 20, 2388-2399 (Pubitemid 34441669)
    • (2002) Journal of Clinical Oncology , vol.20 , Issue.9 , pp. 2388-2399
    • Gerson, S.L.1
  • 7
    • 31544464704 scopus 로고    scopus 로고
    • Targeted modulation of MGMT: Clinical implications
    • DOI 10.1158/1078-0432.CCR-05-2543
    • Liu, L. and Gerson, S. L. (2006) Targeted modulation of MGMT: Clinical implications Clin. Cancer Res. 12, 328-331 (Pubitemid 43166117)
    • (2006) Clinical Cancer Research , vol.12 , Issue.2 , pp. 328-331
    • Liu, L.1    Gerson, S.L.2
  • 9
    • 51649117107 scopus 로고    scopus 로고
    • 6-methylguanine methyltransferase (MGMT) promoter methylation with clinical outcomes in glioblastoma and clinical strategies to modulate MGMT activity
    • 6- methylguanine methyltransferase (MGMT) promoter methylation with clinical outcomes in glioblastoma and clinical strategies to modulate MGMT activity J. Clin. Oncol. 26, 4189-4199
    • (2008) J. Clin. Oncol. , vol.26 , pp. 4189-4199
    • Hegi, M.E.1    Liu, L.2    Herman, J.G.3    Stupp, R.4    Wick, W.5    Weller, M.6    Mehta, M.P.7    Gilbert, M.R.8
  • 12
    • 34447323281 scopus 로고    scopus 로고
    • 6-alkylguanine-DNA alkyltransferase and its implications for cancer chemotherapy
    • DOI 10.1016/j.dnarep.2007.03.011, PII S1568786407001280
    • 6-alkylguanine-DNA alkyltransferase and its implications for cancer chemotherapy DNA Repair 6, 1100-1115 (Pubitemid 47058393)
    • (2007) DNA Repair , vol.6 , Issue.8 , pp. 1100-1115
    • Tubbs, J.L.1    Pegg, A.E.2    Tainer, J.A.3
  • 13
    • 0025194773 scopus 로고
    • 6-alkylguanine-DNA alkyltransferases
    • 6-alkylguanine-DNA alkyltransferases Mutat. Res. 233, 165-175
    • (1990) Mutat. Res. , vol.233 , pp. 165-175
    • Pegg, A.E.1
  • 17
    • 20544455000 scopus 로고    scopus 로고
    • The structure of the human AGT protein bound to DNA and its implications for damage detection
    • DOI 10.1016/j.jmb.2005.05.028, PII S0022283605005711
    • Duguid, E. M., Rice, P. A., and He, C. (2005) The Structure of the Human AGT Protein Bound to DNA and its Implications for Damage Detection J. Mol. Biol. 350, 657-666 (Pubitemid 40848665)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.4 , pp. 657-666
    • Duguid, E.M.1    Rice, P.A.2    He, C.3
  • 19
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • DOI 10.1093/nar/25.17.3389
    • Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J. (1997) Gapped BLAST and PSI-BLAST: A new generation of protein database search programs Nucleic Acids Res. 25, 3389-3402 (Pubitemid 27359211)
    • (1997) Nucleic Acids Research , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 21
    • 33847217198 scopus 로고    scopus 로고
    • Suppression of protein interactions by arginine: A proposed mechanism of the arginine effects
    • Arakawa, T., Ejima, D., Tsumoto, K., Obeyama, N., Tanaka, Y., Kita, Y., and Timasheff, S. N. (2007) Suppression of protein interactions by arginine: A proposed mechanism of the arginine effects Biophys. Chem. 127, 1-8
    • (2007) Biophys. Chem. , vol.127 , pp. 1-8
    • Arakawa, T.1    Ejima, D.2    Tsumoto, K.3    Obeyama, N.4    Tanaka, Y.5    Kita, Y.6    Timasheff, S.N.7
  • 22
    • 0037424237 scopus 로고    scopus 로고
    • 6-alkylguanine-DNA alkyltransferase: Effects of protein and DNA alkylation on complex stability
    • DOI 10.1074/jbc.M211854200
    • 6-alkylguanine-DNA alkyltransferase. Effects of protein and DNA alkylation on complex stability J. Biol. Chem. 278, 7973-7980 (Pubitemid 36800535)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 7973-7980
    • Rasimas, J.J.1    Pegg, A.E.2    Fried, M.G.3
  • 24
    • 0016175370 scopus 로고
    • Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice
    • McGhee, J. and von Hippel, P. H. (1974) Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice J. Mol. Biol. 86, 469-489
    • (1974) J. Mol. Biol. , vol.86 , pp. 469-489
    • McGhee, J.1    Von Hippel, P.H.2
  • 25
    • 0034815433 scopus 로고    scopus 로고
    • Analytic binding isotherms describing competitive interactions of a protein ligand with specific and nonspecific sites on the same DNA oligomer
    • Tsodikov, O. V., Holbrook, J. A., Shkel, I. A., and Record, M. T., Jr. (2001) Analytic binding isotherms describing competitive interactions of a protein ligand with specific and nonspecific sites on the same DNA oligomer Biophys. J. 81, 1960-1969 (Pubitemid 32917148)
    • (2001) Biophysical Journal , vol.81 , Issue.4 , pp. 1960-1969
    • Tsodikov, O.V.1    Holbrook, J.A.2    Shkel, I.A.3    Record Jr., M.T.4
  • 26
    • 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 circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set Anal. Biochem. 287, 252-260 (Pubitemid 32006234)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 27
    • 1642546383 scopus 로고    scopus 로고
    • Computation and Analysis of Protein Circular Dichroism Spectra
    • DOI 10.1016/S0076-6879(04)83013-1
    • Sreerama, N. and Woody, R. W. (2004) Computation and analysis of protein circular dichroism spectra Methods Enzymol. 383, 318-351 (Pubitemid 38401795)
    • (2004) Methods in Enzymology , vol.383 , pp. 318-351
    • Sreerama, N.1    Woody, R.W.2
  • 28
    • 1842428822 scopus 로고    scopus 로고
    • Calculating Sedimentation Coefficient Distributions by Direct Modeling of Sedimentation Velocity Concentration Profiles
    • DOI 10.1016/S0076-6879(04)84012-6
    • Dam, J. and Schuck, P. (2004) Calculating sedimentation coefficient distributions by direct modeling of sedimentation velocity concentration profiles Methods Enzymol. 384, 185-212 (Pubitemid 38420481)
    • (2004) Methods in Enzymology , vol.384 , pp. 185-212
    • Dam, J.1    Schuck, P.2
  • 29
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. (2000) Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling Biophys. J. 78, 1606-1619 (Pubitemid 30141584)
    • (2000) Biophysical Journal , vol.78 , Issue.3 , pp. 1606-1619
    • Schuck, P.1
  • 30
    • 0002498995 scopus 로고
    • Computer-Aided Interpretation of Analytical Sedimentation Data for Proteins
    • Harding S.E. Rowe A.J. Horton J.C. In (, Eds.) pp - 125, The Royal Society of Chemistry, Cambridge, England.
    • Laue, T. M., Shah, B. D., Ridgeway, T. M., and Pelletier, S. L. (1992) Computer-Aided Interpretation of Analytical Sedimentation Data For Proteins. In Analytical Ultracentrifugation in Biochemistry and Polymer Science (Harding, S. E., Rowe, A. J., and Horton, J. C., Eds.) pp 90 - 125, The Royal Society of Chemistry, Cambridge, England.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 31
    • 0028979534 scopus 로고
    • Mutations in the Ada O6-alkylguanine-DNA alkyltransferase conferring sensitivity to inactivation by O6-benzylguanine and 2,4-diamino-6-benzyloxy-5- nitrosopyrimidine
    • Crone, T. M., Kanugula, S., and Pegg, A. E. (1995) Mutations in the Ada O6-alkylguanine-DNA alkyltransferase conferring sensitivity to inactivation by O6-benzylguanine and 2,4-diamino-6-benzyloxy-5-nitrosopyrimidine Carcinogenesis 16, 1687-1692
    • (1995) Carcinogenesis , vol.16 , pp. 1687-1692
    • Crone, T.M.1    Kanugula, S.2    Pegg, A.E.3
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0019551730 scopus 로고
    • "Western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette, W. N. (1981) "Western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A Anal. Biochem. 112, 195-203
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 38
    • 24944516963 scopus 로고    scopus 로고
    • An experiment-based algorithm for predicting the partitioning of unfolded peptides into phosphatidylcholine bilayer interfaces
    • DOI 10.1021/bi051193b
    • Hristova, K. and White, S. H. (2005) An experiment-based algorithm for predicting the partitioning of unfolded peptides into phosphatidylcholine bilayer interfaces Biochemistry 44, 12614-12619 (Pubitemid 41324352)
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12614-12619
    • Hristova, K.1    White, S.H.2
  • 39
    • 0024553005 scopus 로고
    • Effect of the substitution Ala → Gly at each of five residue positions in the C-peptide helix
    • DOI 10.1021/bi00431a025
    • Strehlow, K. G. and Baldwin, R. L. (1989) Effect of the substitution Ala → Gly at each of five residue positions in the C-peptide helix Biochemistry 28, 2130-2133 (Pubitemid 19084440)
    • (1989) Biochemistry , vol.28 , Issue.5 , pp. 2130-2133
    • Strehlow, K.G.1    Baldwin, R.L.2
  • 40
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neill, K. T. and Degrado, W. F. (1990) A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids Science 250, 646-651
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neill, K.T.1    Degrado, W.F.2
  • 44
    • 0029561532 scopus 로고
    • Comparison of protein binding to DNA in vivo and in vitro: Defining an effective intracellular target
    • Yang, S. W. and Nash, H. A. (1995) Comparison of protein binding to DNA in vivo and in vitro: Defining an effective intracellular target EMBO J. 14, 6292-6300 (Pubitemid 26007315)
    • (1995) EMBO Journal , vol.14 , Issue.24 , pp. 6292-6300
    • Yang, S.-W.1    Nash, H.A.2
  • 45
    • 0029085907 scopus 로고
    • Electrostatic Mechanism of Nucleosome Spacing
    • Blank, T. A. and Becker, P. B. (1995) Electrostatic Mechanism of Nucleosome Spacing J. Mol. Biol. 252, 305-313
    • (1995) J. Mol. Biol. , vol.252 , pp. 305-313
    • Blank, T.A.1    Becker, P.B.2
  • 46
    • 21844436803 scopus 로고    scopus 로고
    • X-ray structure of a tetranucleosome and its implications for the chromatin fibre
    • DOI 10.1038/nature03686
    • Schalch, T., Duda, S., Sargent, D. F., and Richmond, T. J. (2005) X-ray structure of a tetranucleosome and its implications for the chromatin fibre Nature 436, 138-141 (Pubitemid 40966200)
    • (2005) Nature , vol.436 , Issue.7047 , pp. 138-141
    • Schalch, T.1    Duda, S.2    Sargent, D.F.3    Richmond, T.J.4
  • 47
    • 70349696256 scopus 로고    scopus 로고
    • On the analysis of sedimentation velocity in the study of protein complexes
    • Brown, P. H., Balbo, A., and Schuck, P. (2009) On the analysis of sedimentation velocity in the study of protein complexes Eur. Biophys. J. 38, 1079-1099
    • (2009) Eur. Biophys. J. , vol.38 , pp. 1079-1099
    • Brown, P.H.1    Balbo, A.2    Schuck, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.