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Volumn 171, Issue , 2013, Pages 38-45

UHRF1 discriminates against binding to fully-methylated CpG-Sites by steric repulsion

Author keywords

DNA methylation; Epigenetics; Free energy calculation; Molecular dynamics simulation; Protein DNA interaction

Indexed keywords

CYTOSINE; UBIQUITIN; UBIQUITIN LIKE CONTAINING PHD AND RING FINGER DOMAINS 1; UNCLASSIFIED DRUG;

EID: 84872332138     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2012.10.002     Document Type: Article
Times cited : (14)

References (40)
  • 1
    • 0033753779 scopus 로고    scopus 로고
    • The DNA methyltransferases of mammals
    • T.H. Bestor The DNA methyltransferases of mammals Human Molecular Genetics 9 2000 2395 2402
    • (2000) Human Molecular Genetics , vol.9 , pp. 2395-2402
    • Bestor, T.H.1
  • 2
    • 0037007175 scopus 로고    scopus 로고
    • Beyond Watson and Crick: DNA methylation and molecular enzymology of DNA methyltransferases
    • A. Jeltsch Beyond Watson and Crick: DNA methylation and molecular enzymology of DNA methyltransferases Chembiochem 3 2002 274 293
    • (2002) Chembiochem , vol.3 , pp. 274-293
    • Jeltsch, A.1
  • 3
    • 0347622294 scopus 로고    scopus 로고
    • Targeting DNA methylation in cancer
    • M. Szyf Targeting DNA methylation in cancer Ageing Research Reviews 2 2003 299 328
    • (2003) Ageing Research Reviews , vol.2 , pp. 299-328
    • Szyf, M.1
  • 4
    • 0036144048 scopus 로고    scopus 로고
    • DNA methylation patterns and epigenetic memory
    • A. Bird DNA methylation patterns and epigenetic memory Genes & Development 16 2002 6 21
    • (2002) Genes & Development , vol.16 , pp. 6-21
    • Bird, A.1
  • 8
    • 34347334590 scopus 로고    scopus 로고
    • Biological functions of DNA methyltransferase 1 require its methyltransferase activity
    • M. Damelin, and T.H. Bestor Biological functions of DNA methyltransferase 1 require its methyltransferase activity Molecular and Cellular Biology 27 2007 3891 3899
    • (2007) Molecular and Cellular Biology , vol.27 , pp. 3891-3899
    • Damelin, M.1    Bestor, T.H.2
  • 10
    • 77954383792 scopus 로고    scopus 로고
    • Mechanism of DNA methylation: The double role of DNA as a substrate and as a cofactor
    • R. Zangi, A. Arrieta, and F.P. Cossío Mechanism of DNA methylation: the double role of DNA as a substrate and as a cofactor Journal of Molecular Biology 400 2010 632 644
    • (2010) Journal of Molecular Biology , vol.400 , pp. 632-644
    • Zangi, R.1    Arrieta, A.2    Cossío, F.P.3
  • 13
    • 66349103332 scopus 로고    scopus 로고
    • UHRF1, a modular multi-domain protein, regulates replication-coupled crosstalk between DNA methylation and histone modifications
    • H. Hashimoto, J.R. Horton, X. Zhang, and X. Cheng UHRF1, a modular multi-domain protein, regulates replication-coupled crosstalk between DNA methylation and histone modifications Epigenetics 4 2009 8 14
    • (2009) Epigenetics , vol.4 , pp. 8-14
    • Hashimoto, H.1    Horton, J.R.2    Zhang, X.3    Cheng, X.4
  • 14
    • 70349463160 scopus 로고    scopus 로고
    • Drug discovery targeting epigenetic codes: The great potential of UHRF1, which links DNA methylation and histone modifications, as a drug target in cancers and toxoplasmosis
    • M. Unoki, J. Brunet, and M. Mousli Drug discovery targeting epigenetic codes: the great potential of UHRF1, which links DNA methylation and histone modifications, as a drug target in cancers and toxoplasmosis Biochemical Pharmacology 78 2009 1279 1288
    • (2009) Biochemical Pharmacology , vol.78 , pp. 1279-1288
    • Unoki, M.1    Brunet, J.2    Mousli, M.3
  • 15
    • 7044245474 scopus 로고    scopus 로고
    • ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain
    • M. Unoki, T. Nishidate, and Y. Nakamura ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain Oncogene 23 2004 7601 7610
    • (2004) Oncogene , vol.23 , pp. 7601-7610
    • Unoki, M.1    Nishidate, T.2    Nakamura, Y.3
  • 19
    • 53649097070 scopus 로고    scopus 로고
    • Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism
    • K. Arita, M. Ariyoshi, H. Tochio, Y. Nakamura, and M. Shirakawa Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism Nature 455 2008 818 821
    • (2008) Nature , vol.455 , pp. 818-821
    • Arita, K.1    Ariyoshi, M.2    Tochio, H.3    Nakamura, Y.4    Shirakawa, M.5
  • 22
    • 84869092270 scopus 로고    scopus 로고
    • How to Distinguish methyl-Cytosine from Cytosine with High Fidelity
    • 10.1016/j.jmb.2012.09.024
    • C. Bianchi, and R. Zangi How to Distinguish methyl-Cytosine from Cytosine with High Fidelity Journal of Molecular Biology 424 3-4 December 7, 2012 215 224 10.1016/j.jmb.2012.09.024
    • (2012) Journal of Molecular Biology , vol.424 , Issue.34 , pp. 215-224
    • Bianchi, C.1    Zangi, R.2
  • 24
    • 41849109457 scopus 로고    scopus 로고
    • PREDICTOR: A web-based tool for the prediction of atomic structure from sequence for double helical DNA with up to 150 base pairs
    • J. Farwer, M.J. Packer, and C.A. Hunter PREDICTOR: a web-based tool for the prediction of atomic structure from sequence for double helical DNA with up to 150 base pairs In Silico Biology 7 2007 595 600
    • (2007) Silico Biology , vol.7 , pp. 595-600
    • Farwer, J.1    Packer, M.J.2    Hunter, C.A.3
  • 25
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • J. Wang, P. Cieplak, and P.A. Kollman How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? Journal of Computational Chemistry 21 2000 1049 1074
    • (2000) Journal of Computational Chemistry , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 29
    • 84986516411 scopus 로고
    • Application of the multimolecule and multiconformational RESP methodology to biopolymers: Charge derivation for DNA, RNA, and proteins
    • P. Cieplak, W.D. Cornell, C. Bayly, and P.A. Kollman Application of the multimolecule and multiconformational RESP methodology to biopolymers: charge derivation for DNA, RNA, and proteins Journal of Computational Chemistry 16 1995 1357 1377
    • (1995) Journal of Computational Chemistry , vol.16 , pp. 1357-1377
    • Cieplak, P.1    Cornell, W.D.2    Bayly, C.3    Kollman, P.A.4
  • 31
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N-log(N) method for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald: an N-log(N) method for Ewald sums in large systems The Journal of Chemical Physics 98 1993 10089 10092
    • (1993) The Journal of Chemical Physics , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 34
    • 84986440341 scopus 로고
    • SETTLE: An analytical version of the SHAKE and RATTLE algorithms for rigid water models
    • S. Miyamoto, and P.A. Kollman SETTLE: an analytical version of the SHAKE and RATTLE algorithms for rigid water models Journal of Computational Chemistry 13 1992 952 962
    • (1992) Journal of Computational Chemistry , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 36
    • 0023380976 scopus 로고
    • Thermodynamic cycle integration by computer simulation as a tool for obtaining free energy differences in molecular chemistry
    • W.F. van Gunsteren, and H.J.C. Berendsen Thermodynamic cycle integration by computer simulation as a tool for obtaining free energy differences in molecular chemistry Journal of Computer-Aided Molecular Design 1 1987 171 176
    • (1987) Journal of Computer-Aided Molecular Design , vol.1 , pp. 171-176
    • Van Gunsteren, W.F.1    Berendsen, H.J.C.2
  • 37
    • 1542398220 scopus 로고    scopus 로고
    • Sampling and convergence in free energy calculations of protein-ligand interactions: The binding of triphenoxypyridine derivatives to factor Xa and trypsin
    • A. Villa, R. Zangi, G. Pieffet, and A.E. Mark Sampling and convergence in free energy calculations of protein-ligand interactions: the binding of triphenoxypyridine derivatives to factor Xa and trypsin Journal of Computer-Aided Molecular Design 17 2003 673 686
    • (2003) Journal of Computer-Aided Molecular Design , vol.17 , pp. 673-686
    • Villa, A.1    Zangi, R.2    Pieffet, G.3    Mark, A.E.4
  • 39
    • 10944256336 scopus 로고    scopus 로고
    • Intermolecular potentials of mean force of amino acid side chain interactions in aqueous medium
    • S.A. Hassan Intermolecular potentials of mean force of amino acid side chain interactions in aqueous medium The Journal of Physical Chemistry. B 108 2004 19501 19509
    • (2004) The Journal of Physical Chemistry. B , vol.108 , pp. 19501-19509
    • Hassan, S.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.