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Volumn 25, Issue 5-6, 2011, Pages 219-221

A rapid fluorescence assay for hSMUG1 activity based on modified molecular beacon

Author keywords

HSMUG1; Molecular beacon; Real time

Indexed keywords

HSMUG1 PROTEIN; UNCLASSIFIED DRUG; URACIL DNA GLYCOSIDASE;

EID: 80055106123     PISSN: 08908508     EISSN: 10961194     Source Type: Journal    
DOI: 10.1016/j.mcp.2011.09.001     Document Type: Article
Times cited : (12)

References (11)
  • 1
    • 0033602148 scopus 로고    scopus 로고
    • Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors
    • Haushalter K.A., Todd Stukenberg M.W., Kirschner M.W., Verdine G.L. Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors. Curr Biol 1999, 9:174-185.
    • (1999) Curr Biol , vol.9 , pp. 174-185
    • Haushalter, K.A.1    Todd Stukenberg, M.W.2    Kirschner, M.W.3    Verdine, G.L.4
  • 2
    • 0038771139 scopus 로고    scopus 로고
    • Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1
    • Wibley J.E., Waters T.R., Haushalter K., Verdine G.L., Pearl L.H. Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1. Mol Cell 2003, 11:1647-1659.
    • (2003) Mol Cell , vol.11 , pp. 1647-1659
    • Wibley, J.E.1    Waters, T.R.2    Haushalter, K.3    Verdine, G.L.4    Pearl, L.H.5
  • 3
    • 0035421186 scopus 로고    scopus 로고
    • Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase
    • Nilsen H., Haushalter K.A., Robins P., Barnes D.E., Verdine G.L., Lindahl T. Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase. EMBO J 2001, 20:4278-4286.
    • (2001) EMBO J , vol.20 , pp. 4278-4286
    • Nilsen, H.1    Haushalter, K.A.2    Robins, P.3    Barnes, D.E.4    Verdine, G.L.5    Lindahl, T.6
  • 4
    • 0037509930 scopus 로고    scopus 로고
    • Mammalian 5-formyluracil-DNA glycosylase. 2. role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions
    • Masaoka A., Matsubara M., Hasegawa R., Tanaka T., Kurisu S., Terato H., et al. Mammalian 5-formyluracil-DNA glycosylase. 2. role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions. Biochemistry 2003, 42:5003-5012.
    • (2003) Biochemistry , vol.42 , pp. 5003-5012
    • Masaoka, A.1    Matsubara, M.2    Hasegawa, R.3    Tanaka, T.4    Kurisu, S.5    Terato, H.6
  • 5
    • 0033636312 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase (UNG)-deficient mice reveal a primary role of the enzyme during DNA replication
    • Nilsen H., Rosewell I., Robins P., Skjelbred C.F., Andersen S., Slupphaug G., et al. Uracil-DNA glycosylase (UNG)-deficient mice reveal a primary role of the enzyme during DNA replication. Mol Cell 2000, 5:1059-1065.
    • (2000) Mol Cell , vol.5 , pp. 1059-1065
    • Nilsen, H.1    Rosewell, I.2    Robins, P.3    Skjelbred, C.F.4    Andersen, S.5    Slupphaug, G.6
  • 6
    • 21844464297 scopus 로고    scopus 로고
    • C--T mutagenesis and gamma-radiation sensitivity due to deficiency in the Smug1 and Ung DNA glycosylases
    • An Q., Robins P., Lindahl T., Barnes D.E. C--T mutagenesis and gamma-radiation sensitivity due to deficiency in the Smug1 and Ung DNA glycosylases. EMBO J 2005, 24:2205-2213.
    • (2005) EMBO J , vol.24 , pp. 2205-2213
    • An, Q.1    Robins, P.2    Lindahl, T.3    Barnes, D.E.4
  • 7
    • 0142092610 scopus 로고    scopus 로고
    • Human uracil-DNA glycosylase deficiency associated with profoundly impaired immunoglobulin class-switch recombination
    • Imai K., Slupphaug G., Lee W.I., Revy P., Nonoyama S., Catalan N., et al. Human uracil-DNA glycosylase deficiency associated with profoundly impaired immunoglobulin class-switch recombination. Nat Immunol 2003, 4:1023-1028.
    • (2003) Nat Immunol , vol.4 , pp. 1023-1028
    • Imai, K.1    Slupphaug, G.2    Lee, W.I.3    Revy, P.4    Nonoyama, S.5    Catalan, N.6
  • 8
    • 0035883852 scopus 로고    scopus 로고
    • A kinetic analysis of substrate recognition by uracil-DNA glycosylase from herpes simplex virus type 1
    • Bellamy S.R., Baldwin G.S. A kinetic analysis of substrate recognition by uracil-DNA glycosylase from herpes simplex virus type 1. Nucleic Acids Res 2001, 29:3857-3863.
    • (2001) Nucleic Acids Res , vol.29 , pp. 3857-3863
    • Bellamy, S.R.1    Baldwin, G.S.2
  • 9
    • 34247148838 scopus 로고    scopus 로고
    • A rapid reaction analysis of uracil DNA glycosylase indicates an active mechanism of base flipping
    • Bellamy S.R., Krusong K., Baldwin G.S. A rapid reaction analysis of uracil DNA glycosylase indicates an active mechanism of base flipping. Nucleic Acids Res 2007, 35:1478-1487.
    • (2007) Nucleic Acids Res , vol.35 , pp. 1478-1487
    • Bellamy, S.R.1    Krusong, K.2    Baldwin, G.S.3
  • 10
    • 34250338508 scopus 로고    scopus 로고
    • Real-time monitoring excision of uracil based on double-stranded probes
    • Liu B., Yang X., Wang K., Tan W., Tang H. Real-time monitoring excision of uracil based on double-stranded probes. Anal Biochem 2007, 366:237-243.
    • (2007) Anal Biochem , vol.366 , pp. 237-243
    • Liu, B.1    Yang, X.2    Wang, K.3    Tan, W.4    Tang, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.