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Volumn 589, Issue 2, 2005, Pages 103-110

Lead toxicity through the leadzyme

Author keywords

Catalytic RNA; Lead; Leadzyme; RNA; tRNA

Indexed keywords

LEAD; MESSENGER RNA;

EID: 15944366181     PISSN: 13835742     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrrev.2004.11.002     Document Type: Review
Times cited : (27)

References (37)
  • 1
    • 0344845177 scopus 로고    scopus 로고
    • Facilitative mechanisms of lead as a carcinogen
    • E.K. Silbergeld Facilitative mechanisms of lead as a carcinogen Mutat. Res. 533 2003 121 133
    • (2003) Mutat. Res. , vol.533 , pp. 121-133
    • Silbergeld, E.K.1
  • 9
    • 0033612767 scopus 로고    scopus 로고
    • 2+ binding to structural zinc-binding domains determined directly by monitoring lead-thiolate charge-transfer bands
    • 2+ binding to structural zinc-binding domains determined directly by monitoring lead-thiolate charge-transfer bands J. Am. Chem. Soc. 121 1999 6850 6855
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 6850-6855
    • Payne, J.C.1    Horst, M.A.2    Godwin, H.A.3
  • 10
    • 0022433369 scopus 로고
    • Crystallographic and biochemical investigation of the lead(II)-catalyzed hydrolysis of yeast phenylalanine tRNA
    • R.S. Brown, J.C. Devan, and A. Klug Crystallographic and biochemical investigation of the lead(II)-catalyzed hydrolysis of yeast phenylalanine tRNA Biochemistry 24 1985 4785 4801
    • (1985) Biochemistry , vol.24 , pp. 4785-4801
    • Brown, R.S.1    Devan, J.C.2    Klug, A.3
  • 12
    • 0033862354 scopus 로고    scopus 로고
    • The crystal structure of yeast phenylalanine tRNA at 1.93 Å resolution: A classic structure revisited
    • H. Shi, and P.B. Moore The crystal structure of yeast phenylalanine tRNA at 1.93 Å resolution: a classic structure revisited RNA 6 2000 1091 1105
    • (2000) RNA , vol.6 , pp. 1091-1105
    • Shi, H.1    Moore, P.B.2
  • 13
    • 0027994489 scopus 로고
    • Aminoacyl-tRNAs. Diversity before and unity after interaction with EF-Tu:GTP
    • J. Barciszewski, M. Sprinzl, and B.F.C. Clark Aminoacyl-tRNAs. Diversity before and unity after interaction with EF-Tu:GTP FEBS Lett. 351 1994 137 139
    • (1994) FEBS Lett. , vol.351 , pp. 137-139
    • Barciszewski, J.1    Sprinzl, M.2    Clark, B.F.C.3
  • 14
    • 0036863325 scopus 로고    scopus 로고
    • Ribozymes, the first 20 years
    • T.R. Cech Ribozymes, the first 20 years Biochem. Soc. Trans. 30 2002 1162 1166
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 1162-1166
    • Cech, T.R.1
  • 15
    • 0346100705 scopus 로고    scopus 로고
    • RNA processing: A postdoc in a great laboratory
    • S. Altman RNA processing: a postdoc in a great laboratory Genetics 165 2003 1633 1639
    • (2003) Genetics , vol.165 , pp. 1633-1639
    • Altman, S.1
  • 16
    • 0028675028 scopus 로고
    • A DNA enzyme that cleaves RNA
    • R.R. Breaker, and G.F. Joyce A DNA enzyme that cleaves RNA Chem. Biol. 1 1994 223 229
    • (1994) Chem. Biol. , vol.1 , pp. 223-229
    • Breaker, R.R.1    Joyce, G.F.2
  • 18
    • 0038131065 scopus 로고    scopus 로고
    • A lead-dependent DNAzyme with a two-step mechanism
    • A.K. Brown, J. Li, C.M.-B. Pavot, and Y. Lu A lead-dependent DNAzyme with a two-step mechanism Biochemistry 42 2003 7152 7161
    • (2003) Biochemistry , vol.42 , pp. 7152-7161
    • Brown, A.K.1    Li, J.2    Pavot, C.M.-B.3    Lu, Y.4
  • 19
    • 0034719109 scopus 로고    scopus 로고
    • Adenine protonation in domain B of the hairpin ribozyme
    • S. Ravindranathan, S.E. Butcher, and J. Feigon Adenine protonation in domain B of the hairpin ribozyme Biochemistry 39 2000 16026 16032
    • (2000) Biochemistry , vol.39 , pp. 16026-16032
    • Ravindranathan, S.1    Butcher, S.E.2    Feigon, J.3
  • 20
    • 0036601149 scopus 로고    scopus 로고
    • The role of metal ions in RNA catalysis
    • M.J. Fedor The role of metal ions in RNA catalysis Curr. Opin. Struct. Biol. 12 2002 289 295
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 289-295
    • Fedor, M.J.1
  • 24
    • 0026669321 scopus 로고
    • A small metalloribozyme with a two-step mechanism
    • T. Pan, and O. Uhlenbeck A small metalloribozyme with a two-step mechanism Nature 358 1992 560 563
    • (1992) Nature , vol.358 , pp. 560-563
    • Pan, T.1    Uhlenbeck, O.2
  • 26
    • 0344874278 scopus 로고    scopus 로고
    • Less isn't always more
    • O.C. Uhlenbeck Less isn't always more RNA 9 2003 1415 1417
    • (2003) RNA , vol.9 , pp. 1415-1417
    • Uhlenbeck, O.C.1
  • 28
    • 0031860104 scopus 로고    scopus 로고
    • Crystallographic structures of the hammerhead ribozyme: Relationship to ribozyme folding and catalysis
    • J.E. Wedekind, and D.B. McKay Crystallographic structures of the hammerhead ribozyme: relationship to ribozyme folding and catalysis Ann. Rev. Biophys. Biomol. Struct. 27 1998 475 502
    • (1998) Ann. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 475-502
    • Wedekind, J.E.1    McKay, D.B.2
  • 29
    • 0033010809 scopus 로고    scopus 로고
    • Crystal structure of a lead-dependent ribozyme revealind metal binding sites relevant to catalysis
    • J.E. Wedekind, and D.B. McKay Crystal structure of a lead-dependent ribozyme revealind metal binding sites relevant to catalysis Nat. Strut. Biol. 6 1999 261 267
    • (1999) Nat. Strut. Biol. , vol.6 , pp. 261-267
    • Wedekind, J.E.1    McKay, D.B.2
  • 30
    • 0034664076 scopus 로고    scopus 로고
    • Active site dynamics in the lead-dependent ribozyme
    • C.G. Hoogstraten, J.R. Wank, and A. Pardi Active site dynamics in the lead-dependent ribozyme Biochemistry 39 2000 9951 9958
    • (2000) Biochemistry , vol.39 , pp. 9951-9958
    • Hoogstraten, C.G.1    Wank, J.R.2    Pardi, A.3
  • 31
    • 0041464604 scopus 로고    scopus 로고
    • Crystal structure of the leadzyme at 1.8 Å resolution: Metal ion binding and the implications for catalytic mechanism and allo site ion regulation
    • J.E. Wedekind, and D.B. McKay Crystal structure of the leadzyme at 1.8 Å resolution: metal ion binding and the implications for catalytic mechanism and allo site ion regulation Biochemistry 42 2003 9554 9563
    • (2003) Biochemistry , vol.42 , pp. 9554-9563
    • Wedekind, J.E.1    McKay, D.B.2
  • 32
    • 0032534641 scopus 로고    scopus 로고
    • Effect of substrate RNA sequence on the cleavage reaction by a short ribozyme
    • T. Ohmichi, Y. Okumoto, and N. Sugimoto Effect of substrate RNA sequence on the cleavage reaction by a short ribozyme Nucleic Acids Res. 26 1998 5655 5661
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5655-5661
    • Ohmichi, T.1    Okumoto, Y.2    Sugimoto, N.3
  • 36
    • 0035162594 scopus 로고    scopus 로고
    • RefSeq and LocusLink: NCBI gene-centered resources
    • K.D. Pruitt, and D.R. Maglott RefSeq and LocusLink: NCBI gene-centered resources Nucleic Acids Res. 29 2001 137 140
    • (2001) Nucleic Acids Res. , vol.29 , pp. 137-140
    • Pruitt, K.D.1    Maglott, D.R.2
  • 37
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • D.H. Mathews, J. Sabina, M. Zuker, and D.H. Turner Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure J. Mol. Biol. 288 1999 911 940
    • (1999) J. Mol. Biol. , vol.288 , pp. 911-940
    • Mathews, D.H.1    Sabina, J.2    Zuker, M.3    Turner, D.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.