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Volumn 12, Issue 11, 2005, Pages 1221-1226

Ligand Requirements for glmS Ribozyme Self-Cleavage (DOI:10.1016/j.chembiol.2005.09.006);Ligand requirements for glmS ribozyme self-cleavage

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Indexed keywords

PROKARYOTA;

EID: 27744525243     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2006.06.003     Document Type: Erratum
Times cited : (128)

References (24)
  • 1
    • 0031711821 scopus 로고    scopus 로고
    • Ribonuclease P: Unity and diversity in a tRNA processing ribozyme
    • D.N. Frank, and N.R. Pace Ribonuclease P: unity and diversity in a tRNA processing ribozyme Annu. Rev. Biochem. 67 1998 153 180
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 153-180
    • Frank, D.N.1    Pace, N.R.2
  • 2
    • 0037062949 scopus 로고    scopus 로고
    • The chemical repertoire of natural ribozymes
    • J.A. Doudna, and T.R. Cech The chemical repertoire of natural ribozymes Nature 418 2002 222 228
    • (2002) Nature , vol.418 , pp. 222-228
    • Doudna, J.A.1    Cech, T.R.2
  • 3
    • 0043268903 scopus 로고    scopus 로고
    • The structural basis of large ribosomal subunit function
    • P.B. Moore, and T.A. Steitz The structural basis of large ribosomal subunit function Annu. Rev. Biochem. 72 2003 813 850
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 813-850
    • Moore, P.B.1    Steitz, T.A.2
  • 4
    • 0032192761 scopus 로고    scopus 로고
    • The hammerhead, hairpin and VS ribozymes are catalytically proficient in monovalent cations alone
    • J.B. Murray, A.A. Seyhan, N.G. Walter, J.M. Burke, and W.G. Scott The hammerhead, hairpin and VS ribozymes are catalytically proficient in monovalent cations alone Chem. Biol. 5 1998 587 595
    • (1998) Chem. Biol. , vol.5 , pp. 587-595
    • Murray, J.B.1    Seyhan, A.A.2    Walter, N.G.3    Burke, J.M.4    Scott, W.G.5
  • 5
    • 0035001461 scopus 로고    scopus 로고
    • Comparison of the hammerhead cleavage reactions stimulated by monovalent and divalent cations
    • J.L. O'Rear, S. Wang, A.L. Feig, L. Beigelman, O.C. Uhlenbeck, and D. Herschlag Comparison of the hammerhead cleavage reactions stimulated by monovalent and divalent cations RNA 7 2001 537 545
    • (2001) RNA , vol.7 , pp. 537-545
    • O'Rear, J.L.1    Wang, S.2    Feig, A.L.3    Beigelman, L.4    Uhlenbeck, O.C.5    Herschlag, D.6
  • 6
    • 0035020626 scopus 로고    scopus 로고
    • The hammerhead cleavage reaction in monovalent cations
    • E.A. Curtis, and D.P. Bartel The hammerhead cleavage reaction in monovalent cations RNA 7 2001 546 552
    • (2001) RNA , vol.7 , pp. 546-552
    • Curtis, E.A.1    Bartel, D.P.2
  • 7
    • 0032497521 scopus 로고    scopus 로고
    • Crystal structure of a hepatitis delta virus ribozyme
    • A.R. Ferre-D'Amare, and J.A. Doudna Crystal structure of a hepatitis delta virus ribozyme Nature 395 1998 567 574
    • (1998) Nature , vol.395 , pp. 567-574
    • Ferre-D'Amare, A.R.1    Doudna, J.A.2
  • 8
    • 0034712097 scopus 로고    scopus 로고
    • General acid-base catalysis in the mechanism of a hepatitis delta virus ribozyme
    • S. Nakano, D.M. Chadalavada, and P.C. Bevilacqua General acid-base catalysis in the mechanism of a hepatitis delta virus ribozyme Science 287 2000 1492 1497
    • (2000) Science , vol.287 , pp. 1492-1497
    • Nakano, S.1    Chadalavada, D.M.2    Bevilacqua, P.C.3
  • 9
    • 0035852640 scopus 로고    scopus 로고
    • Involvement of a cytosine side chain in proton transfer in the rate-determining step of ribozyme self-cleavage
    • I.H. Shih, and M.D. Been Involvement of a cytosine side chain in proton transfer in the rate-determining step of ribozyme self-cleavage Proc. Natl. Acad. Sci. USA 98 2001 1489 1494
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1489-1494
    • Shih, I.H.1    Been, M.D.2
  • 10
    • 0035848837 scopus 로고    scopus 로고
    • Crystal structure of a hairpin ribozyme-inhibitor complex with implications for catalysis
    • P.B. Rupert, and A.R. Ferre-D'Amare Crystal structure of a hairpin ribozyme-inhibitor complex with implications for catalysis Nature 410 2001 780 786
    • (2001) Nature , vol.410 , pp. 780-786
    • Rupert, P.B.1    Ferre-D'Amare, A.R.2
  • 12
    • 0037418547 scopus 로고    scopus 로고
    • Mechanistic considerations for general acid-base catalysis by RNA: Revisiting the mechanism of the hairpin ribozyme
    • P.C. Bevilacqua Mechanistic considerations for general acid-base catalysis by RNA: revisiting the mechanism of the hairpin ribozyme Biochemistry 42 2003 2259 2265
    • (2003) Biochemistry , vol.42 , pp. 2259-2265
    • Bevilacqua, P.C.1
  • 13
    • 0037446518 scopus 로고    scopus 로고
    • Ionization of a critical adenosine residue in the neurospora Varkud Satellite ribozyme active site
    • F.D. Jones, and S.A. Strobel Ionization of a critical adenosine residue in the neurospora Varkud Satellite ribozyme active site Biochemistry 42 2003 4265 4276
    • (2003) Biochemistry , vol.42 , pp. 4265-4276
    • Jones, F.D.1    Strobel, S.A.2
  • 14
    • 1642580826 scopus 로고    scopus 로고
    • The Varkud satellite ribozyme
    • D.M. Lilley The Varkud satellite ribozyme RNA 10 2004 151 158
    • (2004) RNA , vol.10 , pp. 151-158
    • Lilley, D.M.1
  • 15
    • 3042848954 scopus 로고    scopus 로고
    • Crystal structure of a self-splicing group I intron with both exons
    • P.L. Adams, M.R. Stahley, A.B. Kosek, J. Wang, and S.A. Strobel Crystal structure of a self-splicing group I intron with both exons Nature 430 2004 45 50
    • (2004) Nature , vol.430 , pp. 45-50
    • Adams, P.L.1    Stahley, M.R.2    Kosek, A.B.3    Wang, J.4    Strobel, S.A.5
  • 16
    • 1642586299 scopus 로고    scopus 로고
    • Control of gene expression by a natural metabolite-responsive ribozyme
    • W.C. Winkler, A. Nahvi, A. Roth, J.A. Collins, and R.R. Breaker Control of gene expression by a natural metabolite-responsive ribozyme Nature 428 2004 281 286
    • (2004) Nature , vol.428 , pp. 281-286
    • Winkler, W.C.1    Nahvi, A.2    Roth, A.3    Collins, J.A.4    Breaker, R.R.5
  • 18
    • 9644308046 scopus 로고    scopus 로고
    • Human 5′ → 3′ exonuclease Xrn2 promotes transcription termination at co-transcriptional cleavage sites
    • S. West, N. Gromak, and N.J. Proudfoot Human 5′ → 3′ exonuclease Xrn2 promotes transcription termination at co-transcriptional cleavage sites Nature 432 2004 522 525
    • (2004) Nature , vol.432 , pp. 522-525
    • West, S.1    Gromak, N.2    Proudfoot, N.J.3
  • 21
    • 0037377340 scopus 로고    scopus 로고
    • Rube Goldberg goes (ribo)nuclear? Molecular switches and sensors made from RNA
    • S.K. Silverman Rube Goldberg goes (ribo)nuclear? Molecular switches and sensors made from RNA RNA 9 2003 377 383
    • (2003) RNA , vol.9 , pp. 377-383
    • Silverman, S.K.1
  • 22
    • 0036760723 scopus 로고    scopus 로고
    • Coenzymes as coribozymes
    • V.R. Jadhav, and M. Yarus Coenzymes as coribozymes Biochemie 84 2002 877 888
    • (2002) Biochemie , vol.84 , pp. 877-888
    • Jadhav, V.R.1    Yarus, M.2
  • 23
    • 0032568656 scopus 로고    scopus 로고
    • An amino acid as a cofactor for a catalytic polynucleotide
    • A. Roth, and R.R. Breaker An amino acid as a cofactor for a catalytic polynucleotide Proc. Natl. Acad. Sci. USA 95 1998 6027 6031
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6027-6031
    • Roth, A.1    Breaker, R.R.2
  • 24
    • 0032831634 scopus 로고    scopus 로고
    • Relationship between internucleotide linkage geometry and the stability of RNA
    • G.A. Soukup, and R.R. Breaker Relationship between internucleotide linkage geometry and the stability of RNA RNA 5 1999 1308 1325
    • (1999) RNA , vol.5 , pp. 1308-1325
    • Soukup, G.A.1    Breaker, R.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.