메뉴 건너뛰기




Volumn 50, Issue 1, 2001, Pages 7-17

Sequence analysis and structure prediction of aminoglycoside-resistance 16S rRNA:m7G methyltransferases

Author keywords

[No Author keywords available]

Indexed keywords

AMINOGLYCOSIDE ANTIBIOTIC AGENT; METHYLTRANSFERASE; RNA 16S; S ADENOSYLMETHIONINE;

EID: 0034977748     PISSN: 01371320     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (16)

References (41)
  • 3
    • 0003009570 scopus 로고    scopus 로고
    • Comparison of protein structures reveals monophyletic origin of the AdoMet-dependent methyltransferase family and mechanistic convergence rather than recent differentiation of N4-cytosine and N6-adenine DNA methylation
    • (1999) In Silico Biol. , vol.1 , pp. 1-8
    • Bujnicki, J.M.1
  • 4
    • 0034643929 scopus 로고    scopus 로고
    • Homology modelling of the DNA 5mC methyltransferase M.BssHII, is permutation of functional subdomains common to all subfamilies of DNA methyltransferases?
    • (2000) Int. J. Biol. Macromol. , vol.27 , pp. 195-204
    • Bujnicki, J.M.1
  • 5
    • 0033729437 scopus 로고    scopus 로고
    • Phylogenomic analysis of 16S rRNA:(guanine-N2) methyltransferases suggests new family members and reveals highly conserved motifs and a domain structure similar to other nucleic acid amino-methyltransferases
    • (2000) FASEB J , vol.14
    • Bujnicki, J.M.1
  • 6
    • 0033918469 scopus 로고    scopus 로고
    • Sequence, structural, and evolutionary analysis of Prokaryotic ribosomal protein L11 methyltransferases
    • (2000) Acta Microbiol. Pol. , vol.49 , pp. 19-28
    • Bujnicki, J.M.1
  • 7
    • 0032730192 scopus 로고    scopus 로고
    • Is the HemK family of putative S-adenosylmethionine-dependent methyltransferases a "missing" zeta subfamily of adenine methyltransferases? A hypothesis
    • (1999) IUBMB Life , vol.48 , pp. 247-250
    • Bujnicki, J.M.1    Radlińska, M.2
  • 17
    • 0002450504 scopus 로고    scopus 로고
    • Structure and evolution of AdoMet-dependent MTases
    • S-adenosylmethionine-dependent methyltransferases: structures and functions. X. Cheng and R.M. Blumenthal, (eds) World Scientific Inc., Singapore
    • (1999) , pp. 1-38
    • Fauman, E.B.1    Blumenthal, R.M.2    Cheng, X.3
  • 24
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 417-427
    • Kagan, R.M.1    Clarke, S.2
  • 29
    • 0028841409 scopus 로고
    • Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes
    • (1995) J. Mol. Biol. , vol.253 , pp. 618-632
    • Malone, T.1    Blumenthal, R.M.2    Cheng, X.3
  • 31
    • 0027324801 scopus 로고
    • Analysis of the self-defense gene (fmrO) of a fortimicin A (astromicin) producer, Micromonospora olivasterospora: Comparison with other aminoglycoside-resistance-encoding genes
    • (1993) Gene , vol.127 , pp. 63-69
    • Ohta, T.1    Hasegawa, M.2
  • 34
    • 0032705750 scopus 로고    scopus 로고
    • Structural characterization of two tandemly arranged DNA methyltransferase genes from Neisseria gonorrhoeae MS 11: N4-cytosine specific M.NgoMXV and nonfunctional 5-cytosine-type M.NgoMorf2P
    • (1999) Proteins , vol.37 , pp. 717-728
    • Radlińska, M.1    Bujnicki, J.M.2    Piekarowicz, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.