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Volumn 8, Issue 14, 2007, Pages 1700-1709

Differential selectivity of natural and synthetic aminoglycosides towards the eukaryotic and prokaryotic decoding A sites

Author keywords

Aminoglycosides; Ribosomal decoding sites; RNA; Translation inhibition; X ray analysis

Indexed keywords

AMINOGLYCOSIDE ANTIBIOTIC AGENT; APRAMYCIN; GENTAMICIN; NB 30; NB 33; PAROMOMYCIN; UNCLASSIFIED DRUG;

EID: 34948883252     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.200700271     Document Type: Article
Times cited : (54)

References (68)
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    • A similar stacking interaction between a sugar ring and aromatic amino acid side-chains at the active site of glycoside hydrolase enzymes has been reported. For representative examples see: a) K. Haga, R. Kanai, O. Sakamoto, M. Aoyagi, K. Harata, K. Yamane, J. Biochem. 2003, 134, 881-891;
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    • From this comparative analysis one could argue that probably paromamine alone and/or paromamine linked at the 3′-OH position with an additional sugar ring could also lead to similar selective association into the eukaryotic off state conformation and subsequently strongly inhibit eukaryotic translation. Our recent data show however that neither paromamine nor β-linked-paromamine with ribose or 5-amino ribose at 3′-position are effective inhibitors of eukaryotic protein translation in vitro, even though they lack antibacterial activity.[9] These data suggest that only two rings of paromamine or three rings pattern as above, even though they might participate in key interactions for target binding, are not sufficient for proper recognition/binding and for subsequent biological effect in eukaryotes. Similar lack of antibacterial activity of neamine, albeit its same binding mode to those of several 4,5-and 4,6-aminoglycosides to prokaryotic A site
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.