Quinolones share a common interaction domain on topoisomerase II with other DNA cleavage-enhancing antineoplastic drugs

Biochemistry

Volumn 36, Issue 10, 1997, Pages 2919-2924

  Elsea, Sarah H ^a,b   Westergaard, Majken ^a   Burden, D Andrew ^a   Lomenick, Jefferson P ^a   Osheroff, Neil ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMSACRINE; ANTINEOPLASTIC AGENT; CIPROFLOXACIN; CP 115953; CP 80080; DIMETHYL SULFOXIDE; DNA; DNA TOPOISOMERASE (ATP HYDROLYSING); ETOPOSIDE; GENISTEIN; QUINOLONE DERIVATIVE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CHO CELL; COMPETITIVE INHIBITION; CONTROLLED STUDY; CYTOTOXICITY; DNA CLEAVAGE; DROSOPHILA MELANOGASTER; DRUG POTENTIATION; DRUG STRUCTURE; NONHUMAN; PRIORITY JOURNAL;

AMSACRINE; ANIMALS; ANTI-INFECTIVE AGENTS; ANTINEOPLASTIC AGENTS; BINDING SITES; CHO CELLS; CIPROFLOXACIN; CRICETINAE; DNA TOPOISOMERASES, TYPE II; DNA, SUPERHELICAL; DROSOPHILA MELANOGASTER; ELECTROPHORESIS, AGAR GEL; ENZYME ACTIVATION; ETOPOSIDE; FLUOROQUINOLONES; GENISTEIN; ISOFLAVONES; KINETICS; MOLECULAR STRUCTURE; QUINOLONES;

EID: 0030933177     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi962488f     Document Type: Article

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