Human topoisomerase IIα possesses an intrinsic nucleic acid specificity for DNA ligation: Use of 5′ covalently activated oligonucleotide substrates to study enzyme mechanism

Journal of Biological Chemistry

Volumn 277, Issue 34, 2002, Pages 31201-31206

  Bromberg, Kenneth D ^a,b,c   Hendricks, Chris ^a,b,c   Burgin, Alex B ^a,b,c   Osheroff, Neil ^a,b,c  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b SAN DIEGO STATE UNIVERSITY   (United States)

^c Emerald BioStructures   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOASSAY; DNA; ENZYMES; NUCLEIC ACIDS; SUBSTRATES;

LIGATION;

BIOCHEMISTRY;

4 NITROPHENOL; DNA; DNA TOPOISOMERASE (ATP HYDROLYSING); DNA TOPOISOMERASE 2ALPHA; TYROSINE DERIVATIVE; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; DNA TOPOISOMERASE II ALPHA; OLIGONUCLEOTIDE; TUMOR ANTIGEN;

ARTICLE; BINDING KINETICS; COVALENT BOND; DNA DAMAGE; DNA SEQUENCE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME ASSAY; ENZYME DEFECT; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; GENE MUTATION; HUMAN; HUMAN CELL; NUCLEIC ACID ANALYSIS; PRIORITY JOURNAL; CHEMISTRY; METABOLISM;

ANTIGENS, NEOPLASM; DNA; DNA TOPOISOMERASES, TYPE II, EUKARYOTIC; DNA-BINDING PROTEINS; HUMANS; OLIGONUCLEOTIDES;

EID: 0037162621     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M204741200     Document Type: Article

References (42)