Effects of deletion and site-directed mutations on ligation steps of NAD+-dependent DNA ligase: a biochemical analysis of BRCA1 C-terminal domain.
Feng
Hong
H
Department of Genetics, Biochemistry & Life Science Studies, South Carolina Experiment Station, Clemson University, Room 219, Biosystems Research Complex, 51 New Cherry Street, Clemson, South Carolina 29634, USA.
Parker
Jeremy M
JM
Lu
Jing
J
Cao
Weiguo
W
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution / Q000235:genetics; D019313:BRCA1 Protein / Q000737:chemistry* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D020137:Base Pair Mismatch / Q000235:genetics; D001483:Base Sequence; D011088:DNA Ligases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009243:NAD / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics; D017434:Protein Structure, Tertiary / Q000235:genetics; D017384:Sequence Deletion; D013379:Substrate Specificity / Q000235:genetics; D013824:Thermus / Q000201:enzymology / Q000235:genetics
D019313:BRCA1 Protein; D001426:Bacterial Proteins; D008024:Ligands; D010446:Peptide Fragments; D009243:NAD; D011088:DNA Ligases; C120640:DNA ligase (NAD)