Mackey, Z B <br/><br/>
DNA ligase III is recruited to DNA strand breaks by a zinc finger motif homologous to that of poly(ADP-ribose) polymerase. Identification of two functionally distinct DNA binding regions within DNA ligase III.  [electronic resource] 

 -  The Journal of biological chemistry  Jul 1999 
 - 21679-87 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Standard No.: </label>10.1074/jbc.274.31.21679  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adenosine Monophosphate--metabolism<br/>Adenosine Triphosphate--metabolism<br/>Amino Acid Sequence<br/>Amino Acid Substitution<br/>Animals<br/>Binding Sites<br/>Catalytic Domain<br/>Conserved Sequence<br/>DNA Footprinting<br/>DNA Ligase ATP<br/>DNA Ligases--chemistry<br/>DNA Repair<br/>Deoxyribonuclease I<br/>Humans<br/>Lysine<br/>Mammals<br/>Molecular Sequence Data<br/>Mutagenesis, Site-Directed<br/>Poly(ADP-ribose) Polymerases--chemistry<br/>Poly-ADP-Ribose Binding Proteins<br/>Recombinant Proteins--chemistry<br/>Sequence Alignment<br/>Sequence Homology, Amino Acid<br/>Xenopus Proteins<br/>Zinc Fingers