Martin, G <br/><br/>
Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and catalytic domain, homologous to the family X polymerases, and to other nucleotidyltransferases.  [electronic resource] 

 -  The EMBO journal  May 1996 
 - 2593-603 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0261-4189 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Animals<br/>Aspartic Acid<br/>Binding Sites<br/>Caenorhabditis elegans--enzymology<br/>Cattle<br/>DNA Nucleotidylexotransferase--chemistry<br/>DNA Polymerase I--chemistry<br/>DNA Polymerase beta<br/>DNA-Directed DNA Polymerase--chemistry<br/>Fungal Proteins--chemistry<br/>Helminth Proteins--chemistry<br/>Humans<br/>Mice<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Multigene Family<br/>Mutagenesis, Site-Directed<br/>Nucleotidyltransferases--chemistry<br/>Polynucleotide Adenylyltransferase--chemistry<br/>Protein Binding<br/>RNA--metabolism<br/>RNA Precursors--metabolism<br/>Recombinant Proteins--metabolism<br/>Saccharomyces cerevisiae--enzymology<br/>Saccharomyces cerevisiae Proteins<br/>Sequence Alignment<br/>Sequence Deletion<br/>Sequence Homology, Amino Acid<br/>Species Specificity<br/>Xenopus laevis