Hurlin, P J <br/><br/>
Mga, a dual-specificity transcription factor that interacts with Max and contains a T-domain DNA-binding motif.  [electronic resource] 

 -  The EMBO journal  Dec 1999 
 - 7019-28 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>0261-4189 
<br/><br/><label>Standard No.: </label>10.1093/emboj/18.24.7019  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Animals<br/>Base Sequence<br/>Basic Helix-Loop-Helix Leucine Zipper Transcription Factors<br/>Basic Helix-Loop-Helix Transcription Factors<br/>Basic-Leucine Zipper Transcription Factors<br/>Binding Sites<br/>Cloning, Molecular<br/>DNA-Binding Proteins--chemistry<br/>Dimerization<br/>Embryonic and Fetal Development<br/>Fetal Proteins--genetics<br/>Gene Expression Regulation, Developmental<br/>Helix-Loop-Helix Motifs<br/>Leucine Zippers<br/>Mice<br/>Molecular Sequence Data<br/>Proto-Oncogene Proteins c-myc--chemistry<br/>Recombinant Proteins--chemistry<br/>Sequence Alignment<br/>Sequence Homology, Amino Acid<br/>T-Box Domain Proteins--genetics<br/>Transcription Factors--chemistry<br/>Brachyury Protein