Abstract

Since the discovery of the c-Myc dimerization partner Max (Blackwood and Eisenman 1991; Prendergast et al. 1991) a startling number of proteins capable to interact directly or indirectly with c-Myc and/or Max have been described (for review see Marcu et al. 1992; Henriksson and Luscher 1996). It has become evident that at the center of this network lies Max which on one hand forms heterodimers with the Myc family of proteins, including c-, N-, and L-Myc and on the other hand heterodimerizes with proteins of the Mad family, including Mad1, Mxi1 (or Mad2), Mad3, and Mad4. In addition Max has also the ability to form homodimers. Thus Max is the true center of this array of proteins which we will refer to as the Myc/Max/Mad network.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.