Published in Gene Therapy Weekly, May 24th, 1999
A. Nakayama and colleagues from the University of Tsukuba, Japan, demonstrated previously that shortened forms of (stem II-deleted) hammerhead ribozymes with low intrinsic activity form very active dimers with a common stem II (very active short ribozymes capable of forming dimers were designated maxizymes). As a result of such a dimeric structure, the researchers noted that heterodimeric maxizymes are potentially capable of cleaving a substrate at two different sites simultaneously.
As such, active heterodimers are in equilibrium with inactive homodimers, they reported and longer forms of...
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