Sandbox Reserved 200: Difference between revisions

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The RNase A 3D swapped oligomers show significant biological activity including allostery, antitumor, and immunorepression activity.  This same activity has not observed in the monomer and the non-3D domain swapped dimers .<ref name="liu98">PMID:9502384</ref > This could be due to the fact that the monomer has a cystolic RNase A inhibitor that is unable to inhibit the active sites of the oligomers. <ref name="liu01">PMID:11790847</ref >   
The RNase A 3D swapped oligomers show significant biological activity including allostery, antitumor, and immunorepression activity.  This same activity has not observed in the monomer and the non-3D domain swapped dimers .<ref name="liu98">PMID:9502384</ref > This could be due to the fact that the monomer has a cystolic RNase A inhibitor that is unable to inhibit the active sites of the oligomers. <ref name="liu01">PMID:11790847</ref >   


The RNase A 3D domain swapped oligomers show significant biological activity including allostery, antitumor, and immunorepression activity.  This same activity has not observed in the monomer and the non-3D domain swapped oligomers .<ref name="liu98">PMID:9502384</ref > This could be due to the fact that the monomer has a cystolic RNase A inhibitor that is unable to inhibit the active sites of the oligomers. <ref name="liu01">PMID:11790847</ref > 


All oligomers of RNase A have antitumor activity, but the larger oligomers show greater activity. <ref name="tumor"/>
The RNase A 3D domain swapped oligomers show significant biological activity including allostery, antitumor, and immunorepression activity.  In antitumor activity, the oligomers degrade dsRNA, but they are also capable of degrading DNA and RNA hybrids which can be found during the translation of genes.<ref name="antitumor"/>  This same activity has not observed in the monomer and the non-3D domain swapped oligomers .<ref name="liu98">PMID:9502384</ref > This could be due to the fact that the monomer has a cystolic RNase A inhibitor that is unable to inhibit the active sites of the oligomers. <ref name="liu01">PMID:11790847</ref > 
 
 
All oligomers of RNase A have antitumor activity, but the higher ordered oligomers show greater activity. <ref name="tumor"/> Though the higher ordered oligomers are more active, they are also much more unstable when ''in vivo''.  The pathway of the oligomer once it is inside the cell is unknown, but they do seem to be unregulated.  <ref name="tumor"/>  In cancer cells because the movement of proteins into the nucleus is unregulated, oligomers can sometimes enter into the nucleus.  Once the oligomer is in the nucleus, it is able to degrade RNA and DNA hybrids.<ref name="tumor"/>  This will eventually prevent the cell from dividing and decrease the tumor size.