Sandbox Reserved 492: Difference between revisions

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== '''Uses & Potential Benefits''' ==
== '''Uses & Potential Benefits''' ==


While measures of treating someone with CX intoxication generally involves carefully replenishing electrolytes and other vital fluids there have been plenty of tests conducted that show that the toxin can be directly inhibited on the molecular level as well. The catalytic subunit of the CX protein has shown to bind, with high affinity a molecule known as PJ34- as well as other structurally conserved, fused-hydrocarbon ring inhibitors. Essentially, the PJ34 replaces what would target protein in the epithelial cell of a human host and prevent the ill effects of intoxication...in theory.                                                         {{clear}}    This is wheree the text would go
While measures of treating someone with CX intoxication generally involves carefully replenishing electrolytes and other vital fluids there have been plenty of tests conducted that show that the toxin can be directly inhibited on the molecular level as well. The catalytic subunit of the CX protein has shown to bind, with high affinity a molecule known as PJ34- as well as other structurally conserved, fused-hydrocarbon ring inhibitors. Essentially, the <scene name='Sandbox_Reserved_492/Pj34_inhibitor/1'>PJ34</scene>replaces what would target protein in the epithelial cell of a human host and prevent the ill effects of intoxication...in theory.                                              
        {{clear}}    This is wheree the text would go


<Structure load='2Q6M' size='425' color='black' frame='true' align='middle' caption='X-Ray Diffraction image at 2.1Å of catalytic fragment with PJ34 inhibitor bound.' />  
<Structure load='2Q6M' size='425' color='black' frame='true' align='middle' caption='X-Ray Diffraction image at 2.1Å of catalytic fragment with PJ34 inhibitor bound.' />  

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Charlie Zogzas