The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Studies on the accessability of ribosomes to inactivation by the toxic lectins abrin and ricin.

The rate of protein synthesis in HeLa cells was measured at various periods of time after addition of abrin and ricin to the medium and compared with the concurrent ability of the isolated ribosomes to support poly(U)-stimulated synthesis of polyphenylalanine in a cell-free system. Similarly, the endogenous synthesis in unfractionated cell-free systems from HeLa cells and rabbit reticulocytes was compared with the ability of the isolated ribosomes to support poly(U)-stimulated polymerization of phenylalanine. In the intact cells and the unfractionated cell-free systems protein synthesis decreased progressively with the time after addition of toxins or toxin A chains. In contrast, the ability of the isolated ribosomes to support polyphenylalanine synthesis was only moderately reduced initially and then remained constant or even increased. The activity of isolated monosomes decreased progressively with time after addition of toxin A chain, whereas polysomes were only partly inactivated and the extent of inactivation varied from one experiment to another. The results indicate that the inactivation of one or a few ribosomes per polysome stops the translation of mRNA. It is suggested that the intact ribosomes thus trapped are inaccessible to the toxins and that the isolation of polysomes results in release of functionally intact ribosomes capable of supporting poly(U)-directed polymerization of phenylalanine.[1]

References

 
WikiGenes - Universities