Development of a simple label-free fluorescence hybridization assay to monitor the
depurination activity of toxic ribosome inactivating proteins by using a fluorescent ligand that …

Combinatorial protein libraries based on a protein template offer a vast potential for deriving
protein variants harboring new receptor specificity while retaining other tem-plate functions …

Ribosome-inactivating proteins (RIPs) were first isolated over a century ago and have been
shown to be catalytic toxins that irreversibly inactivate protein synthesis. Elucidation of …

Molecular farming in plants is an emerging platform for the production of pharmaceutical
proteins, and host species such as tobacco are now becoming competitive with …

Ribotoxins constitute a family of toxic extracellular fungal RNases that exert a highly specific
activity on a conserved region of the larger molecule of rRNA, known as the sarcin-ricin loop …

Background Treatment with tumor-targeted toxins attempts to overcome the disadvantages
of conventional cancer therapies by directing a drug's cytotoxic effect specifically towards …

Several protein toxins, such as the potent plant toxin ricin, enter mammalian cells by
endocytosis and undergo retrograde transport via the Golgi complex to reach the …

Protein translation is the most common target of toxin-antitoxin system (TA) toxins. Sequence-
specific endoribonucleases digest RNA in a sequence-specific manner, thereby blocking …

Bryodin 1 (BD1) is a potent ribosome-inactivating protein (RIP) isolated from the plant
Bryonia dioica. It is relatively nontoxic in rodents (LD50> 40 mg/kg) and represents a …

Ricin is a member of the ribosome-inactivating protein (RIP) family of plant and bacterial
toxins. In this study we used a high-throughput, cell-based assay to screen more than …