α-Sarcin and ricin represent two structurally and mechanistically distinct families of site-
specific enzymes that block translation by irreversibly modifying the sarcin/ricin loop (SRL) of …

Abstract α-sarcin ribotoxins comprise a unique family of ribonucleases that cripple the
ribosome by catalyzing endoribonucleolytic cleavage of ribosomal RNA at a specific location …

The plant toxin ricin is highly toxic for mammalian cells and is of concern for bioterrorism.
Ricin belongs to a family of functionally related toxins, collectively referred to as ribosome …

Ribosome inactivating proteins (RIPs) depurinate a universally conserved adenine in the α-
sarcin/ricin loop (SRL) and inhibit protein synthesis at the translation elongation step. We …

Ricin belongs to the group of ribosome-inactivating proteins (RIPs), ie, toxins that have
evolved to provide particular species with an advantage over other competitors in nature …

Ribotoxins are potent inhibitors of protein biosynthesis and inactivate ribosomes from a
variety of organisms. The ribotoxin α-sarcin cleaves the large 23S ribosomal RNA (rRNA) at …

Restrictocin and related fungal endoribonucleases from the α-sarcin family site-specifically
cleave the sarcin/ricin loop (SRL) on the ribosome to inhibit translation and ultimately trigger …

Ribosome-inactivating proteins (RIPs) are potent toxins that inactivate ribosomes by
catalytically removing a specific adenine from the α-sarcin/ricin loop (SRL) of the large …

Ribosome-inactivating proteins (RIPs) including ricin, Shiga toxin, and trichosanthin, are
RNA N-glycosidases that depurinate a specific adenine residue (A-4324 in rat 28S …

Ricin produced by the castor bean plant and Shiga toxins produced by pathogenic
Escherichia coli (STEC) and Shigella dysenteriae are type II ribosome inactivating proteins …