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 …

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 …

Ricin is a potent, plant‐derived, ribosome inactivating protein. To target ribosomes in the
mammalian cytosol, ricin must firstly negotiate the endomembrane system of the cell to …

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 …

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 …

Ricin is a potent ribotoxin that is considered a bioterror threat due to its ease of isolation and
possibility of aerosolization. In yeast, mutation of arginine residues away from the active site …

The generally accepted model of ricin intoxication assumes that direct inactivation of
ribosomes by depurination of a specific adenine residue within the sarcin-ricin-loop (SRL) …

Ribosome inactivating proteins (RIPs) form a vast family of hundreds of toxins from plants,
fungi, algae, and bacteria. RIP activities have also been detected in animal tissues. They …

Ricin interacts with the ribosomal P stalk to cleave a conserved adenine from the α-
sarcin/ricin loop (SRL) of the rRNA. Ricin toxin A chain (RTA) uses Arg235 as the most …

Ribosome-inactivating proteins (RIPs) are toxic N-glycosidases that depurinate the
universally conserved α-sarcin loop of large rRNAs. They have received attention in …