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 …

A family of structurally related protein toxins extracted from bacteria or plants have a similar
mechanism of action, namely, blocking protein synthesis by ribosome inactivation. Members …

Protein toxins are among the oldest and most exotic warfare agents.[1] Among these,
ribosomeinactivating proteins (RIPs), particularly ricin, represent some of the most …

Adenine quantitation is required for a variety of applications. To date, the prevalent method
for quantifying free adenine, in a variety of applications, is the detection of fluorescent …

Ricin is a member of the ubiquitous ribosome‐inactivating protein (RIP) family of toxins. The
Centers for Disease Control and Prevention (CDC) classify ricin and related toxins as …

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 …

Ricin acts to damage cells by producing a site of depurination in 28S ribosomal RNA. This
depurination results in ribosome inactivation which inhibits protein synthesis and ultimately …

A number of plant proteins inhibit protein synthesis by irreversibly inactivating the 60S
ribosomal subunit in a catalytical, that is, enzymatic, manner. For this property, they are …

The intent of this article is to review recent literature on ribosome inactivating proteins (RIPs)
including isolation and characterization of new RIPs, studies on the crystal structures and …

Ribosome inactivating proteins (RIPs) form a class of toxins that was identified over a
century ago. They continue to fascinate scientists and the public due to their very high …