Ribosome-inactivating proteins (RIPs) are N-glycosidases, which depurinate a specific
adenine residue in the conserved α-sarcin/ricin loop (α-SRL) of rRNA. This loop is important …

Most molecular target-based therapeutic research facilities use two basic techniques:
protein-kinase inhibitors and monoclonal antibodies. However, they continue to face …

Ribosome-inactivating proteins (RIPs) are enzymes (3.2. 2.22) that possess N-glycosilase
activity that irreversibly inhibits protein synthesis. RIPs have been found in plants, fungi …

The term ribosome-inactivating protein (RIP) is used to denominate proteins mostly of plant
origin, which have N-glycosidase enzymatic activity leading to a complete destruction of the …

The concept of “magic bullets”, ie, drugs able to selectively act on target cells, formulated by
Paul Ehrlich more than one century ago, gave rise to the idea of immunotargeting, one of the …

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

Ribosome-inactivating proteins (RIPs) are toxic because they bind to 28S rRNA and
depurinate a specific adenine residue from the α-sarcin/ricin loop (SRL), thereby inhibiting …

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 …

Toxin domains from plants or bacterial origin (such as Diphtheria toxin (DT) or
Pseudomonas exotoxin A (PEA), which are endowed with ADP-ribosylation activity of the …

Ribosome‐inactivating proteins (RIPs) are toxic proteins with N‐glycosidase activity. RIPs
exert their action by removing a specific purine from 28S rRNA, thereby, irreversibly …