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 …

Ribosome-inactivating proteins (RIPs) are EC3. 2.32. 22 N-glycosidases that recognize a
universally conserved stem-loop structure in 23S/25S/28S rRNA, depurinating a single …

Extracellular vesicles (EVs) including exosomes have been shown to play crucial roles in
cell-to-cell communication because of their ability to carry biofunctional molecules (eg …

Thirty years ago, the type 1 ribosome-inactivating protein (RIP) saporin-S6 (also known as
saporin) was isolated from Saponaria officinalis L. seeds. Since then, the properties and …

Extracellular vesicles (EVs, exosomes) are approximately 30-to 200-nm-long vesicles that
have received increased attention due to their role in cell-to-cell communication. Although …

Many plants contain proteins that are commonly designated as ribosome-inactivating
proteins (RIPs). Based on the structure of the genes and the mature proteins a novel system …

The antimicrobial protein CAP18 (approximate molecular weight: 18 000), which was first
isolated from rabbit granulocytes, comprises a C-terminal fragment that has negatively …

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 …

Seed storage proteins are major source of proteins because of readily available bioactive
peptides. These peptides are fragments of a protein, which showed positive implications on …

We demonstrate a novel system for inducing clustering of cell surface receptors via
recognition peptide segments displayed on exosomes, leading to receptor activation. With …