Protein folding is a complex, error-prone process that often results in an irreparable protein
by-product. These by-products can be recognized by cellular quality control machineries …

Accidental and intended Ricinus communis intoxications in humans and animals have been
known for centuries but the causative agent remained elusive until 1888 when Stillmark …

The ubiquitin proteasome system (UPS) maintains the integrity of the proteome by
selectively degrading misfolded or mis-assembled proteins, but the rules that govern how …

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 …

ER-associated degradation (ERAD) is a mechanism by which numerous ER-localized
proteins are targeted for cytosolic degradation by the ubiquitin–proteasome system. A …

The 26S proteasome is a chambered protease in which the majority of selective cellular
protein degradation takes place. Throughout evolution, access of protein substrates to …

A number of protein toxins bind at the surface of mammalian cells and after endocytosis
traffic to the endoplasmic reticulum, where the toxic A chains are liberated from the …

Ricin can be isolated from the seeds of the castor bean plant (Ricinus communis). It belongs
to the ribosome-inactivating protein (RIP) family of toxins classified as a bio-threat agent due …

The heterodimeric plant toxin ricin binds exposed galactosyls at the cell surface of target
mammalian cells, and, following endocytosis, is transported in vesicular carriers to the …

ER-associated degradation (ERAD) is a protein clearance mechanism by which misfolded,
misassembled, or metabolically regulated proteins are specifically dislocated from the ER …