Literature summary for 3.2.2.22 extracted from

Arfilli, V.; Carnicelli, D.; Rocchi, L.; Ricci, F.; Pagliaro, P.; Tazzari, P.L.; Brigotti, M.
Shiga toxin 1 and ricin A chain bind to human polymorphonuclear leucocytes through a common receptor (2010), Biochem. J., 432, 173-180.

Search for more literature for 3.2.2.22

Organism

Organism	UniProt	Comment	Textmining
Ricinus communis	-	-	-
Saponaria officinalis	-	-	-
Suregada multiflora	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
seed	-	Ricinus communis	-
seed	-	Saponaria officinalis	-
seed	-	Suregada multiflora	-

Synonyms

Synonyms	Comment	Organism
gelonin	-	Suregada multiflora
ribosome-inactivating protein	-	Ricinus communis
ribosome-inactivating protein	-	Saponaria officinalis
ribosome-inactivating protein	-	Suregada multiflora
ricin	-	Ricinus communis
RIP	-	Ricinus communis
RIP	-	Saponaria officinalis
RIP	-	Suregada multiflora
saporin S6	-	Saponaria officinalis

General Information

General Information	Comment	Organism
physiological function	gelonin inhibits the binding of Shiga toxin1 to polymorphonuclear leucocytes	Suregada multiflora
physiological function	gelonin saporin S6 inhibits the binding of Shiga toxin1 to polymorphonuclear leucocytes	Saponaria officinalis
physiological function	ricin is highly toxic as it contains, in addition to the enzymatically active A chain, a second B chain that binds to galactose-containing surface molecules mediating endocytosis of the RIP	Ricinus communis

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Release 2023.1 (January 2023)