Literature summary for 2.4.1.B62 extracted from

Savidge, T,C,; Urvil, P.;, Oezguen, N.; Ali, K.; Choudhury, A.; Acharya, V.; Pinchuk, I.; Torres, A.G., English, R.D.; Wiktorowicz, J.E.; Loeffelholz, M.; Kumar, R.; Shi, L.; Nie, W.; Braun, W.; Herman, B., Hausladen, A.; Feng, H.; Stamler, J.S.; Pothoulakis, C.
Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins (2011), Nat. Med., 17, 1136-1141.

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Application

Application	Comment	Organism
medicine	Peptoclostridium difficile toxins A and B are S-nitrosylated by the infected host and S-nitrosylation attenuates virulence by inhibiting toxin self-cleavage and cell entry. InsP(6)- and inositol diphosphate InsP(7)-induced conformational changes in the toxin enable host S-nitrosothiols to transnitrosylate the toxin catalytic cysteine, which forms part of a structurally conserved nitrosylation motif. Treatment with exogenous InsP(6) enhances the therapeutic actions of oral S-nitrosothiols in mouse models of Peptoclostridium difficile infection	Clostridioides difficile

Organism

Organism	UniProt	Comment	Textmining
Clostridioides difficile	-	-	-

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Release 2023.1 (January 2023)