Biochemical and Biophysical Research Communications
Bacitracin: An inhibitor of the insulin degrading activity of glutathione-insulin transhydrogenase
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Involvement of protein disulfide isomerase in subtilase cytotoxin-induced cell death in HeLa cells
2020, Biochemical and Biophysical Research CommunicationsEvaluation of Leishmania donovani disulfide isomerase as a potential target of cellular immunity against visceral leishmaniasis
2014, Cellular ImmunologyCitation Excerpt :To date, little is known about the role of PDI in lower eukaryotes such as protozoan parasite, L. donovani and its relevance to host parasite interaction during visceral leishmaniasis. The precise mechanism, especially in relation to redox changes and its effects on immunological responses is also not completely understood [43,34,33,44]. The characterisation of PDIs obviously has important implication for the design of new drug or vaccine against Leishmania parasites.
Protein disulfide isomerase: A promising target for cancer therapy
2014, Drug Discovery TodayEntamoeba histolytica: Biochemical characterization of a protein disulfide isomerase
2011, Experimental ParasitologyCitation Excerpt :Despite the slight difference between the Km values, the micromolar order and the highly similar enzymatic rate suggest that EhPDI acts mainly as oxidase/isomerase. The inhibitory effect of the antibiotic bacitracin, a well-known inhibitor of PDI enzymes (Roth, 1981; Mizunaga et al., 1990; Mandel et al., 1993), was evaluated on the oxidoreductase activities of recombinant EhPDI. Typical inhibition profiles were observed (Fig. 4) for the reductase, oxidase and isomerase activities, with apparent IC50 values of 1.137, 0.172 and 0.334 mM, respectively.
FAD oxidizes the ERO1-PDI electron transfer chain: The role of membrane integrity
2005, Biochemical and Biophysical Research CommunicationsCitation Excerpt :FAD-driven oxidation was also hindered by bacitracin treatment. During these experiments, we found that bacitracin, the inhibitor of PDI oxidoreductase activity [34–36], completely inhibited the FAD-driven oxidation of ER lumenal proteins. These data suggest that FAD uses the Ero1-PDI pathway for the oxidation of ER proteins.