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dc.contributor.authorSpicer, JA
dc.contributor.authorMiller, CK
dc.contributor.authorO'Connor, PD
dc.contributor.authorJose, J
dc.contributor.authorHuttunen, KM
dc.contributor.authorJaiswal, JK
dc.contributor.authorDenny, WA
dc.contributor.authorAkhlaghi, H
dc.contributor.authorBrowne, KA
dc.contributor.authorTrapani, JA
dc.date.accessioned2021-02-04T02:02:58Z
dc.date.available2021-02-04T02:02:58Z
dc.date.issued2017-09-08
dc.identifierpii: S0223-5234(17)30409-9
dc.identifier.citationSpicer, J. A., Miller, C. K., O'Connor, P. D., Jose, J., Huttunen, K. M., Jaiswal, J. K., Denny, W. A., Akhlaghi, H., Browne, K. A. & Trapani, J. A. (2017). Substituted arylsulphonamides as inhibitors of perforin-mediated lysis. EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY, 137, pp.139-155. https://doi.org/10.1016/j.ejmech.2017.05.048.
dc.identifier.issn0223-5234
dc.identifier.urihttp://hdl.handle.net/11343/259553
dc.description.abstractThe structure-activity relationships for a series of arylsulphonamide-based inhibitors of the pore-forming protein perforin have been explored. Perforin is a key component of the human immune response, however inappropriate activity has also been implicated in certain auto-immune and therapy-induced conditions such as allograft rejection and graft versus host disease. Since perforin is expressed exclusively by cells of the immune system, inhibition of this protein would be a highly selective strategy for the immunosuppressive treatment of these disorders. Compounds from this series were demonstrated to be potent inhibitors of the lytic action of both isolated recombinant perforin and perforin secreted by natural killer cells in vitro. Several potent and soluble examples were assessed for in vivo pharmacokinetic properties and found to be suitable for progression to an in vivo model of transplant rejection.
dc.languageEnglish
dc.publisherELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.titleSubstituted arylsulphonamides as inhibitors of perforin-mediated lysis
dc.typeJournal Article
dc.identifier.doi10.1016/j.ejmech.2017.05.048
melbourne.affiliation.departmentSir Peter MacCallum Department of Oncology
melbourne.affiliation.facultyMedicine, Dentistry & Health Sciences
melbourne.source.titleEuropean Journal of Medicinal Chemistry
melbourne.source.volume137
melbourne.source.pages139-155
dc.rights.licenseCC BY
melbourne.elementsid1214936
melbourne.contributor.authorTrapani, Joseph
dc.identifier.eissn1768-3254
melbourne.accessrightsOpen Access


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