Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/1754
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dc.contributor.authorKaur, M.-
dc.contributor.authorDubey, A.-
dc.contributor.authorKhatri, M.-
dc.contributor.authorSehrawat, S.-
dc.date.accessioned2020-11-18T06:08:17Z-
dc.date.available2020-11-18T06:08:17Z-
dc.date.issued2019-
dc.identifier.citationToxicon, 172, pp. 15-18.en_US
dc.identifier.otherhttps://doi.org/10.1016/j.toxicon.2019.10.240-
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S0041010119307238?via%3Dihub-
dc.identifier.urihttp://hdl.handle.net/123456789/1754-
dc.description.abstractDespite continued destruction of human lives by snakebites, appreciable improvements in immunotherapies have not been made. We selected and characterized venom-specific single domain antibodies (sdAbs) from a constructed phage display library of camelid variable region of heavy chain of the heavy chain antibodies (VHHs). Secretory phospholipase A2-specific sdAbs neutralized venom-induced toxicity in vitro and in vivo. Such monoclonal sdAbs could serve as an alternative to help manage snakebites to save lives.en_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.subjectPhage displayen_US
dc.subjectMonoclonal Aben_US
dc.subjectsdAben_US
dc.subjectRVV envenomingen_US
dc.titleSecretory PLA2 specific single domain antibody neutralizes Russell viper venom induced cellular and organismal toxicityen_US
dc.typeArticleen_US
Appears in Collections:Research Articles

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