Reassessment of the Catalytic activity and substrate specificity of FKBP35 from Plasmodium Knowlesi using Protease-Free Assay
FK506-binding protein35 of Plasmodium knowlesi (Pk-FKBP35) is a member of peptidyl prolyl cis-trans isomerase (PPIase) and is considered as a promising avenue of antimalarial drug target development. This protein is organized into the N-terminal domain responsible for PPIase catalytic activity follo...
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| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English English |
| Published: |
Borneo International Journal of Biotechnology (BIJB)
2020
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| Online Access: | https://eprints.ums.edu.my/id/eprint/27448/1/Reassessment%20of%20the%20Catalytic%20activity%20and%20substrate%20specificity%20of%20FKBP35%20from%20Plasmodium%20Knowlesi%20using%20Protease-Free%20Assay%20abstract.pdf https://eprints.ums.edu.my/id/eprint/27448/2/Reassessment%20of%20the%20Catalytic%20activity%20and%20substrate%20specificity%20of%20FKBP35%20from%20Plasmodium%20Knowlesi%20using%20Protease-Free%20Assay%20FULLTEXT.pdf https://eprints.ums.edu.my/id/eprint/27448/ https://jurcon.ums.edu.my/ojums/index.php/bijb/article/view/2602 https://doi.org/10.51200/bijb.vi.2602 |
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https://eprints.ums.edu.my/id/eprint/27448/1/Reassessment%20of%20the%20Catalytic%20activity%20and%20substrate%20specificity%20of%20FKBP35%20from%20Plasmodium%20Knowlesi%20using%20Protease-Free%20Assay%20abstract.pdfhttps://eprints.ums.edu.my/id/eprint/27448/2/Reassessment%20of%20the%20Catalytic%20activity%20and%20substrate%20specificity%20of%20FKBP35%20from%20Plasmodium%20Knowlesi%20using%20Protease-Free%20Assay%20FULLTEXT.pdf
https://eprints.ums.edu.my/id/eprint/27448/
https://jurcon.ums.edu.my/ojums/index.php/bijb/article/view/2602
https://doi.org/10.51200/bijb.vi.2602