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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Bibliographic Details
Main Authors: Cahyo, Budiman, Carlmond, Goh Kah Wun, Lee, Ping Chin, Rafida, Razali, Thean, Chor Leow
Format: Article
Language:en
Published: Universiti Malaysia Sabah (UMS) 2020
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Online Access:http://ir.unimas.my/id/eprint/48747/3/REASSESSMENT%20-%20Copy.pdf
http://ir.unimas.my/id/eprint/48747/
https://jurcon.ums.edu.my/ojums/index.php/bijb/article/view/2602
https://doi.org/10.51200/bijb.vi.2602
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