Structural and functional importance of a non-catalytic domain of FKBP35 from Plasmodium knowlesi
A 35 kDa FK506-binding protein (FKBP35) from Plasmodium knowlesi (PkFKBP35) is considered as a viable target for development of antimalarial drugs without resistant effects. This protein is a member of peptidyl prolyl cis-trans isomerase (PPIase) with the ability to catalyze isomerization of cis-pro...
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Main Author: | Jovi Silvester |
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Format: | Thesis |
Language: | English |
Published: |
2019
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Subjects: | |
Online Access: | https://eprints.ums.edu.my/id/eprint/25123/1/Structural%20and%20functional%20importance%20of%20a%20non-catalytic%20domain%20of%20fkbp35%20from%20Plasmodium%20knowlesi.pdf |
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