CPN60 co-localizes, binds and stabilizes PfClpP.

<p>A. A diagram depicting integration of a transgenic inactive PfClpP with a point mutation in the proteolytic active site (S264A) and a C-terminal Ty tag. CRISPR-mediated integration into the parasite’s genome under the endogenous <i>hsp110</i> promoter enables constant and modera...

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מחבר ראשי:	Amanda Tissawak (21762930) (author)
מחברים אחרים:	Yarden Rosin (21762933) (author), Shirly Katz Galay (21762936) (author), Alia Qasem (21762939) (author), Michal Shahar (15266558) (author), Nirit Trabelsi (21762942) (author), Ora Furman-Schueler (21762945) (author), Steven M. Johnson (17357) (author), Anat Florentin (21762948) (author)
יצא לאור:	2025
נושאים:	Biophysics Biochemistry Medicine Microbiology Cell Biology Genetics Pharmacology Evolutionary Biology Hematology Infectious Diseases Biological Sciences not elsewhere classified using genetic tools first replication cycle computational structural model additional targets outside previously unknown function synthesize essential biomolecules parasite death due div >< p cpn60 physically binds affect hs response apicoplast translation inhibitors apicoplast function work reveals taken together stable interface refolding safeguard plasmodium </ parasites serves organellar damage minimal control metabolic hub inactive forms immediately within heat shock evidence suggests eukaryotic cells endosymbiotic organelles directly involved conserved chaperonin close orthologues chaperonin inhibition cell nucleus caseinolytic protease balanced activities anti -<
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CPN60 co-localizes, binds and stabilizes PfClpP.

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