Plasmodium actin is incompletely folded by heterologous protein-folding machinery and likely requires the native Plasmodium chaperonin complex to enter a mature functional state.
about
The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosolSurface attachment, promoted by the actomyosin system of Toxoplasma gondii is important for efficient gliding motility and invasionToxoplasma gondii F-actin forms an extensive filamentous network required for material exchange and parasite maturationApicomplexan actin polymerization depends on nucleation.Reconstitution of the core of the malaria parasite glideosome with recombinant Plasmodium class XIV myosin A and Plasmodium actin.The substrate specificity of eukaryotic cytosolic chaperonin CCT.
P2860
Plasmodium actin is incompletely folded by heterologous protein-folding machinery and likely requires the native Plasmodium chaperonin complex to enter a mature functional state.
description
2015 nî lūn-bûn
@nan
2015 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Plasmodium actin is incomplete ...... ter a mature functional state.
@ast
Plasmodium actin is incomplete ...... ter a mature functional state.
@en
type
label
Plasmodium actin is incomplete ...... ter a mature functional state.
@ast
Plasmodium actin is incomplete ...... ter a mature functional state.
@en
prefLabel
Plasmodium actin is incomplete ...... ter a mature functional state.
@ast
Plasmodium actin is incomplete ...... ter a mature functional state.
@en
P2860
P356
P1433
P1476
Plasmodium actin is incomplete ...... ter a mature functional state.
@en
P2093
Hella Baumann
Maya A Olshina
P2860
P304
P356
10.1096/FJ.15-276618
P407
P577
2015-10-06T00:00:00Z