Identification of new PNEPs indicates a substantial non-PEXEL exportome and underpins common features in Plasmodium falciparum protein export
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Plasmodium falciparum Secretome in Erythrocyte and BeyondA Plasmodium falciparum PHIST protein binds the virulence factor PfEMP1 and comigrates to knobs on the host cell surfaceProteome mapping of Plasmodium: identification of the P. yoelii remodellomePTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytesExpansion of Lysine-rich Repeats in Plasmodium Proteins Generates Novel Localisation Sequences that Target the Periphery of the Host ErythrocyteProteomic analysis reveals novel proteins associated with the Plasmodium protein exporter PTEX and a loss of complex stability upon truncation of the core PTEX component, PTEX150Trafficking of the exported P. falciparum chaperone PfHsp70xStable Translocation Intermediates Jam Global Protein Export in Plasmodium falciparum Parasites and Link the PTEX Component EXP2 with Translocation ActivityAlternative Protein Secretion in the Malaria Parasite Plasmodium falciparumThe Plasmodium falciparum exportome contains non-canonical PEXEL/HT proteinsA conserved domain targets exported PHISTb family proteins to the periphery of Plasmodium infected erythrocytesCharacterization of the small exported Plasmodium falciparum membrane protein SEMP1Exported Epoxide Hydrolases Modulate Erythrocyte Vasoactive Lipids during Plasmodium falciparum InfectionPlasmodium falciparum transfected with ultra bright NanoLuc luciferase offers high sensitivity detection for the screening of growth and cellular trafficking inhibitorscAMP-Signalling Regulates Gametocyte-Infected Erythrocyte Deformability Required for Malaria Parasite TransmissionThe chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosolPlasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeletonA genetic system to study Plasmodium falciparum protein functionPTEX is an essential nexus for protein export in malaria parasitesIdentity of a Plasmodium lactate/H(+) symporter structurally unrelated to human transportersP-selectin is a host receptor for Plasmodium MSP7 ligandsHomology-Based Prediction of Potential Protein-Protein Interactions between Human Erythrocytes and Plasmodium falciparum.Identification of malaria parasite-infected red blood cell surface aptamers by inertial microfluidic SELEX (I-SELEX).Malaria: Protein-export pathway illuminatedMaurer's clefts, the enigma of Plasmodium falciparum.Plasmodium Helical Interspersed Subtelomeric (PHIST) Proteins, at the Center of Host Cell Remodeling.Experimental determination of the membrane topology of the Plasmodium protease Plasmepsin VIn Vivo Function of PTEX88 in Malaria Parasite Sequestration and Virulence.Plasmodial HSP70s are functionally adapted to the malaria parasite life cycleContrasting Inducible Knockdown of the Auxiliary PTEX Component PTEX88 in P. falciparum and P. berghei Unmasks a Role in Parasite Virulence.Plasmodium falciparum Protein Microarray Antibody Profiles Correlate With Protection From Symptomatic Malaria in KenyaExport of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding.Feeling at home from arrival to departure: protein export and host cell remodelling during Plasmodium liver stage and gametocyte maturation.Protein export in malaria parasites: an update.Plasmodial Hsp40 and Hsp70 chaperones: current and future perspectives.Structural analysis of P. falciparum KAHRP and PfEMP1 complexes with host erythrocyte spectrin suggests a model for cytoadherent knob protrusions.The exported chaperone Hsp70-x supports virulence functions for Plasmodium falciparum blood stage parasites.Regulation of PfEMP1-VAR2CSA translation by a Plasmodium translation-enhancing factor.The aspartyl protease TgASP5 mediates the export of the Toxoplasma GRA16 and GRA24 effectors into host cells.Hemoglobin S and C affect protein export in Plasmodium falciparum-infected erythrocytes.
P2860
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P1343
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P2860
Identification of new PNEPs indicates a substantial non-PEXEL exportome and underpins common features in Plasmodium falciparum protein export
description
2013 nî lūn-bûn
@nan
2013 թուականին հրատարակուած գիտական յօդուած
@hyw
2013 թվականին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Identification of new PNEPs in ...... dium falciparum protein export
@ast
Identification of new PNEPs in ...... dium falciparum protein export
@en
Identification of new PNEPs in ...... dium falciparum protein export
@nl
type
label
Identification of new PNEPs in ...... dium falciparum protein export
@ast
Identification of new PNEPs in ...... dium falciparum protein export
@en
Identification of new PNEPs in ...... dium falciparum protein export
@nl
prefLabel
Identification of new PNEPs in ...... dium falciparum protein export
@ast
Identification of new PNEPs in ...... dium falciparum protein export
@en
Identification of new PNEPs in ...... dium falciparum protein export
@nl
P2093
P2860
P50
P921
P3181
P1433
P1476
Identification of new PNEPs in ...... dium falciparum protein export
@en
P2093
Alexander Oberli
Arlett Heiber
Christian Pick
Florian Kruse
Hanno Schoeler
Leonie Hecht
Madhusudan Kadekoppala
Paolo Mesén-Ramírez
Silke Retzlaff
Tim-Wolf Gilberger
P2860
P304
P3181
P356
10.1371/JOURNAL.PPAT.1003546
P407
P577
2013-08-08T00:00:00Z