Parasite-encoded Hsp40 proteins define novel mobile structures in the cytosol of the P. falciparum-infected erythrocyte
about
Selection and refinement: the malaria parasite's infection and exploitation of host hepatocytesThe exported protein PbCP1 localises to cleft-like structures in the rodent malaria parasite Plasmodium bergheiPTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytesTrafficking of PfExp1 to the parasitophorous vacuolar membrane of Plasmodium falciparum is independent of protein folding and the PTEX transloconPlasmodium falciparum Hsp70-x: a heat shock protein at the host-parasite interfaceTrafficking of the exported P. falciparum chaperone PfHsp70xThe Malarial Exported PFA0660w Is an Hsp40 Co-Chaperone of PfHsp70-xThe Plasmodium falciparum exportome contains non-canonical PEXEL/HT proteinsCharacterization of the small exported Plasmodium falciparum membrane protein SEMP1The Plasmodium PHIST and RESA-Like Protein Families of Human and Rodent Malaria ParasitesNew Export Pathway in Plasmodium falciparum-Infected Erythrocytes: Role of the Parasite Group II Chaperonin, PfTRiCHost cell remodeling by pathogens: the exomembrane system in Plasmodium-infected erythrocytesPlasmodium falciparum antigen 332 is a resident peripheral membrane protein of Maurer's cleftsThe chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosolIdentification of a Plasmodium falciparum phospholipid transfer proteinAn exported heat shock protein 40 associates with pathogenesis-related knobs in Plasmodium falciparum infected erythrocytesProteomic and genetic analyses demonstrate that Plasmodium berghei blood stages export a large and diverse repertoire of proteinsExport of virulence proteins by malaria-infected erythrocytes involves remodeling of host actin cytoskeletonHost erythrocyte environment influences the localization of exported protein 2, an essential component of the Plasmodium translocon.Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shockProteomic analysis of exported chaperone/co-chaperone complexes of P. falciparum reveals an array of complex protein-protein interactionsAn exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytesP. falciparum modulates erythroblast cell gene expression in signaling and erythrocyte production pathways.Maurer's clefts, the enigma of Plasmodium falciparum.Plasmodium Helical Interspersed Subtelomeric (PHIST) Proteins, at the Center of Host Cell Remodeling.Plasmodial HSP70s are functionally adapted to the malaria parasite life cycleThe exported Plasmodium berghei protein IBIS1 delineates membranous structures in infected red blood cells.Spatial and temporal mapping of the PfEMP1 export pathway in Plasmodium falciparum.Identification of an exported heat shock protein 70 in Plasmodium falciparum.Protein export in malaria parasites: many membranes to cross.The heat shock protein 40 family of the malaria parasite Plasmodium falciparum.Human erythrocyte remodelling during Plasmodium falciparum malaria parasite growth and egress.Protein export in malaria parasites: an update.Plasmodial Hsp40 and Hsp70 chaperones: current and future perspectives.A conserved co-chaperone is required for virulence in fungal plant pathogens.Chaperone expression profiles correlate with distinct physiological states of Plasmodium falciparum in malaria patients.Functional analysis of Plasmodium vivax VIR proteins reveals different subcellular localizations and cytoadherence to the ICAM-1 endothelial receptor.PHISTc protein family members localize to different subcellular organelles and bind Plasmodium falciparum major virulence factor PfEMP-1.A seven-helix protein constitutes stress granules crucial for regulating translation during human-to-mosquito transmission of Plasmodium falciparum
P2860
Q27025899-A213DFF5-49EC-4177-9B5E-645DC088AA99Q27324734-476F027E-ECA3-4AEF-B6A7-532CB84FB5EAQ27972589-5D9B723C-2240-4EF9-8D42-BB03F76DA3AFQ27972779-4EDDE740-7744-48B7-9AFA-DC78CD61DE1FQ27972950-2B686963-7BED-4634-8627-BAC182E1F4B7Q27972952-2B741B5C-27E9-4A68-AA7C-17CE7E8D3F4FQ27972953-042AA1E1-E933-45D3-8DBE-153ABAF3ABCCQ27973779-B22E492A-19DF-4800-8602-BF6AE6D94538Q27974134-DCB3E027-8BD4-4369-8586-960DB18F6604Q27974508-DB637392-83A7-45C5-B0F0-251C2A3DF797Q27976478-D3857CA4-45C6-4B7C-B58C-FFEEE1945300Q28072465-16071F25-C815-45B7-B09F-53C3C22A6789Q28485271-32425527-2AF4-4973-982F-3D7DEF44B535Q30038962-A94EC9A0-A417-4896-83B3-CF0E2A24FC42Q30039048-28EA2607-7B22-4998-A89A-9134D4B5B2F5Q30039191-F6569B7B-EAED-49AC-B86F-50BF187E620CQ30040949-B45F1369-0FC4-4B97-BBE6-53D61BCE9C57Q30042333-9BF3EFF7-A3AA-4B27-9B80-E067B398E65BQ30043299-DBA87765-59C9-43F9-9A1B-8AF7037F4B2FQ30047735-1A92A91C-D955-40DF-B146-8A7E1E39C889Q30839238-1C81D1AE-5F79-49D4-9EA5-1E29D9F90CB6Q33899922-C6F7BE41-83CA-4281-8AF7-B4AF3C802D96Q33900949-630FAC20-0CC3-48AE-A22B-A03A6B9AA5A2Q34388395-5FEB96C5-4011-4286-A81F-B002F418AFDEQ34539136-30C07306-2290-4B1B-9AFD-23F830415420Q35782885-07F064E3-00DF-4359-AB66-3D8159CE7726Q36413355-C01084E4-095F-42D0-8411-FF777C1270BFQ37014760-013D6B7A-4AC9-4853-9B71-50DDF4316890Q37032952-B6AB613C-0957-45F0-89F0-3004F580B561Q37126101-98414A67-6305-4D00-80C2-E72100CB1A0AQ37970046-CA2D0120-979E-435C-A914-9AD5DDF32DEFQ37982132-C30CB5D1-074D-4318-9F69-84B2E802D494Q38177979-F5BD927D-CB9F-4DC4-A95F-CA9812B67367Q38199259-C1580AAC-77E2-48AD-9A37-1944CD29652EQ40942879-C53B2964-7F70-402E-9CD2-2AAD58D9E860Q41969120-9148588D-178A-46A4-856E-11153093AF06Q44636278-70C8623C-F59F-43F9-B5F5-9A0DC1755CE0Q47384984-1DB3A644-DA9C-44F5-9A96-BA3A1B3FCA86Q56341962-A590D90B-9706-4A4C-8B83-DA92B4DA5B8E
P2860
Parasite-encoded Hsp40 proteins define novel mobile structures in the cytosol of the P. falciparum-infected erythrocyte
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Parasite-encoded Hsp40 protein ...... alciparum-infected erythrocyte
@ast
Parasite-encoded Hsp40 protein ...... alciparum-infected erythrocyte
@en
Parasite-encoded Hsp40 protein ...... alciparum-infected erythrocyte
@nl
type
label
Parasite-encoded Hsp40 protein ...... alciparum-infected erythrocyte
@ast
Parasite-encoded Hsp40 protein ...... alciparum-infected erythrocyte
@en
Parasite-encoded Hsp40 protein ...... alciparum-infected erythrocyte
@nl
prefLabel
Parasite-encoded Hsp40 protein ...... alciparum-infected erythrocyte
@ast
Parasite-encoded Hsp40 protein ...... alciparum-infected erythrocyte
@en
Parasite-encoded Hsp40 protein ...... alciparum-infected erythrocyte
@nl
P2093
P50
P921
P3181
P1476
Parasite-encoded Hsp40 protein ...... alciparum-infected erythrocyte
@en
P2093
Jude M Przyborski
Klaus Brinkmann
Klaus Lingelbach
Melanie Rug
Ping Cannon
Simone Külzer
P304
P3181
P356
10.1111/J.1462-5822.2010.01477.X
P407
P577
2010-10-01T00:00:00Z