Structural analysis of the Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) intracellular domain reveals a conserved interaction epitope
about
A Plasmodium falciparum PHIST protein binds the virulence factor PfEMP1 and comigrates to knobs on the host cell surfaceExpansion of Lysine-rich Repeats in Plasmodium Proteins Generates Novel Localisation Sequences that Target the Periphery of the Host ErythrocyteA conserved domain targets exported PHISTb family proteins to the periphery of Plasmodium infected erythrocytesCharacterization of the small exported Plasmodium falciparum membrane protein SEMP1The Plasmodium PHIST and RESA-Like Protein Families of Human and Rodent Malaria ParasitesAn exported heat shock protein 40 associates with pathogenesis-related knobs in Plasmodium falciparum infected erythrocytesPlasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeletonTargeted disruption of a ring-infected erythrocyte surface antigen (RESA)-like export protein gene in Plasmodium falciparum confers stable chondroitin 4-sulfate cytoadherence capacityA member of the Plasmodium falciparum PHIST family binds to the erythrocyte cytoskeleton component band 4.1Structure and regulatory interactions of the cytoplasmic terminal domains of serotonin transporter.A subset of group A-like var genes encodes the malaria parasite ligands for binding to human brain endothelial cellsMaurer's clefts, the enigma of Plasmodium falciparum.A spiral scaffold underlies cytoadherent knobs in Plasmodium falciparum-infected erythrocytes.Plasmodium Helical Interspersed Subtelomeric (PHIST) Proteins, at the Center of Host Cell Remodeling.Variant surface antigens of malaria parasites: functional and evolutionary insights from comparative gene family classification and analysis.Plasmodium falciparum-infected erythrocyte knob density is linked to the PfEMP1 variant expressedNMR contributions to structural dynamics studies of intrinsically disordered proteinsStructural analysis of P. falciparum KAHRP and PfEMP1 complexes with host erythrocyte spectrin suggests a model for cytoadherent knob protrusions.Cerebral malaria--clinical manifestations and pathogenesis.Dynamic association of PfEMP1 and KAHRP in knobs mediates cytoadherence during Plasmodium invasion.Protonation-dependent conformational variability of intrinsically disordered proteins.Protein-Specific Features Associated with Variability in Human Antibody Responses to Plasmodium falciparum Malaria Antigens.Repetitive sequences in malaria parasite proteins.PFI1785w: A highly conserved protein associated with pregnancy associated malaria.Proteome and Structural Organization of the Knob Complex on the Surface of the Plasmodium Infected Red Blood Cell.Interaction between the C. elegans centriolar protein SAS-5 and microtubules facilitates organelle assembly.SURGE complex of Plasmodium falciparum in the rhoptry-neck (SURFIN4.2-RON4-GLURP) contributes to merozoite invasion
P2860
Q27684513-3489BDB3-DB70-4D20-AB21-AE074E8F3164Q27972793-111A02D2-2B65-47DC-8DD8-A35FB8F14066Q27973884-D00DE8D6-384A-400E-A22E-05441B688232Q27974134-0FB721B7-CE46-4A51-9B94-338208848D99Q27974508-DA3761A9-D2EE-41A9-95D7-6EA8F0164939Q30039191-D589C2B3-AC87-4E15-A57D-2AA701B8645BQ30039477-409998BD-D8C2-4E9B-B3EA-E438A1789495Q30042328-5334BF81-8F23-4F74-ABD4-092E020CBAC2Q30043144-1E1FA8BD-4CCB-48EA-A100-3AB6AAD1F335Q34103328-FD842D1E-C2E7-47DD-91CB-ED73BD3ABD4FQ34276770-DEAF4BFD-E7E0-4333-93CC-77D793CA9F16Q34388395-1D87CBB5-CE0B-4961-A541-468F9FBE8E37Q34504148-CF669DA9-ED08-48C0-BFD7-27A9023CE021Q34539136-06C4FF11-4FCD-41B5-89BA-C95BAEE7141FQ34785832-ADDB65D6-1A3B-494B-A048-2531E0023512Q36177571-7501A4E9-A7D3-4506-BD4F-75D354452A25Q38198240-2A74B6BC-BB83-4EA3-9F07-428955EF1FFAQ38625607-F4FE4A29-B3C5-48C1-8FBC-E4F67CBC6624Q38690668-4D86181C-326C-4201-8264-CE60341AA01CQ41458208-F6729B02-EC0B-40D9-95DD-1BFC11EC4E2CQ42073011-0B84C5EE-DA41-4C18-878F-8890884AB558Q45939224-BFC0E277-9611-4A49-B15E-EBBE228EAB30Q46273301-0F29AE9C-18D8-410F-AA95-A6CD5CC16E7AQ46338646-D3068FD7-048F-4BB2-B754-DDF5050BB403Q47660775-E984CAAC-59DF-4C36-9850-854C33F1ABD2Q49788386-BA4A07C8-CC6C-47BE-BA76-87608F0A022AQ56345699-4ADB75CD-C167-4F98-A5B4-BABA7C51E092
P2860
Structural analysis of the Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) intracellular domain reveals a conserved interaction epitope
description
2012 nî lūn-bûn
@nan
2012 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մարտին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Structural analysis of the Pla ...... conserved interaction epitope
@ast
Structural analysis of the Pla ...... conserved interaction epitope
@en
Structural analysis of the Pla ...... conserved interaction epitope
@nl
type
label
Structural analysis of the Pla ...... conserved interaction epitope
@ast
Structural analysis of the Pla ...... conserved interaction epitope
@en
Structural analysis of the Pla ...... conserved interaction epitope
@nl
altLabel
Structural Analysis of the Pla ...... Conserved Interaction Epitope
@en
prefLabel
Structural analysis of the Pla ...... conserved interaction epitope
@ast
Structural analysis of the Pla ...... conserved interaction epitope
@en
Structural analysis of the Pla ...... conserved interaction epitope
@nl
P2093
P2860
P921
P3181
P356
P1476
Structural analysis of the Pla ...... conserved interaction epitope
@en
P2093
Christina Mayer
Ioannis Vakonakis
Leanne Slater
Michele C Erat
Robert Konrat
P2860
P304
P3181
P356
10.1074/JBC.M111.330779
P407
P577
2012-03-02T00:00:00Z