Reticulocyte binding protein homologues are key adhesins during erythrocyte invasion by Plasmodium falciparum
about
The Genome of Haemoproteus tartakovskyi and Its Relationship to Human Malaria ParasitesPfRH2b specific monoclonal antibodies inhibit merozoite invasionPlasmodium falciparum merozoite invasion is inhibited by antibodies that target the PfRh2a and b binding domainsPlasmodium falciparum Adhesins Play an Essential Role in Signalling and Activation of Invasion into Human ErythrocytesStructural Determination of Functional Units of the Nucleotide Binding Domain (NBD94) of the Reticulocyte Binding Protein Py235 of Plasmodium yoeliiUsing mutagenesis and structural biology to map the binding site for the Plasmodium falciparum merozoite protein PfRh4 on the human immune adherence receptor.Targeting and function of proteins mediating translation initiation in organelles of Plasmodium falciparumAnalyses of interactions between heparin and the apical surface proteins of Plasmodium falciparumPlasmodium falciparum glucose-6-phosphate dehydrogenase 6-phosphogluconolactonase is a potential drug targetA thrombospondin structural repeat containing rhoptry protein from Plasmodium falciparum mediates erythrocyte invasionInhibition of Plasmepsin V activity demonstrates its essential role in protein export, PfEMP1 display, and survival of malaria parasitesThe Plasmodium rhoptry associated protein complex is important for parasitophorous vacuole membrane structure and intraerythrocytic parasite growthAn EGF-like protein forms a complex with PfRh5 and is required for invasion of human erythrocytes by Plasmodium falciparumA dual-targeted aminoacyl-tRNA synthetase in Plasmodium falciparum charges cytosolic and apicoplast tRNACysComplement activation by merozoite antigens of Plasmodium falciparumTriggers of key calcium signals during erythrocyte invasion by Plasmodium falciparumPlasmodium falciparum reticulocyte binding-like homologue protein 2 (PfRH2) is a key adhesive molecule involved in erythrocyte invasion.The moving junction protein RON8 facilitates firm attachment and host cell invasion in Toxoplasma gondii.An update on the rapid advances in malaria parasite cell biology.Crystallographic studies of the coupling segment NBD94(674-781) of the nucleotide-binding domain of the Plasmodium yoelii reticulocyte-binding protein Py235.Reticulocyte and erythrocyte binding-like proteins function cooperatively in invasion of human erythrocytes by malaria parasitesCharacterization of Inhibitors and Monoclonal Antibodies That Modulate the Interaction between Plasmodium falciparum Adhesin PfRh4 with Its Erythrocyte Receptor Complement Receptor 1.Two functional reticulocyte binding-like (RBL) invasion ligands of zoonotic Plasmodium knowlesi exhibit differential adhesion to monkey and human erythrocytes.Red blood cell polymorphism and susceptibility to Plasmodium vivax.The role of the reticulocyte-binding-like protein homologues of Plasmodium in erythrocyte sensing and invasion.Differences in erythrocyte receptor specificity of different parts of the Plasmodium falciparum reticulocyte binding protein homologue 2a.Evidence that the Plasmodium falciparum Protein Sortilin Potentially Acts as an Escorter for the Trafficking of the Rhoptry-Associated Membrane Antigen to the Rhoptries.
P2860
Q26315344-4D1A3974-90D9-4D49-9A74-E63FDCBAD290Q27230101-68474F07-1E05-4A47-9BD3-696A9AFF5061Q27230103-EA8B7083-7084-48CF-B8B1-85E0A5601B5FQ27316537-DD9CEE05-801A-4122-81BC-524F3929FAD1Q27659886-029FDF0B-9E9C-49A0-A44D-C2106CA29D9CQ27680572-F81FB089-C27E-425C-AE00-E699D98E0934Q27972663-ED6D616D-7668-4388-A210-1C9F99342439Q27972735-546938FA-AD9A-4676-8C6E-F95749BD728AQ27974089-5B41C688-48BD-46B7-BFBF-C9EE2F424A1FQ27974332-CB052A62-A72F-43BF-9BC6-C412FE08D81DQ28540204-1D2733AD-638B-4E58-B3E4-8F6729F0FD33Q30042719-1876B88C-3D6B-4C63-B84F-36EE8ED590E9Q30043132-B1AA5DBC-129C-48DC-A8B2-D14933A39BB2Q30044413-37DCAE3A-98D5-434A-AF6B-50E1EF72FE73Q30411191-D7EFA54B-F65A-4AEC-ADBF-25F0B12CED3BQ30560148-E425D3A3-44A9-4F32-B1EF-7C83681BCF73Q33840763-E2F2775B-743D-4D78-98EE-40193717755BQ33851492-FCE7C3D8-0D12-40BE-BDAA-E30A6A183083Q33905946-35B48E0A-2753-4A50-AFC6-AEB96F138424Q34387264-A05DFC6F-644A-4C94-9AD6-1E619D53F818Q34739631-6CA93817-7AA4-4FCB-8EAE-972E33AB88C3Q36283289-492D4596-26F6-4330-A581-078010381AFCQ36298824-9C8C43C5-F106-4302-AA89-80DEA86A0306Q37058815-55966B95-93BC-4802-A83C-46967D6A65F4Q38050526-73202938-5728-4660-8BD6-ED63EE1D4E00Q42153182-ADFC931D-381B-406B-86C0-6B00D930C64CQ47096088-2B94A0CE-1BF5-4584-B818-3028ABB68E4A
P2860
Reticulocyte binding protein homologues are key adhesins during erythrocyte invasion by Plasmodium falciparum
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 13 July 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Reticulocyte binding protein h ...... asion by Plasmodium falciparum
@en
Reticulocyte binding protein h ...... sion by Plasmodium falciparum.
@nl
type
label
Reticulocyte binding protein h ...... asion by Plasmodium falciparum
@en
Reticulocyte binding protein h ...... sion by Plasmodium falciparum.
@nl
prefLabel
Reticulocyte binding protein h ...... asion by Plasmodium falciparum
@en
Reticulocyte binding protein h ...... sion by Plasmodium falciparum.
@nl
P2860
P50
P921
P1476
Reticulocyte binding protein h ...... asion by Plasmodium falciparum
@en
P2093
Anthony Hodder
P2860
P304
P356
10.1111/J.1462-5822.2009.01358.X
P577
2009-07-13T00:00:00Z