Plasmodium falciparum erythrocyte invasion through glycophorin C and selection for Gerbich negativity in human populations
about
How malaria has affected the human genome and what human genetics can teach us about malariaThe cellular and molecular basis for malaria parasite invasion of the human red blood cellCrossing the line: selection and evolution of virulence traitsInvasion by P. falciparum merozoites suggests a hierarchy of molecular interactionsBasigin is a receptor essential for erythrocyte invasion by Plasmodium falciparumMolecular evolution of GYPC: evidence for recent structural innovation and positive selection in humansMerozoite surface proteins in red blood cell invasion, immunity and vaccines against malariaThe influence of host genetics on erythrocytes and malaria infection: is there therapeutic potential?A novel erythrocyte binding antigen-175 paralogue from Plasmodium falciparum defines a new trypsin-resistant receptor on human erythrocytesAntibodies to reticulocyte binding protein-like homologue 4 inhibit invasion of Plasmodium falciparum into human erythrocytesThe glycophorin C N-linked glycan is a critical component of the ligand for the Plasmodium falciparum erythrocyte receptor BAEBL.PfRH2b specific monoclonal antibodies inhibit merozoite invasionPlasmodium falciparum merozoite invasion is inhibited by antibodies that target the PfRh2a and b binding domainsComplement receptor 1 is a sialic acid-independent erythrocyte receptor of Plasmodium falciparumInsights into Duffy Binding-like Domains through the Crystal Structure and Function of the Merozoite Surface Protein MSPDBL2 from Plasmodium falciparumCrystal and Solution Structures of Plasmodium falciparum Erythrocyte-binding Antigen 140 Reveal Determinants of Receptor Specificity during Erythrocyte InvasionMolecular Basis for Sialic Acid-dependent Receptor Recognition by the Plasmodium falciparum Invasion Protein Erythrocyte-binding Antigen-140/BAEBLUsing mutagenesis and structural biology to map the binding site for the Plasmodium falciparum merozoite protein PfRh4 on the human immune adherence receptor.STEVOR is a Plasmodium falciparum erythrocyte binding protein that mediates merozoite invasion and rosettingAnalyses of interactions between heparin and the apical surface proteins of Plasmodium falciparumHuman erythrocyte band 3 functions as a receptor for the sialic acid-independent invasion of Plasmodium falciparum. Role of the RhopH3-MSP1 complexNovel putative glycosylphosphatidylinositol-anchored micronemal antigen of Plasmodium falciparum that binds to erythrocytesSemaphorin-7A is an erythrocyte receptor for P. falciparum merozoite-specific TRAP homolog, MTRAPA novel DBL-domain of the P. falciparum 332 molecule possibly involved in erythrocyte adhesionBinding of Plasmodium falciparum Merozoite Surface Proteins DBLMSP and DBLMSP2 to Human Immunoglobulin M Is Conserved among Broadly Diverged Sequence VariantsA Presenilin-like protease associated with Plasmodium falciparum micronemes is involved in erythrocyte invasionRecent advances in malaria genomics and epigenomicsGenetic conservation of the GIL blood group determining aquaporin 3 gene in African and Caucasian populationsHost reticulocytes provide metabolic reservoirs that can be exploited by malaria parasitesThe Binding of Plasmodium falciparum Adhesins and Erythrocyte Invasion Proteins to Aldolase Is Enhanced by PhosphorylationGlycophorins, Blood Groups, and Protection from Severe MalariaEvidence of functional divergence in MSP7 paralogous proteins: a molecular-evolutionary and phylogenetic analysisPlasmodium falciparum ligand binding to erythrocytes induce alterations in deformability essential for invasionAn EGF-like protein forms a complex with PfRh5 and is required for invasion of human erythrocytes by Plasmodium falciparumIntramembrane proteolysis mediates shedding of a key adhesin during erythrocyte invasion by the malaria parasiteComplement receptor 1 is the host erythrocyte receptor for Plasmodium falciparum PfRh4 invasion ligand.Systematic genetic analysis of the Plasmodium falciparum MSP7-like family reveals differences in protein expression, location, and importance in asexual growth of the blood-stage parasitePfRH5: a novel reticulocyte-binding family homolog of plasmodium falciparum that binds to the erythrocyte, and an investigation of its receptorFunctions of red cell surface proteins.Plasmodium falciparum uses a key functional site in complement receptor type-1 for invasion of human erythrocytes.
P2860
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P2860
Plasmodium falciparum erythrocyte invasion through glycophorin C and selection for Gerbich negativity in human populations
description
2002 nî lūn-bûn
@nan
2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Plasmodium falciparum erythroc ...... egativity in human populations
@ast
Plasmodium falciparum erythroc ...... egativity in human populations
@en
Plasmodium falciparum erythroc ...... egativity in human populations
@nl
type
label
Plasmodium falciparum erythroc ...... egativity in human populations
@ast
Plasmodium falciparum erythroc ...... egativity in human populations
@en
Plasmodium falciparum erythroc ...... egativity in human populations
@nl
prefLabel
Plasmodium falciparum erythroc ...... egativity in human populations
@ast
Plasmodium falciparum erythroc ...... egativity in human populations
@en
Plasmodium falciparum erythroc ...... egativity in human populations
@nl
P2860
P50
P921
P356
P1433
P1476
Plasmodium falciparum erythroc ...... egativity in human populations
@en
P2093
Peter A Zimmerman
Sheral S Patel
P2860
P2888
P356
10.1038/NM807
P407
P577
2002-12-09T00:00:00Z