Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Polymorphism in the Plasmodium falciparum erythrocyte-binding ligand JESEBL/EBA-181 alters its receptor specificity

11 Feb 2004

Abstract excerpt

The malaria parasite lives within erythrocytes and depends on the binding of parasite ligands to host cell surface receptors for invasion. The most virulent human malaria parasite, Plasmodium falciparum, uses multiple ligands, including EBA-175, BAEBL, and JESEBL of the Duffy-binding-like (DBL) family of erythrocyte-binding proteins, for invasion of human erythrocytes. Region II of these parasite ligands is the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Complement system in diseases
Share to Drug Transport and Resistance Mechanisms
Share to Malaria Research and Control

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 14983041
DOI: 10.1073/pnas.0307318101

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Polymorphism in the Plasmodium falciparum erythrocyte-binding ligand JESEBL/EBA-181 alters its receptor specificityPMID 14983041Read ↗

Polymorphism in a <i>Plasmodium falciparum</i> Erythrocyte-binding Ligand Changes Its Receptor SpecificitySemantic proximity Read ↗

Polymorphisms in Erythrocyte Binding Antigens 140 and 181 Affect Function and Binding but Not Receptor Specificity in <i>Plasmodium falciparum</i>Semantic proximity Read ↗

Glycophorin B is the erythrocyte receptor of <i>Plasmodium falciparum</i> erythrocyte-binding ligand, EBL-1Semantic proximity Read ↗

A novel erythrocyte binding antigen-175 paralogue from Plasmodium falciparum defines a new trypsin-resistant receptor on human erythrocytes.Semantic proximity Read ↗

An analysis of genetic diversity within the ligand domains of the Plasmodium falciparum ebl-1 gene.Semantic proximity Read ↗

A novel Plasmodium falciparum erythrocyte binding protein-2 (EBP2/BAEBL) involved in erythrocyte receptor bindingSemantic proximity Read ↗

Prevalence of 5' insertion mutants and analysis of single nucleotide polymorphism in the erythrocyte binding-like 1 (ebl-1) gene in Kenyan Plasmodium falciparum field isolates.Semantic proximity Read ↗

The glycophorin C N-linked glycan is a critical component of the ligand for the Plasmodium falciparum erythrocyte receptor BAEBL.Semantic proximity Read ↗

Natural genetic diversity of the DBL domain of a novel member of the Plasmodium vivax erythrocyte binding-like proteins (EBP2) in the Amazon rainforest.Semantic proximity Read ↗

Reticulocyte and Erythrocyte Binding-Like Proteins Function Cooperatively in Invasion of Human Erythrocytes by Malaria ParasitesSemantic proximity Read ↗

Erythrocyte-binding antigens of Plasmodium falciparum are targets of human inhibitory antibodies and function to evade naturally acquired immunity.Semantic proximity Read ↗

Characterization of a Plasmodium falciparum erythrocyte-binding protein paralogous to EBA-175.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.