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

Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2 (baebl).

Blood - 1 Jun 2003

Lobo Cheryl-Ann, Rodriguez Marilis, Reid Marion, Lustigman Sara

Abstract excerpt

We report in this paper that glycophorin C (GPC) is the receptor for PfEBP-2 (baebl, EBA-140), the newly identified erythrocyte binding ligand of Plasmodium falciparum. PfEBP-2 is a member of the Duffy binding-like erythrocyte binding protein (DBL-EBP) family. Although several reports have been published characterizing PfEBP-2, the identity of its erythrocytic receptor was still unknown. Using a combination of...

Read the complete abstract on PubMed

Topics

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

Share to Carrier Proteins
Share to Erythrocyte Membrane
Share to Glycophorins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to N-Acetylneuraminic Acid

Share to Plasmodium falciparum

Share to Protozoan Proteins

Share to Receptors, Cell Surface

Share to Sequence Deletion

Source

Identifiers

PMID: 12576308
DOI: 10.1182/blood-2002-10-3076

Genes

EBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2 (baebl).PMID 12576308Read ↗

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

Critical glycosylated residues in exon three of erythrocyte glycophorin A engage Plasmodium falciparum EBA-175 and define receptor specificity.Semantic proximity Read ↗

Genetic Evidence for Erythrocyte Receptor Glycophorin B Expression Levels Defining a Dominant Plasmodium falciparum Invasion Pathway into Human ErythrocytesSemantic proximity Read ↗

A Novel Erythrocyte Binding Protein of Plasmodium vivax Suggests an Alternate Invasion Pathway into Duffy-Positive ReticulocytesSemantic proximity Read ↗

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

Targeted disruption of an erythrocyte binding antigen in Plasmodium falciparum is associated with a switch toward a sialic acid-independent pathway of invasion.Semantic proximity Read ↗

Crystal and Solution Structures of Plasmodium falciparum Erythrocyte-binding Antigen 140 Reveal Determinants of Receptor Specificity during Erythrocyte InvasionSemantic proximity Read ↗

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

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

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

Erythrocyte-binding antigen 175 mediates invasion in Plasmodium falciparum utilizing sialic acid-dependent and -independent pathways.Semantic proximity Read ↗

The cytoplasmic domain of the Plasmodium falciparum ligand EBA-175 is essential for invasion but not protein trafficking.Semantic proximity Read ↗

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