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

Heparan sulfate on endothelial cells mediates the binding ofPlasmodium falciparum–infected erythrocytes via the DBL1α domain of PfEMP1

27 Feb 2003

Abstract excerpt

Plasmodium falciparum may cause severe forms of malaria when excessive sequestration of infected and uninfected erythrocytes occurs in vital organs. The capacity of wild-type isolates of P falciparum-infected erythrocytes (parasitized red blood cells [pRBCs]) to bind glycosaminoglycans (GAGs) such as heparin has been identified as a marker for severe disease. Here we report that pRBCs of the parasite FCR3S1.2 and...

Read the complete abstract on PubMed

Topics

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

Share to Research on Leishmaniasis Studies
Share to Toxoplasma gondii Research Studies
Share to Trypanosoma species research and implications

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 12433689
DOI: 10.1182/blood-2002-07-2016

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Heparan sulfate on endothelial cells mediates the binding ofPlasmodium falciparum–infected erythrocytes via the DBL1α domain of PfEMP1PMID 12433689Read ↗

Structure of a Plasmodium falciparum PfEMP1 rosetting domain reveals a role for the N-terminal segment in heparin-mediated rosette inhibition.Semantic proximity Read ↗

Molecular basis for the dichotomy in Plasmodium falciparum adhesion to CD36 and chondroitin sulfate A.Semantic proximity Read ↗

Rosetting Plasmodium falciparum-Infected Erythrocytes Bind to Human Brain Microvascular Endothelial Cells <i>In Vitro</i> , Demonstrating a Dual Adhesion Phenotype Mediated by Distinct P. falciparum Erythrocyte Membrane Protein 1 DomainsSemantic proximity Read ↗

CD36—A Host Receptor Necessary for Malaria Parasites to Establish and Maintain InfectionSemantic proximity Read ↗

Chondroitin sulfate proteoglycan but not hyaluronic acid is the receptor for the adherence of Plasmodium falciparum-infected erythrocytes in human placenta, and infected red blood cell adherence up-regulates the receptor expression.Semantic proximity Read ↗

Characterization of Proteoglycans of Human Placenta and Identification of Unique Chondroitin Sulfate Proteoglycans of the Intervillous Spaces That Mediate the Adherence ofPlasmodium falciparum-infected Erythrocytes to the PlacentaSemantic proximity Read ↗

Structural Requirements for the Adherence ofPlasmodium falciparum-infected Erythrocytes to Chondroitin Sulfate Proteoglycans of Human PlacentaSemantic proximity Read ↗

Investigating the host binding signature on the Plasmodium falciparum PfEMP1 protein family.Semantic proximity Read ↗

Chondroitin sulphate A (CSA)-binding of single recombinant Duffy-binding-like domains is not restricted to Plasmodium falciparum Erythrocyte Membrane Protein 1 expressed by CSA-binding parasites.Semantic proximity Read ↗

Complement C1s cleaves PfEMP1 at interdomain conserved sites inhibiting Plasmodium falciparum cytoadherenceSemantic proximity Read ↗

Dynamic interactions ofPlasmodiumspp. with vascular endotheliumSemantic proximity Read ↗

Binding of human serum proteins to Plasmodium falciparum-infected erythrocytes and its association with malaria clinical presentationSemantic proximity Read ↗

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