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

Single-molecule imaging and quantification of the immune-variant adhesin VAR2CSA on knobs of Plasmodium falciparum-infected erythrocytes

8 May 2019

Abstract excerpt

Abstract PfEMP1 (erythrocyte membrane protein 1) adhesins play a pivotal role in the pathophysiology of falciparum malaria, by mediating sequestration of Plasmodium falciparum-infected erythrocytes in the microvasculature. PfEMP1 variants are expressed by var genes and are presented on membrane elevations, termed knobs. However, the organization of PfEMP1 on knobs is largely unclear. Here, we use super-resolution...

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 Lipid Membrane Structure and Behavior
Share to Malaria Research and Control

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 31098405
DOI: 10.1038/s42003-019-0429-z

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

Single-molecule imaging and quantification of the immune-variant adhesin VAR2CSA on knobs of Plasmodium falciparum-infected erythrocytesPMID 31098405Read ↗

Abnormal PfEMP1/knob display on Plasmodium falciparum-infected erythrocytes containing hemoglobin variants: fresh insights into malaria pathogenesis and protectionSemantic proximity Read ↗

Hemoglobin C modulates the surface topography of Plasmodium falciparum-infected erythrocytes.Semantic proximity Read ↗

Knobs, Adhesion, and Severe Falciparum MalariaSemantic proximity Read ↗

The role of KAHRP domains in knob formation and cytoadherence of P falciparum-infected human erythrocytes.Semantic proximity Read ↗

Architecture of Human IgM in Complex with P. falciparum Erythrocyte Membrane Protein 1Semantic proximity Read ↗

Structural Analysis of the Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) Intracellular Domain Reveals a Conserved Interaction EpitopeSemantic proximity Read ↗

<i>Plasmodium falciparum Plasmodium</i>helical interspersed subtelomeric proteins contribute to cytoadherence and anchor<i>P. falciparum</i>erythrocyte membrane protein 1 to the host cell cytoskeletonSemantic proximity Read ↗

Localisation-based imaging of malarial antigens during erythrocyte entry reaffirms a role for AMA1 but not MTRAP in invasionSemantic proximity Read ↗

Targeted Gene Disruption Shows That Knobs Enable Malaria-Infected Red Cells to Cytoadhere under Physiological Shear StressSemantic proximity Read ↗

Multiple stiffening effects of nanoscale knobs on human red blood cells infected with <i>Plasmodium falciparum</i> malaria parasiteSemantic proximity Read ↗

Type of in vitro cultivation influences cytoadhesion, knob structure, protein localization and transcriptome profile of Plasmodium falciparumSemantic proximity Read ↗

A <i>Plasmodium falciparum</i> PHIST protein binds the virulence factor PfEMP1 and comigrates to knobs on the host cell surfaceSemantic proximity Read ↗

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