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Article

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

Blood - 1 Jul 2006

Rug Melanie, Prescott Stuart W, Fernandez Kate M, Cooke Brian M, Cowman Alan F

Abstract excerpt

Surface protrusions of Plasmodium falciparum-infected erythrocytes, called knobs, display focal aggregates of P falciparum erythrocyte membrane protein 1 (PfEMP1), the adhesion ligand binding endothelial-cell receptors. The resulting sequestration of infected erythrocytes in tissues represents an important factor in the course of fatalities in patients with malaria. The main component of knobs is the...

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Identifiers

PMID: 16507777
DOI: 10.1182/blood-2005-11-4624
PMCID: PMC1895844

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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The role of KAHRP domains in knob formation and cytoadherence of P falciparum-infected human erythrocytes.PMID 16507777Read ↗

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Exported Proteins Required for Virulence and Rigidity of Plasmodium falciparum-Infected Human ErythrocytesSemantic proximity Read ↗

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

An Exported Heat Shock Protein 40 Associates with Pathogenesis-Related Knobs in Plasmodium falciparum Infected ErythrocytesSemantic proximity Read ↗

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Role of Plasmodium falciparum Protein GEXP07 in Maurer’s Cleft Morphology, Knob Architecture, and P. falciparum EMP1 TraffickingSemantic proximity Read ↗

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