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

The Exported Protein PbCP1 Localises to Cleft-Like Structures in the Rodent Malaria Parasite Plasmodium berghei

26 Apr 2013

Abstract excerpt

Protein export into the host red blood cell is one of the key processes in the pathobiology of the malaria parasite Plasmodiumtrl falciparum, which extensively remodels the red blood cell to ensure its virulence and survival. In this study, we aimed to shed further light on the protein export mechanisms in the rodent malaria parasite P. berghei and provide further proof of the conserved nature of host cell...

Read the complete abstract on PubMed

Topics

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

Share to Drug Transport and Resistance Mechanisms
Share to Malaria Research and Control
Share to Mosquito-borne diseases and control

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 23658610
DOI: 10.1371/journal.pone.0061482

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Exported Protein PbCP1 Localises to Cleft-Like Structures in the Rodent Malaria Parasite Plasmodium bergheiPMID 23658610Read ↗

New insights into protein export in malaria parasitesSemantic proximity Read ↗

Proteomic and genetic analyses demonstrate that Plasmodium berghei blood stages export a large and diverse repertoire of proteins.Semantic proximity Read ↗

An exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytesSemantic proximity Read ↗

A repeat sequence domain of the ring-exported protein-1 of Plasmodium falciparum controls export machinery architecture and virulence protein trafficking.Semantic proximity Read ↗

PEXEL is a proteolytic maturation site for both exported and non-exported <i>Plasmodium</i> proteinsSemantic proximity Read ↗

Protein export in malaria parasites: an updateSemantic proximity Read ↗

A revised mechanism for how Plasmodium falciparum recruits and exports proteins into its erythrocytic host cellSemantic proximity Read ↗

Illuminating how malaria parasites export proteins into host erythrocytesSemantic proximity Read ↗

Lineage-specific expansion of proteins exported to erythrocytes in malaria parasitesSemantic proximity Read ↗

Contrasting Inducible Knockdown of the Auxiliary PTEX Component PTEX88 in P. falciparum and P. berghei Unmasks a Role in Parasite VirulenceSemantic proximity Read ↗

A Plasmodium homolog of ER tubule‐forming proteins is required for parasite virulenceSemantic proximity Read ↗

<i>In Vivo</i> Function of PTEX88 in Malaria Parasite Sequestration and VirulenceSemantic proximity Read ↗

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