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

Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers.

Nature communications - 1 Jan 2012

Muralidharan Vasant, Oksman Anna, Pal Priya, Lindquist Susan, Goldberg Daniel E

Abstract excerpt

One-fourth of Plasmodium falciparum proteins have asparagine repeats that increase the propensity for aggregation, especially at elevated temperatures that occur routinely in malaria-infected patients. Here we report that a Plasmodium Asn repeat-containing protein (PFI1155w) formed aggregates in mammalian cells at febrile temperatures, as did a yeast Asn/Gln-rich protein (Sup35). Co-expression of the cytoplasmic...

Read the complete abstract on PubMed

Topics

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

Share to Asparagine
Share to Chaperonin 10

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Knockdown Techniques

Share to Malaria, Falciparum

Share to Plasmodium falciparum

Share to Proteome

Share to Repetitive Sequences, Amino Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 23250440
DOI: 10.1038/ncomms2306
PMCID: PMC3639100

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers.PMID 23250440Read ↗

Plasmodium falciparum heat shock proteins as antimalarial drug targets: An updateSemantic proximity Read ↗

Partners in Mischief: Functional Networks of Heat Shock Proteins of Plasmodium falciparum and Their Influence on Parasite VirulenceSemantic proximity Read ↗

Suppression of aggregate and amyloid formation by a novel intrinsically disordered region in metazoan Hsp110 chaperonesSemantic proximity Read ↗

The heat shock protein 40 family of the malaria parasite <i>Plasmodium falciparum</i>Semantic proximity Read ↗

The exported chaperone PfHsp70x is dispensable for the <i>Plasmodium falciparum</i> intraerythrocytic lifecycleSemantic proximity Read ↗

Essential role for HSP40 in asexual replication and thermotolerance of malaria parasitesSemantic proximity Read ↗

Plasmodium falciparum-encoded exported hsp70/hsp40 chaperone/co-chaperone complexes within the host erythrocyteSemantic proximity Read ↗

Activation mechanism of small heat shock protein HSPB5 revealed by disease-associated mutants.Semantic proximity Read ↗

Plasmodium falciparum Molecular Chaperones: Guardians of the Malaria Parasite Proteome and Renovators of the Host ProteomeSemantic proximity Read ↗

The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum.Semantic proximity Read ↗

The PfAP2-HS transcription factor protects malaria parasites from febrile temperaturesSemantic proximity Read ↗

Plasmodial HSP70s are functionally adapted to the malaria parasite life cycleSemantic proximity Read ↗

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