ArticleParasitology research2007
Proof of interaction between Leishmania SIR2RP1 deacetylase and chaperone HSP83.
Article in Parasitology research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Heat Shock Protein 90 Regulates the Activity of Histone Deacetylase Sir2 in Plasmodium falciparum.mSphere · 2022Article
- Antimony susceptibility of Leishmania isolates collected over a 30-year period in Algeria.PLoS neglected tropical diseases · 2018Article
- Molecular Chaperones of Leishmania: Central Players in Many Stress-Related and -Unrelated Physiological Processes.BioMed research international · 2015Review
- The antileishmanial activity of isoforms 6- and 8-selective histone deacetylase inhibitors.Bioorganic & medicinal chemistry letters · 2014Article
- Potent antitrypanosomal activities of heat shock protein 90 inhibitors in vitro and in vivo.The Journal of infectious diseases · 2013Article
- Sirtuins of parasitic protozoa: in search of function(s).Molecular and biochemical parasitology · 2012Review
- A structure-activity relationship study of the antimalarial and antileishmanial activities of nonpeptide macrocyclic histone deacetylase inhibitors.ChemMedChem · 2010Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cytoplasmic Leishmania silent information regulator 2 (SIR2)RP1 protein is essential for parasite growth and survival and constitutes an attractive therapeutic target. Little information is available on putative substrate(s) and/or partner(s) that could shed light on the pathways in which this enzyme plays a role. We carried out co-immunoprecipitation experiments on the soluble fractions of wild-type and parasites overexpressing LmSIR2RP1 and found that the essential chaperone heat shock protein (HSP) 83, the Leishmania ortholog of the mammalian HSP90, constantly co-immunoprecipitated with LmSIR2RP1. We found that Leishmania HSP83 is among the lysine acetylated protein, but the intracellular level of SIR2RP1 does not influence the acetylation status of HSP83. Finally, the modified Geldanamycin susceptibility (an inhibitor of HSP83) exhibited by SIR2RP1 mutant parasites support an in vivo relationship between the chaperone activity of HSP83 and LmSIR2RP1. An insight on the nature of the interaction in Leishmania is required to understand its role in the cell fate control during cytodifferentiation.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.