ArticleCell stress & chaperones2010
The co-chaperone SGT of Leishmania donovani is essential for the parasite's viability.
Article in Cell stress & chaperones, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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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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Who cites it
21 citing papers in PubMed, 41 citations in OpenAlex.
- Evolutionary remodeling of a remnant GET pathway factor into PEX38, an essential peroxin.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Hsp90 and associates shaping parasite biology.mSphere · 2025Review
- Transcriptome profiling of L. infantum-infected human macrophages reveals sex-specific type I interferon induction.PLoS pathogens · 2025Article
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- Promastigote-to-Amastigote Conversion inPathogens (Basel, Switzerland) · 2022Review
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- High Content Analysis of Macrophage-TargetingMicroorganisms · 2021Article
- Heat Shock Proteins as the Druggable Targets in Leishmaniasis: Promises and Perils.Infection and immunity · 2021Review
- Repurposing Carvedilol as a Novel Inhibitor of theFrontiers in cellular and infection microbiology · 2021Article
- Leishmania donovani 90 kD Heat Shock Protein - Impact of Phosphosites on Parasite Fitness, Infectivity and Casein Kinase Affinity.Scientific reports · 2019Article
- Hsp90 inhibitors radicicol and geldanamycin have opposing effects on Leishmania Aha1-dependent proliferation.Cell stress & chaperones · 2017Article
- MAPK1 of Leishmania donovani interacts and phosphorylates HSP70 and HSP90 subunits of foldosome complex.Scientific reports · 2017Article
- A Telomeric Cluster of Antimony Resistance Genes on Chromosome 34 of Leishmania infantum.Antimicrobial agents and chemotherapy · 2016Article
- Leishmania donovani P23 protects parasites against HSP90 inhibitor-mediated growth arrest.Cell stress & chaperones · 2015Article
- Molecular Chaperones of Leishmania: Central Players in Many Stress-Related and -Unrelated Physiological Processes.BioMed research international · 2015Review
- A small heat shock protein is essential for thermotolerance and intracellular survival of Leishmania donovani.Journal of cell science · 2014Article
- The cochaperone SGTA (small glutamine-rich tetratricopeptide repeat-containing protein alpha) demonstrates regulatory specificity for the androgen, glucocorticoid, and progesterone receptors.The Journal of biological chemistry · 2014Article
- Genetically modified organisms and visceral leishmaniasis.Frontiers in immunology · 2014Review
- Expression and clinical role of small glutamine-rich tetratricopeptide repeat (TPR)-containing protein alpha (SGTA) as a novel cell cycle protein in NSCLC.Journal of cancer research and clinical oncology · 2013Article
- The Hsp90-Sti1 interaction is critical for Leishmania donovani proliferation in both life cycle stages.Cellular microbiology · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular chaperone proteins play a pivotal role in the protozoan parasite Leishmania donovani, controlling cell fate and ensuring intracellular survival. In higher eukaryotes, the so-called co-chaperone proteins are required for client protein recognition and proper function of chaperones, among them the small glutamine-rich tetratricopeptide repeat proteins (SGT) which interact with both HSP70 and HSP90 chaperones. An atypical SGT homolog is found in the L. donovani genome, encoding a protein lacking the C-terminal glutamine-rich region, normally typical for SGT family members. The gene is expressed constitutively during the life cycle and is essential for survival and/or growth of the parasites. LdSGT forms large, stable complexes that also include another putative co-chaperone, HSC70 interacting protein (HIP). The gene product forms cytoplasmic clusters, matching the subcellular distribution of HIP and partly that of the major cytoplasmic chaperones, HSP70 and HSP90, reflecting a direct molecular interaction with both chaperones.
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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.