ArticleCell stress & chaperones2009
Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms.
Article in Cell stress & chaperones, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 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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Who cites it
57 citing papers in PubMed, 119 citations in OpenAlex.
- Genome-wide comparative analysis of the HSP90 gene family in four Ipomoea species and functional insights into the potentiality of IbHSP90-2 in low temperature tolerance.Frontiers in plant science · 2026Article
- Climate change-induced stress in the honey beeFrontiers in physiology · 2025Review
- Genome-Wide Identification and Expression Analysis of HSP70 Gene Family Under High-Temperature Stress in Lettuce (International journal of molecular sciences · 2024Article
- Hsp90 and Associated Co-Chaperones of the Malaria Parasite.Biomolecules · 2022Review
- Extracellular vesicles from Trichinella spiralis: Proteomic analysis and protective immunity.PLoS neglected tropical diseases · 2022Article
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- Heat Shock Proteins as the Druggable Targets in Leishmaniasis: Promises and Perils.Infection and immunity · 2021Review
- Human Hsp90 cochaperones: perspectives on tissue-specific expression and identification of cochaperones with similar in vivo functions.Cell stress & chaperones · 2021Review
- Heat Shock Proteins as Targets for Novel Antimalarial Drug Discovery.Advances in experimental medicine and biology · 2021Article
- Role of Heat Shock Proteins in Immune Modulation in Malaria.Advances in experimental medicine and biology · 2021Article
- The Role of Hsp70s in the Development and Pathogenicity of Plasmodium falciparum.Advances in experimental medicine and biology · 2021Article
- Role of Hsp90 in Plasmodium falciparum Malaria.Advances in experimental medicine and biology · 2021Article
- Genome-Wide Characterization of HSP90 Gene Family in Cucumber and Their Potential Roles in Response to Abiotic and Biotic Stresses.Frontiers in genetics · 2021Article
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- Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection after Brain Injury.Cells · 2020Review
- Effects of thermal stress on mortality and HSP90 expression levels in the noble scallops Chlamys nobilis with different total carotenoid content.Cell stress & chaperones · 2020Article
- Proteomic Analysis of Exosome-Like Vesicles Isolated From Saliva of the TickFrontiers in cellular and infection microbiology · 2020Article
- Plasmodium falciparum R2TP complex: driver of parasite Hsp90 function.Biophysical reviews · 2019Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Hsp90 is critical for the regulation and activation of numerous client proteins critical for diverse functions such as cell growth, differentiation, and reproduction. Cytosolic Hsp90 function is dependent on a battery of co-chaperone proteins that regulate the ATPase activity of Hsp90 function or direct Hsp90 to interact with specific client proteins. Little is known about how Hsp90 complexes vary between different organisms and how this affects the scope of clients that are activated by Hsp90. This study determined whether ten distinct Hsp90 co-chaperones were encoded by genes in 19 disparate eukaryotic organisms. Surprisingly, none of the co-chaperones were present in all organisms. The co-chaperone Hop/Sti1 was most widely dispersed (18 out of 19 species), while orthologs of Cdc37, which is critical for the stability and activation of diverse protein kinases in yeast and mammals, were identified in only nine out of 19 species examined. The organism with the smallest proteome, Encephalitozoon cuniculi, contained only three of these co-chaperones, suggesting a correlation between client diversity and the complexity of the Hsp90 co-chaperone machine. Our results suggest co-chaperones are critical for cytosolic Hsp90 function in vivo, but that the composition of Hsp90 complexes varies depending on the specialized protein folding requirements of divergent species.
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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.