Hsp90: From Cellular to Organismal Proteostasis
Cells, 2022 Assuring a healthy proteome is indispensable for survival and organismal health. Proteome disbalance and the loss of the proteostasis buffer are hallmarks of various diseases.
Milán Somogyvári +2 more
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Trematode infection buffers heat stress in blue mussels Mytilus edulis: The role of heat shock proteins. [PDF]
J Anim EcolThe study shows that parasite infection changes heat shock protein expression and can increase heat tolerance in blue mussels. By separating parasite and temperature effects, the results suggest that infection may improve survival during heat stress, highlighting important parasite–host interactions for climate change resilience. Abstract The influence
Greve A +3 more
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Cells, 2020 Tumor cells exhibit therapeutic stress resistance-associated secretory phenotype involving extracellular vesicles (EVs) such as oncosomes and heat shock proteins (HSPs). Such a secretory phenotype occurs in response to cell stress and cancer therapeutics.
Takanori Eguchi +8 more
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Targeting GRP75 improves HSP90 inhibitor efficacy by enhancing p53-mediated apoptosis in hepatocellular carcinoma. [PDF]
PLoS ONE, 2014 Heat shock protein 90 (HSP90) inhibitors are potential drugs for cancer therapy. The inhibition of HSP90 on cancer cell growth largely through degrading client proteins, like Akt and p53, therefore, triggering cancer cell apoptosis.
Weiwei Guo +8 more
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Membrane fluidity and temperature sensing are coupled via circuitry comprised of Ole1, Rsp5, and Hsf1 in Candida albicans [PDF]
, 2014 Peer reviewedPublisher ...
Cowen, Leah E., Leach, Michelle D.
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Ydj1 governs fungal morphogenesis and stress response, and facilitates mitochondrial protein import via Mas1 and Mas2 [PDF]
, 2017 We thank Zhen-Yuan Lin for help in the preparation of the AP-MS samples, and Cathy Collins for technical assistance. MDL is supported by a Sir Henry Wellcome Postdoctoral Fellowship (Wellcome Trust 096072), LEC is supported by a Canada Research Chair in ...
Bohovych, Iryna +7 more
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Cell Reports, 2019 Summary: Molecular chaperones such as heat-shock proteins (HSPs) help in protein folding. Their function in the cytosol has been well studied. Notably, chaperones are also present in the nucleus, a compartment where proteins enter after completing de ...
Aneliya Antonova +12 more
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Regulation of CLC-1 chloride channel biosynthesis by FKBP8 and Hsp90β. [PDF]
, 2016 Mutations in human CLC-1 chloride channel are associated with the skeletal muscle disorder myotonia congenita. The disease-causing mutant A531V manifests enhanced proteasomal degradation of CLC-1.
Chen, Shu-Ching +7 more
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Discovery and development of natural heat shock protein 90 inhibitors in cancer treatment
Acta Pharmaceutica Sinica B, 2012 Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that plays a vital role in the signal transduction of cancers. Hsp90 inhibitors are able to inhibit Hsp90 or the complex of Hsp90 and co-chaperones resulting in the degradation of ...
Yong Li +6 more
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In silico analysis of the HSP90 chaperone system from the African trypanosome, Trypanosoma brucei
Frontiers in Molecular Biosciences, 2022 African trypanosomiasis is a neglected tropical disease caused by Trypanosoma brucei (T. brucei) and spread by the tsetse fly in sub-Saharan Africa. The trypanosome relies on heat shock proteins for survival in the insect vector and mammalian host.
Miebaka Jamabo +5 more
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