![]() Deciphering the Hsp90 chaperone network holds great promise for the development of suitable measures to combat fungal drug resistance and counter the ever-increasing number of Candida infections.Molecular chaperones often work collaboratively with the ubiquitylation-proteasome system (UPS) to facilitate the degradation of misfolded proteins, which typically safeguards cellular differentiation and protects cells from stress. ![]() albicans, discuss its divergence from that of its relative Saccharomyces cerevisiae and illustrate how the network informs our understanding of fungal biology, stress responses and virulence. We describe the first Hsp90 genetic interaction network in C. While specific Hsp90 clients have been identified and described, a global overview of Hsp90 interactions in this pathogen remained elusive until recently.Here we discuss recent advancements in mapping the C. In the leading fungal pathogen of humans, Candida albicans, Hsp90 governs virulence, morphogenesis and drug resistance. In doing so, Hsp90 interacts with up to 10% of the eukaryotic cell’s proteome. Deciphering the Hsp90 chaperone network holds great promise for the development of suitable measures to combat fungal drug resistance and counter the ever-increasing number of Candida infections.ĪB - The essential molecular chaperone heat shock protein 90 (Hsp90) is a highly conserved protein hub, which modulates the genotype to phenotype translation in animals, plants and fungi. N2 - The essential molecular chaperone heat shock protein 90 (Hsp90) is a highly conserved protein hub, which modulates the genotype to phenotype translation in animals, plants and fungi. T1 - The Candida albicans Hsp90 Chaperone Network is Environmentally Flexible and Evolutionarily Divergent Deciphering the Hsp90 chaperone network holds great promise for the development of suitable measures to combat fungal drug resistance and counter the ever-increasing number of Candida infections.", In doing so, Hsp90 interacts with up to 10% of the eukaryotic cells proteome. Deciphering the Hsp90 chaperone network holds great promise for the development of suitable measures to combat fungal drug resistance and counter the ever-increasing number of Candida infections.Ībstract = "The essential molecular chaperone heat shock protein 90 (Hsp90) is a highly conserved protein hub, which modulates the genotype to phenotype translation in animals, plants and fungi. ![]() The essential molecular chaperone heat shock protein 90 (Hsp90) is a highly conserved protein hub, which modulates the genotype to phenotype translation in animals, plants and fungi.
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