{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,14]],"date-time":"2026-03-14T11:01:42Z","timestamp":1773486102037,"version":"3.50.1"},"reference-count":162,"publisher":"Oxford University Press (OUP)","issue":"7","license":[{"start":{"date-parts":[[2021,10,28]],"date-time":"2021-10-28T00:00:00Z","timestamp":1635379200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000268","name":"BBSRC","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,11,16]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n               <jats:p>Heat-shock protein 90 (Hsp90) is a central regulator of cellular proteostasis. It stabilizes numerous proteins that are involved in fundamental processes of life, including cell growth, cell-cycle progression and the environmental response. In addition to stabilizing proteins, Hsp90 governs gene expression and controls the release of cryptic genetic variation. Given its central role in evolution and development, it is important to identify proteins and genes that interact with Hsp90. This requires sophisticated genetic and biochemical tools, including extensive mutant collections, suitable epitope tags, proteomics approaches and Hsp90-specific pharmacological inhibitors for chemogenomic screens. These usually only exist in model organisms, such as the yeast Saccharomyces cerevisiae. Yet, the importance of other fungal species, such as Candida albicans and Cryptococcus neoformans, as serious human pathogens accelerated the development of genetic tools to study their virulence and stress response pathways. These tools can also be exploited to map Hsp90 interaction networks. Here, we review tools and techniques for Hsp90 network mapping available in different fungi and provide a summary of existing mapping efforts. Mapping Hsp90 networks in fungal species spanning &amp;gt;500\u00a0million years of evolution provides a unique vantage point, allowing tracking of the evolutionary history of eukaryotic Hsp90 networks.<\/jats:p>","DOI":"10.1093\/femsyr\/foab054","type":"journal-article","created":{"date-parts":[[2021,10,26]],"date-time":"2021-10-26T11:09:09Z","timestamp":1635246549000},"source":"Crossref","is-referenced-by-count":18,"title":["Hsp90 interaction networks in fungi\u2014tools and techniques"],"prefix":"10.1093","volume":"21","author":[{"given":"Julia L","family":"Crunden","sequence":"first","affiliation":[{"name":"School of Cellular and Molecular Medicine, University of Bristol , University Walk, Bristol BS8 1TD, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9528-1495","authenticated-orcid":false,"given":"Stephanie","family":"Diezmann","sequence":"additional","affiliation":[{"name":"School of Cellular and Molecular Medicine, University of Bristol , University Walk, Bristol BS8 1TD, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2021,10,28]]},"reference":[{"key":"2022072910385423200_bib1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fcimb.2021.637836","article-title":"Identification and phenotypic characterization of Hsp90 phosphorylation sites that modulate virulence traits in the major human fungal pathogen Candida albicans","volume":"11","author":"Alaalm","year":"2021","journal-title":"Front Cell Infect Microbiol"},{"key":"2022072910385423200_bib2","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1038\/nature04716","article-title":"Crystal structure of an Hsp90-nucleotide-p23\/Sba1 closed chaperone complex","volume":"440","author":"Ali","year":"2006","journal-title":"Nature"},{"key":"2022072910385423200_bib3","doi-asserted-by":"crossref","first-page":"2360","DOI":"10.1093\/gbe\/evz147","article-title":"Molecular chaperones 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