Lysine

Hsp90 family chaperone HSP82 ; Saccharomyces cerevisiae S288C







5 Article(s)
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Title
Pub. Year
#Total Relationships
1 32139682 A methylated lysine is a switch point for conformational communication in the chaperone Hsp90. 2020 Mar 5 1
2 27868254 Extensive functional redundancy in the regulation of Candida albicans drug resistance and morphogenesis by lysine deacetylases Hos2, Hda1, Rpd3 and Rpd31. 2017 Feb 2
3 23041319 Lysine deacetylases Hda1 and Rpd3 regulate Hsp90 function thereby governing fungal drug resistance. 2012 Oct 25 1
4 12145316 A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90. 2002 Oct 25 3
5 9990037 Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation. 1999 Feb 16 1