In vivo aspects of protein folding and quality control, Science, vol.353, p.4354, 2016. ,
Experimental milestones in the discovery of molecular chaperones as polypeptide unfolding enzymes, Annu Rev Biochem, vol.85, pp.715-742, 2016. ,
The HSP90 chaperone machinery, Nat Rev Mol Cell Biol, vol.18, pp.345-360, 2017. ,
Dancing with the diva: Hsp90-client interactions, J Mol Biol, vol.430, pp.3029-3040, 2018. ,
Hsp90: breaking the symmetry, Mol Cell, vol.58, pp.8-20, 2015. ,
HSP90 at the hub of protein homeostasis: emerging mechanistic insights, Nat Rev Mol Cell Biol, vol.11, pp.515-528, 2010. ,
Evolution and function of diverse Hsp90 homologs and cochaperone proteins, Biochim Biophys Acta, vol.1823, pp.607-613, 2012. ,
Hsp90 and Hsp70 chaperones: collaborators in protein remodeling, J Biol Chem, vol.294, pp.2109-2120, 2019. ,
Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling, Proc Natl Acad Sci U S A, vol.108, pp.8206-8211, 2011. ,
Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins, J Biol Chem, vol.289, pp.6110-6119, 2014. ,
Hsp90 breaks the deadlock of the Hsp70 chaperone system, Mol Cell, vol.70, pp.545-552, 2018. ,
Ancient heat shock gene is dispensable, J Bacteriol, vol.170, pp.2977-2983, 1988. ,
ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells, Mol Microbiol, vol.36, pp.1360-1370, 2000. ,
Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity, Biochem Biophys Res Commun, vol.400, pp.241-245, 2010. ,
High-temperature protein G is essential for activity of the Escherichia coli clustered regularly interspaced short palindromic repeats (CRISPR)/Cas system, Proc Natl Acad Sci U S A, vol.108, pp.20136-20141, 2011. ,
,
, Genome-scale co-evolutionary inference identifies functions and clients of bacterial Hsp90, PLoS Genet, vol.9
Hsp90 is essential under heat stress in the bacterium Shewanella oneidensis, Cell Rep, vol.19, pp.680-687, 2017. ,
HtpG, the prokaryotic homologue of Hsp90, stabilizes a phycobilisome protein in the cyanobacterium Synechococcus elongatus PCC 7942, Mol Microbiol, vol.76, pp.576-589, 2010. ,
Interactions of Escherichia coli molecular chaperone HtpG with DnaA replication initiator DNA, Cell Stress Chaperones, vol.20, pp.951-957, 2015. ,
Discovery and characterization of tRNAIle lysidine synthetase (TilS), FEBS Lett, vol.584, pp.272-277, 2010. ,
Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase, Nature, vol.461, pp.1144-1148, 2009. ,
AAA? proteases: ATP-fueled machines of protein destruction, Annu Rev Biochem, vol.80, pp.587-612, 2011. ,
The bacterial stress-responsive Hsp90 chaperone (HtpG) is required for the production of the genotoxin colibactin and the siderophore yersiniabactin in Escherichia coli, J Infect Dis, vol.214, pp.916-924, 2016. ,
Quality control and fate determination of Hsp90 client proteins, Biochim Biophys Acta, vol.1823, pp.683-688, 2012. ,
CHIP: a co-chaperone for degradation by the proteasome, Subcell Biochem, vol.78, pp.219-242, 2015. ,