Table:
The potential approaches to disrupt the Hsp90-Cdc37-client protein interaction	Related mechanisms	References
Targeting Cdc37
siRNAs or shRNA	Silencing Cdc37	[56, 57]
Targeting Cdc37-client interaction
4,5,6,7-Tetrabromobenzotriazole	CK2 inhibitors, suppressing Cdc37 phosphorylation at Ser13 site	[59]
PP5 mutation	Suppressing Cdc37 dephosphorylation	[48]
Vemurafenib	B-raf inhibitor. Antagonize Cdc37 interaction with kinases	[67]
Lapatinib	EGFR/HER2 inhibitor. Antagonize Cdc37 interaction with kinases	[67]
Targeting Hsp90-Cdc37 interaction
Celastrol	Blocking the critical interaction of Hsp90 at Glu33 and Cdc37 at Arg167	[68, 69]
Sulforaphane	Disrupting the formation of Hsp90-Cdc37 complex by direct modification of specific amino acids residues of Hsp90	[70]
FW-04-804	Binding sites at Gln133 and Glu47/Arg46 of Hsp90	[71, 72]
Withaferin A	Blocking several H-bond between Hsp90-Cdc37 interaction, like Ser113 (Hsp90)-Gln208 (Cdc37) bond and Gln133 (Hsp90)-Arg166 (Cdc37) bond	[73–75]
Kongensin A	Covalently binds to a cysteine 420 in the middle domain of Hsp90 and dissociates Hsp90 from Cdc37	[76, 77]
Platycodin D	H-bond connection with Hsp90 at Arg32 and Phe200 and Cdc37 at Asp169 and Asp170	[78, 79]
Pep-1	Cdc37-derived peptides, bound to Hsp90 N-terminal domain and inhibited Hsp90 ATPase activity	[80]

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| The potential approaches to disrupt the Hsp90-Cdc37-client protein interaction | Related mechanisms | References | 
 | --- | --- | --- | 
 | <COLSPAN=3> Targeting Cdc37 | 
 | siRNAs or shRNA | Silencing Cdc37 | [56, 57] | 
 | <COLSPAN=3> Targeting Cdc37-client interaction | 
 | 4,5,6,7-Tetrabromobenzotriazole | CK2 inhibitors, suppressing Cdc37 phosphorylation at Ser13 site | [59] | 
 | PP5 mutation | Suppressing Cdc37 dephosphorylation | [48] | 
 | Vemurafenib | B-raf inhibitor. Antagonize Cdc37 interaction with kinases | [67] | 
 | Lapatinib | EGFR/HER2 inhibitor. Antagonize Cdc37 interaction with kinases | [67] | 
 | <COLSPAN=3> Targeting Hsp90-Cdc37 interaction | 
 | Celastrol | Blocking the critical interaction of Hsp90 at Glu33 and Cdc37 at Arg167 | [68, 69] | 
 | Sulforaphane | Disrupting the formation of Hsp90-Cdc37 complex by direct modification of specific amino acids residues of Hsp90 | [70] | 
 | FW-04-804 | Binding sites at Gln133 and Glu47/Arg46 of Hsp90 | [71, 72] | 
 | Withaferin A | Blocking several H-bond between Hsp90-Cdc37 interaction, like Ser113 (Hsp90)-Gln208 (Cdc37) bond and Gln133 (Hsp90)-Arg166 (Cdc37) bond | [73–75] | 
 | Kongensin A | Covalently binds to a cysteine 420 in the middle domain of Hsp90 and dissociates Hsp90 from Cdc37 | [76, 77] | 
 | Platycodin D | H-bond connection with Hsp90 at Arg32 and Phe200 and Cdc37 at Asp169 and Asp170 | [78, 79] | 
 | Pep-1 | Cdc37-derived peptides, bound to Hsp90 N-terminal domain and inhibited Hsp90 ATPase activity | [80] |