Pan‐HSP90 ligand binding reveals isoform‐specific differences in plasticity and water networks

Isoforms of heat shock protein 90 (HSP90) fold oncoproteins that facilitate all 10 hallmarks of cancer. However, its promise as a therapeutic target remains unfulfilled as there is still no FDA‐approved drug targeting HSP90 in disease. Among the reasons hindering progress are side effects caused by...

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Veröffentlicht in:	Protein science Jg. 32; H. 5; S. e4629 - n/a
Hauptverfasser:	Stachowski, Timothy R., Nithianantham, Stanley, Vanarotti, Murugendra, Lopez, Karlo, Fischer, Marcus
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Hoboken, USA John Wiley & Sons, Inc 01.05.2023 Wiley Subscription Services, Inc
Schlagworte:	Antineoplastic Agents - chemistry Binding conformational flexibility Heat shock proteins HSP90 Heat-Shock Proteins - chemistry Hsp90 isoforms Hsp90 protein Humans Isoforms ligand binding Ligands pan‐Hsp90 inhibitors Protein Binding Protein Conformation Protein folding Protein Isoforms - chemistry Proteins Side effects Therapeutic targets water networks Hsp90 isoforms conformational flexibility pan-Hsp90 inhibitors water networks ligand binding
ISSN:	0961-8368, 1469-896X, 1469-896X
Online-Zugang:	Volltext
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