N-terminal and C-terminal modulation of Hsp90 produce dissimilar phenotypes

N-terminal and C-terminal modulation of Hsp90 produce dissimilar phenotypes

Classic oncogenic heat shock protein 90 (Hsp90) inhibitors target the N-terminus of the protein, triggering a survival mechanism in cancer cells referred to as the heat shock response (HSR). Inhibiting Hsp90 by modulating the C-terminus does not trigger a HSR, making it a highly attractive chemother...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2015-01, Vol.51 (8), p.1410-1413
Hauptverfasser: Wang, Y, McAlpine, S R
Format: Artikel
Sprache:eng
Schlagworte:
Benzoquinones - pharmacology
HCT116 Cells
Heat-Shock Response - drug effects
HSP90 Heat-Shock Proteins - antagonists & inhibitors
HSP90 Heat-Shock Proteins - chemistry
HSP90 Heat-Shock Proteins - genetics
HSP90 Heat-Shock Proteins - metabolism
Humans
Lactams, Macrocyclic - pharmacology
Neoplasms - genetics
Neoplasms - metabolism
Peptides, Cyclic - pharmacology
Phenotype
Protein Conformation
Protein Folding
RNA, Messenger - metabolism
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Zusammenfassung:Classic oncogenic heat shock protein 90 (Hsp90) inhibitors target the N-terminus of the protein, triggering a survival mechanism in cancer cells referred to as the heat shock response (HSR). Inhibiting Hsp90 by modulating the C-terminus does not trigger a HSR, making it a highly attractive chemotherapeutic approach.
ISSN:1359-7345
1364-548X
DOI:10.1039/c4cc07284g