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Heat shock protein 90 (Hsp90) is a ubiquitous molecular chaperone that is responsible for the stabilization and maturation of many oncogenic proteins.
Heat shock protein 90 (Hsp90) represents an attractive cancer therapeutic target due to its role in the stabilization and maturation of many oncogenic proteins.
PCs are required for activation and maturation of many secreted proteins.
HSP90 chaperone protein stabilizes and enhances conformational maturation of many proteins [ 65] including KIT and PDGFRA.
ABA is involved in the maturation of many climacteric and non-climacteric fruit.
Cytokines help regulate virtually all immune processes, affect the balance between humoral and cellular immunity, and help control the growth and maturation of many immune cells.
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A recent report implicates p53 in the enhancement of miRNA maturation for many miRNAs following DNA damage [ 41], attesting to global miRNA upregulation as a possible anti-cancer mechanism.
Heat shock protein 90 (Hsp90) is a molecular chaperone that plays an important role in regulating the maturation and stabilization of many oncogenic proteins.
The 90 kDa heat shock proteins (Hsp90) represent a class of molecular chaperones responsible for the maturation and stabilization of many oncogenic proteins.
The enzymatic cleavage of double-stranded(ds) RNA structures is an essential step in the maturation and decay of many eukaryotic and prokaryotic RNAs.
This family plays essential roles in the folding, maturation and activity of many proteins that are involved in signal transduction and transcriptional regulation.
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