| Source: HalifaxProj(inhibit) |
| Type: |
| Heat shock protein 90 (Hsp90) is a molecular chaperone that plays a critical role in the proper folding, stabilization, and function of many proteins, including those involved in cell signaling, cell cycle regulation, and stress responses. -Hsp90 interacts with a variety of client proteins that are often mutated or overexpressed in cancer. These include oncogenes (like HER2, BRAF, and AKT) and tumor suppressor proteins (like p53). -Hsp90 is often overexpressed in cancer cells, which can help them survive under stressful conditions, such as those found in the tumor microenvironment. This overexpression is associated with poor prognosis in several types of cancer. -HSPs, particularly HSP90, are known to stabilize many proteins that drive cancer progression (oncoproteins). |
| Acute Myeloid Leukemia |
| 1352- | And, | Andrographolide downregulates the v-Src and Bcr-Abl oncoproteins and induces Hsp90 cleavage in the ROS-dependent suppression of cancer malignancy |
| - | in-vitro, | AML, | K562 |
| 5944- | Cela, | HSP90 inhibitor, celastrol, arrests human monocytic leukemia cell U937 at G0/G1 in thiol-containing agents reversible way |
| - | in-vitro, | AML, | U937 |
Query results interpretion may depend on "conditions" listed in the research papers. Such Conditions may include : -low or high Dose -format for product, such as nano of lipid formations -different cell line effects -synergies with other products -if effect was for normal or cancerous cells
Filter Conditions: Pro/AntiFlg:% IllCat:% CanType:2 Cells:% prod#:% Target#:149 State#:% Dir#:1
wNotes=0 sortOrder:rid,rpid