HSP90 Cancer Research Results

HSP90, HSP90: Click to Expand ⟱

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).

GC, Gastric Adenocarcinoma: Click to Expand ⟱

Stomach/Gastric Cancer

Scientific Papers found: Click to Expand⟱

2924-

LT,

Luteolin selectively kills STAT3 highly activated gastric cancer cells through enhancing the binding of STAT3 to SHP-1

in-vitro,

GC,

in-vivo,

NA,

p‑STAT3↓, STAT3↓, Mcl-1↓, survivin↓, Bcl-xL↓, HSP90↓,

Showing Research Papers: 1 to 1 of 1

* indicates research on normal cells as opposed to diseased cells
Total Research Paper Matches: 1

Pathway results for Effect on Cancer / Diseased Cells:

Cell Death ⓘ

Bcl-xL↓, 1, Mcl-1↓, 1, survivin↓, 1,

Protein Folding & ER Stress ⓘ

HSP90↓, 1,

Proliferation, Differentiation & Cell State ⓘ

STAT3↓, 1, p‑STAT3↓, 1,
Total Targets: 6

Pathway results for Effect on Normal Cells:

Total Targets: 0

Scientific Paper Hit Count for: HSP90, HSP90

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