HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Further development of such tool compounds may lead to new classes of Hsp90 inhibitors with applications in cancer and other diseases.
|
31662027 |
2020 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Cells also displayed impedance to the pharmacological inhibition of cancer chaperone Hsp90 inhibition with respect to induced cytotoxicity.
|
31692039 |
2020 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Hsp90 is one of the most important chaperones involved in regulating the maturation of more than 300 client proteins, many of which are closely associated with refractory diseases, including cancer, neurodegenerative diseases, and viral infections.
|
31663736 |
2020 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Because of its critical roles in regulating cellular signal transduction, the molecular chaperone heat-shock protein 90 (Hsp90) has become a novel therapeutic target for various diseases, including cancer, inflammation, and neurological diseases.
|
31592648 |
2020 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Since it is involved in all hallmarks of cancer, HSP90 has been considered as a promising drug target for cancer therapy.
|
31465284 |
2020 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
The emerging information now suggests that Hsp90 family of chaperones display additional cellular roles contributing to diseases like cancer.
|
31669620 |
2020 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Heat shock protein 90 (HSP90) is a promising target for treatment of cancer, and inhibitor bindings can generate efficient suppression on tumor in multiple ways.
|
31560152 |
2020 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
This review summarizes current knowledge on the role of HSP90 protein in cancer with focus on melanoma, and provides an overview of structurally different HSP90 inhibitors that are considered as potential therapeutics for melanoma treatment.
|
31659567 |
2020 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Therefore, HSP90 inhibitors represent potential new therapeutic agents for cancer.
|
31650359 |
2020 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Oral targeted delivery by nanoparticles enhances efficacy of an Hsp90 inhibitor by reducing systemic exposure in murine models of colitis and colitis-associated cancer.
|
31168612 |
2020 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Nonsteroidal Anti-inflammatory Drugs Sensitize CD44-Overexpressing Cancer Cells to Hsp90 Inhibitor Through Autophagy Activation.
|
30982499 |
2019 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
AlteredExpression |
BEFREE |
Heat shock factor 1 followed a similar trend as HSP90AA1, with higher expression in cancer.
|
31567483 |
2019 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Extracellular heat shock protein 90 alpha (eHsp90α, also known as HSP90AA1) has been widely reported to promote tumor cell motility and tumor metastasis in various types of cancer.
|
31273033 |
2019 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Inhibiting protein-protein interactions of Hsp90 as a novel approach for targeting cancer.
|
31176095 |
2019 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
HSP90 inhibitors have the potential to treat many types of cancer due to the dependence of tumor cells on HSP90 for cell growth and proliferation.
|
30999048 |
2019 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Inhibition of heat shock protein 90 (Hsp90) is known to be a significantly effective strategy in cancer therapy.
|
31452440 |
2019 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
These HSP90 inhibitors have undergone or are undergoing clinical trials for the treatment of cancer.
|
31113013 |
2019 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
The hsp90 chaperones govern the function of essential client proteins critical for normal cell function as well as cancer initiation and progression.
|
31501246 |
2019 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
AlteredExpression |
BEFREE |
Pearson's correlation coefficients between HSP90 expression values and other mRNA expression values were calculated based on The Cancer Genome Atlas dataset and bioinformatic analysis was done about these screened genes.
|
31687275 |
2019 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
In tumor-bearing nude mice, dorsomorphin enhanced HSP90 inhibitor-induced cancer cell apoptosis, tumor growth inhibition, and HSP70 expression.
|
31516744 |
2019 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Curcumin has been shown to regulate different members of HSPs including HSP27, HSP40, HSP60, HSP70, and HSP90 in cancer.
|
31136038 |
2019 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Despite this, preclinical and clinical research continues to show that Hsp90 inhibitors effectively target cancer cell death and decrease tumor progression supporting the rationale for development of novel Hsp90 inhibitors.
|
31793427 |
2019 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
HSP90AA1 exhibited a highest degree (degree = 32) and was enriched in 'pathways in cancer' and 'signal transduction'.
|
30982140 |
2019 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
The goal of this study is to explore the mechanism of a heat shock protein 90 (Hsp90) C-terminal inhibitor, Penicisulfuranol A (PEN-A), for cancer therapy.
|
30857829 |
2019 |
HSP90AA1
|
Primary malignant neoplasm
|
0.100 |
Biomarker |
BEFREE |
Recent years have seen heat shock protein 90 kDa (Hsp90) attract significant interest as a viable drug target, particularly for cancer.
|
30733455 |
2019 |