|
HSP90AA1
|
Malignant Neoplasms
|
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
|
Malignant Neoplasms
|
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
|
Malignant Neoplasms
|
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
|
Malignant Neoplasms
|
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
|
Malignant Neoplasms
|
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
|
Malignant Neoplasms
|
0.100 |
AlteredExpression |
BEFREE |
Based on our previous finding that a humanized monoclonal antibody against ROR1 increases the activity of Ibrutinib against CLL, which is currently undergoing evaluation in clinical trials for the treatment of B-cell lymphoid malignancies, we then provided evidence that treatment with HSP90i (17-DMAG) enhances anti-CLL activity of Ibrutinib in vitro and in vivo, by down-modulating ROR1. iTRAQ-based quantitative proteomic analysis of other HSP90 oncogenic clients in addition to ROR1, followed by GO/KEGG enrichment analysis, showed that Bruton's Tyrosine Kinase (BTK), B-lymphoid Tyrosine Kinase (BLK), Lymphocyte-specific Protein Tyrosine Kinase (LCK), or LCK/YES-Related Novel Protein Tyrosine Kinase (LYN), as HSP90 clients, were significantly involved in 11 biological processes and 6 signaling pathways.
|
31726100 |
2020 |
|
HSP90AA1
|
Malignant Neoplasms
|
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
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
Therefore, HSP90 inhibitors represent potential new therapeutic agents for cancer.
|
31650359 |
2020 |
|
HSP90AA1
|
Malignant Neoplasms
|
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
|
Malignant Neoplasms
|
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
|
Malignant Neoplasms
|
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
|
Malignant Neoplasms
|
0.100 |
GeneticVariation |
BEFREE |
In contrast to the notion that Hsp90 interacts with and protects mutant p53 in cancer, Hsp90β preferentially bound to wild-type p53 and modulated its degradation via a proteasome-dependent manner.
|
31313490 |
2019 |
|
HSP90AA1
|
Malignant Neoplasms
|
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
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
HSP90AA1 exhibited a highest degree (degree = 32) and was enriched in 'pathways in cancer' and 'signal transduction'.
|
30982140 |
2019 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
A Chemical Biology Approach to the Chaperome in Cancer-HSP90 and Beyond.
|
30936118 |
2019 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
Nonsteroidal Anti-inflammatory Drugs Sensitize CD44-Overexpressing Cancer Cells to Hsp90 Inhibitor Through Autophagy Activation.
|
30982499 |
2019 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
KCNQ1OT1 presented a positive correlation with HSP90AA1 which predicted the tumor progression in NSCLC from The Cancer Genome Atlas database.
|
30471108 |
2019 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
Heat shock protein 90 (Hsp90) is a validated molecular chaperone considered as the new key recipient for cancer intervention.
|
30485473 |
2019 |
|
HSP90AA1
|
Malignant Neoplasms
|
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
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
However, both intrinsic and acquired resistance to HSP90 inhibitors (HSP90i) limits their effectiveness in cancer patients.
|
30678647 |
2019 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
The development of C-terminal heat shock protein 90 kDa (Hsp90) inhibitors has emerged as a potential treatment for cancer.
|
31591016 |
2019 |
|
HSP90AA1
|
Malignant Neoplasms
|
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
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
In cutaneous melanoma, a cancer with one of the high levels of Hsp90 overexpression, such expression was correlated with a panel of protein kinases, thus offering an opportunity to identify Hsp90-based multi-kinase inhibitors for novel cancer therapies.
|
30957641 |
2019 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
AlteredExpression |
BEFREE |
Heat shock factor 1 followed a similar trend as HSP90AA1, with higher expression in cancer.
|
31567483 |
2019 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
Inhibition of heat shock protein 90 (Hsp90) is known to be a significantly effective strategy in cancer therapy.
|
31452440 |
2019 |