|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
New research now shows that Hsp90 exists in cancer cells in a heightened, activated state that is highly susceptible to inhibition by 17AAG.
|
15106614 |
2004 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
Hsp90 and environmental impacts on epigenetic states: a model for the trans-generational effects of diethylstibesterol on uterine development and cancer.
|
15809267 |
2005 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
Hsp90 and Cdc37 -- a chaperone cancer conspiracy.
|
15661534 |
2005 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
AlteredExpression |
BEFREE |
Hsp90 is essential for restoring cellular functions of temperature-sensitive p53 mutant protein but not for stabilization and activation of wild-type p53: implications for cancer therapy.
|
15613472 |
2005 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
Because numerous oncoproteins belonging to the Hsp90 client protein family are selectively degraded by Hsp90 inhibitors, 17-allylamino-17-demethoxygeldanamycin (17-AAG), a first-in-class Hsp90 inhibitor, is now under clinical trials as a novel molecular-targeted agent for a wide range of malignancies.
|
17185503 |
2006 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
The molecular chaperone hsp90 has emerged as an important therapeutic target in cancer and neurodegenerative diseases, including the polyglutamine expansion disorders, because of its ability to regulate the activity, turnover and trafficking of many proteins.
|
16644868 |
2006 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
We review the potential advantages of HSP90 inhibitors, particularly the simultaneous combinatorial depletion of multiple oncogenic "client" proteins, leading to blockade of many cancer-causing pathways and the antagonism of all of the hallmark pathological traits of malignancy.
|
17513464 |
2007 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
The results identify important roles played by Hsp90 in maintaining and facilitating the degenerative phenotype in these diseases and provide a common principle governing cancer and neurodegenerative diseases.
|
17517623 |
2007 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
The results suggest that targeting both the Hsp70 family, as well as the Hsp90 protein will have an additive negative effect on cancer cell survival, even though their pathways of action are separate.
|
17487411 |
2007 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
Three emerging concepts that are addressing these therapeutic needs and that are key to blocking steps in tumourigenesis will be highlighted in this review: (a) attacking cancer cell immortality by targeting the telomere/telomerase complex; (b) targeting oncogene activation by inhibiting the molecular chaperone Hsp90; and (c) stabilizing tumour suppressor proteins by modulating the ubiquitin-proteasome system.
|
16647200 |
2007 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
We also discuss the possible functions of Hsp90 in FA pathophysiology and stem cell/cancer biology.
|
17881891 |
2007 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
AlteredExpression |
BEFREE |
In contrast to HSP90-directed agents, Cdc37 targeting seems to affect cancer cells through a distinct mechanism and does not significantly deplete the intracellular levels of most known HSP90 client proteins.
|
18089825 |
2007 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
Inhibitors of HSP90 may have a role in chemoprevention in addition to cancer therapy.
|
19138996 |
2008 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
GeneticVariation |
BEFREE |
In addition to identifying new prolactin-regulated genes in breast cancer cells, we found that prolactin-JAK2-STAT5 induces expression of the HSP90A gene, which encodes the master chaperone of cancer.
|
19014541 |
2008 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
AlteredExpression |
BEFREE |
Here we show that silencing either heat-shock cognate 70 (HSC70) or HSP72 expression in human cancer cell lines has no effect on HSP90 activity or cell proliferation.
|
18772114 |
2008 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
Other malignancies that rely on intact and efficient UPR to survive could be considered as new indications for Hsp90 inhibitors.
|
17624530 |
2008 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
The current study discovers a therapeutically important, unique property of cancer cell associated-GR that may be linked to a compromised role of Hsp90.Molecular Therapy (2009) 17 4, 623-631 doi:10.1038/mt.2009.4.
|
19223869 |
2009 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
Targeting HSP90 for cancer therapy.
|
19401686 |
2009 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
These results support an essential role for CDC37 in concert with HSP90 in maintaining oncogenic protein kinase clients and endorse the therapeutic potential of targeting CDC37 in cancer.
|
18931700 |
2009 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
AlteredExpression |
BEFREE |
These results suggest that DYX1C1 is a novel Hsp70 and Hsp90-interacting co-chaperone protein and its expression is associated with malignancy.
|
19277710 |
2009 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
Overall, these findings demonstrate that HSP70 and HSP90 are potent molecular targets of EGCG and suggest EGCG as a drug candidate for the treatment of human cancer.
|
20537126 |
2010 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
We will review the clinical data on Hsp90 inhibitors in different malignancies.
|
20231121 |
2010 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
Molecular chaperone heat shock protein 90 (Hsp90) inhibitors are promising targeted cancer therapeutic drugs, with the advantage that they deplete multiple oncogenic client proteins and modulate all the classical hallmarks of cancer.
|
21037799 |
2010 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
AlteredExpression |
BEFREE |
Akt kinase and HSP90 are therefore highly over-expressed in a large panel of cancer cell lines and are present in multi-chaperoning complexes.
|
20585984 |
2011 |
|
HSP90AA1
|
Malignant Neoplasms
|
0.100 |
Biomarker |
BEFREE |
In this review, the Hsp90 inhibitors that show promise for cancer therapy are summarized.
|
21811259 |
2011 |