Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
HSP70 played an important role in the pathogenesis of cancer which stabilized the production of large amount of oncogenic proteins and finally supported growth and survival of tumor.
|
30245753 |
2018 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
This is the first description of an miRNA-mediated mechanism of HSP70 regulation in cancer, making miR-142-3p an attractive target for PDAC therapeutic intervention.
|
23635652 |
2013 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
HSP70, a major HSP protein (molecular weight, 70 KDa), regulates diverse cellular pathways including protein quality control, translation, immune response, and cancer survival.
|
29017815 |
2017 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
Our JG-98 series of Hsp70 inhibitors show anti-cancer activities affecting both cancer cells and tumor-associated macrophages.
|
29445088 |
2018 |
Malignant Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
These findings highlight a new and unconventional role for the chaperonin activity of Hsp70 in the localization of a key regulatory protein (tTG) at the leading edges of cancer cells and the important consequences that this holds for their ability to migrate.
|
21896482 |
2011 |
Malignant Neoplasms
|
0.100 |
GeneticVariation
|
group |
BEFREE |
Efforts have been taken to develop monoclonal antibodies (mAbs) and antibody fragments targeting extracellular Hsp90 and Hsp70, alone or conjugated with standard anticancer agents, to control several types of cancer, such as breast, colon, prostate or melanoma.
|
27881057 |
2017 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
Surface-exposed HSP70 and calreticulin are damage-associated molecular patterns (DAMPs) crucially involved in modulating the success of cancer therapy.
|
22193987 |
2012 |
Malignant Neoplasms
|
0.100 |
AlteredExpression
|
group |
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 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
The overexpression of heat shock protein 70 (HSP70), a major stress-inducible heat shock protein, has been identified to enhance the proliferation, survival, invasion and metastasis of diverse types of human cancer.
|
28928813 |
2017 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
Stability of the cancer target DDIAS is regulated by the CHIP/HSP70 pathway in lung cancer cells.
|
28079882 |
2017 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
Stress-induced phosphoprotein-1 (STIP1), an adaptor protein that coordinates the functions of HSP70 and HSP90 in protein folding, has been implicated in the development of human gynecologic malignancies.
|
29304094 |
2018 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
Cancer cells rely on the chaperone heat shock protein 70 (Hsp70) for survival and proliferation.
|
29953808 |
2018 |
Malignant Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
Our results demonstrate the critical role of the stress-activated Stub1-Hsp70 complex in promoting Treg cell inactivation, thus providing a potential therapeutic target for the intervention against autoimmune disease, infection, and cancer.
|
23973223 |
2013 |
Malignant Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
As a stress‑inducible heat shock protein, HSP70 is highly expressed in a variety of cancers and correlates with metastasis, chemotherapy resistance and tumor prognosis.
|
30066840 |
2018 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
In this review, the history, regulation, mechanism of action and role in cancer of the HSP70 family are reviewed.
|
23563090 |
2013 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
Importantly, the cancer drug target ribonucleotide reductase was shown to be a client of Hsp70 and Hsp90 in both yeast and breast cancer cells.
|
25452130 |
2015 |
Malignant Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
Heat-shock protein-70 (HSP70) is critical to the folding, stability, and activity of several client proteins including many responsible for cancer cell proliferation, apoptosis, drug toxicity, and metastasis.
|
30273495 |
2019 |
Malignant Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
The present study demonstrates the potential of hsp70 in protecting SW480 cells from curcumin-induced apoptosis and highlights that silencing the expression of hsp70 is an effective approach to augment curcumin-based therapy in cancers that are resistant due to hsp70 expression.
|
14604899 |
2004 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
Among the 65 cases, p53 and hsp70 immunoreaction in cancer cell nuclei was detected immunohistochemically in 16 (25%) and 23 (35%) cases, respectively.
|
7540234 |
1995 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
Thus, this work demonstrates the importance of the interaction between AIMP2-DX2 and HSP70 on tumor progression and its therapeutic potential against cancer.
|
31792442 |
2020 |
Malignant Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
Thus, increasing Hsp70 levels combined with inhibiting its ATPase function may serve to dramatically reduce Akt levels and facilitate cell death in certain types of cancer.
|
19889640 |
2010 |
Malignant Neoplasms
|
0.100 |
GeneticVariation
|
group |
BEFREE |
Although the tumorigenic potential and prognostic applications of Hsp70 have been widely investigated, it remains unclear whether genetic variations of the human isoforms HSPA1L, HSPA1A, and HSPA1B are associated with cancer risk and prognosis.
|
22037874 |
2011 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
We identified HDAC1 and HDAC7 as novel targets of miR-34a in breast cancer, and further uncovered that deacetylation of HSP70 K246 by HDAC1 and HDAC7 promotes cancer cell survival and therapy resistance by inhibiting autophagic cell death.
|
25173798 |
2014 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
The mechanism by which Hsp70 is translocated to plasma membrane of tumor cells and the recent discoveries of drugs targeting this Hsp70 in cancer therapy will be also highlighted.
|
31669516 |
2020 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
Our results demonstrate that HSP70 enriched EXO is an effective immunoadjuvant in cancer immunotherapy and causes tumor regression in animal model.
|
28843722 |
2017 |