Relevant bibliographies by topics / HSC70; Cancer

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'HSC70; Cancer'

Author: Grafiati
Published: 4 June 2021
Last updated: 3 February 2022

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Journal articles on the topic "HSC70; Cancer"

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Mahboubi, Hicham, and Ursula Stochaj. "Quantitative analysis of the interplay between hsc70 and its co-chaperone HspBP1." PeerJ 3 (December 21, 2015): e1530. http://dx.doi.org/10.7717/peerj.1530.

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Background.Chaperones and their co-factors are components of a cellular network; they collaborate to maintain proteostasis under normal and harmful conditions. In particular, hsp70 family members and their co-chaperones are essential to repair damaged proteins. Co-chaperones are present in different subcellular compartments, where they modulate chaperone activities.Methods and Results.Our studies assessed the relationship between hsc70 and its co-factor HspBP1 in human cancer cells. HspBP1 promotes nucleotide exchange on hsc70, but has also chaperone-independent functions. We characterized the interplay between hsc70 and HspBP1 by quantitative confocal microscopy combined with automated image analyses and statistical evaluation. Stress and the recovery from insult changed significantly the subcellular distribution of hsc70, but had little effect on HspBP1. Single-cell measurements and regression analysis revealed that the links between the chaperone and its co-factor relied on (i) the physiological state of the cell and (ii) the subcellular compartment. As such, we identified a linear relationship and strong correlation between hsc70 and HspBP1 distribution in control and heat-shocked cells; this correlation changed in a compartment-specific fashion during the recovery from stress. Furthermore, we uncovered significant stress-induced changes in the colocalization between hsc70 and HspBP1 in the nucleus and cytoplasm.Discussion.Our quantitative approach defined novel properties of the co-chaperone HspBP1 as they relate to its interplay with hsc70. We propose that changes in cell physiology promote chaperone redistribution and thereby stimulate chaperone-independent functions of HspBP1.
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Oda, Tsukasa, Hidenobu Miyaso, and Takayuki Yamashita. "Nuclear Localization of Fanconi Anemia Protein FANCA Is Regulated by Hsc70/Hsp90 Chaperone Machinery." Blood 104, no. 11 (November 16, 2004): 2835. http://dx.doi.org/10.1182/blood.v104.11.2835.2835.

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Abstract Fanconi anemia (FA) is a genetic disorder characterized by bone marrow failure, cancer susceptibility and cellular hypersensitivity to DNA crosslinkers such as mitomycin C (MMC). Current evidence indicates that formation of a nuclear multiprotein complex (core complex) including six FA proteins FANCA/C/E/F/G/L is essential for FANCL/PHF9 ubiquitin ligase-mediated activation of FANCD2 into a monoubiquinated form, which participates in BRCA1 and FANCD1/BRCA2-mediated DNA repair (the FA/BRCA pathway). Subcellular distribution of FANCA plays a crucial role in the regulation of the FA/BRCA pathway. However, the underlying molecular mechanisms are not fully understood. To address this issue, we tried to identify FANCA-associated proteins. To this end, Flag-FANCA ectopically expressed in HeLa cells was immunopurified from the cytoplasmic fraction, using anti-Flag antibody-conjugated sepharose beads. Analysis of the immune complex on SDS polyacrylamide gel electrophoresis revealed that several proteins of Mr. 60–70 kD specifically associated with Flag-FANCA. These proteins were identified as FANCG and Hsc (heat shock cognate protein) 70 by LC-MS/MS. Immunoblot analysis showed that FANCA associated with Hsp90 as well as Hsc70. Hsc70 is an ATP-dependent molecular chaperone highly homologous to Hsp70 and often cooperates with Hsp90 to form a chaperone machinery involved in the regulation of diverse protein functions. Patient-derived FANCA mutants failed to bind FANCC but associated with larger amounts of Hsc70 than wt-FANCA, indicating that the interaction between FANCA and Hsc70 is not mediated by FANCC, as suggested by previous observations of the interaction of FANCC with Hsp70. To study the role of Hsc70 and Hsp90 in the regulation of FANCA, we examined effects of a dominant-negative (dn) form of Hsc70 with inactivated ATPase activity, and a specific inhibitor of Hsp90, 17-AAG (a geldanamycin analog). Overexpression of dn-Hsc70 inhibited nuclear localization of FANCA and inhibited its core complex formation, whereas wt-Hsc70 did not. 17-AAG induced cytoplasmic distribution and proteosomal degradation of FANCA and suppressed FANCD2 mono-ubiquitination. Taken together, these results suggest that Hsc70/Hsp90 chaperone machinery interacts with FANCA and regulates its subcellular distribution and stability, thereby controlling activation of the FA/BRCA pathway.
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Luan, Haitao, Tameka A. Bailey, Robert J. Clubb, Bhopal C. Mohapatra, Aaqib M. Bhat, Sukanya Chakraborty, Namista Islam, et al. "CHIP/STUB1 Ubiquitin Ligase Functions as a Negative Regulator of ErbB2 by Promoting Its Early Post-Biosynthesis Degradation." Cancers 13, no. 16 (August 4, 2021): 3936. http://dx.doi.org/10.3390/cancers13163936.

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Overexpression of the epidermal growth factor receptor (EGFR) family member ErbB2 (HER2) drives oncogenesis in up to 25% of invasive breast cancers. ErbB2 expression at the cell surface is required for oncogenesis but mechanisms that ensure the optimal cell surface display of overexpressed ErbB2 following its biosynthesis in the endoplasmic reticulum are poorly understood. ErbB2 is dependent on continuous association with HSP90 molecular chaperone for its stability and function as an oncogenic driver. Here, we use knockdown and overexpression studies to show that the HSP90/HSC70-interacting negative co-chaperone CHIP (C-terminus of HSC70-Interacting protein)/STUB1 (STIP1-homologous U-Box containing protein 1) targets the newly synthesized, HSP90/HSC70-associated, ErbB2 for ubiquitin/proteasome-dependent degradation in the endoplasmic reticulum and Golgi, thus identifying a novel mechanism that negatively regulates cell surface ErbB2 levels in breast cancer cells, consistent with frequent loss of CHIP expression previously reported in ErbB2-overexpressing breast cancers. ErbB2-overexpressing breast cancer cells with low CHIP expression exhibited higher endoplasmic reticulum stress inducibility. Accordingly, the endoplasmic reticulum stress-inducing anticancer drug Bortezomib combined with ErbB2-targeted humanized antibody Trastuzumab showed synergistic inhibition of ErbB2-overexpressing breast cancer cell proliferation. Our findings reveal new insights into mechanisms that control the surface expression of overexpressed ErbB2 and suggest that reduced CHIP expression may specify ErbB2-overexpressing breast cancers suitable for combined treatment with Trastuzumab and ER stress inducing agents.
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DeGeer, Jonathan, Andrew Kaplan, Pierre Mattar, Morgane Morabito, Ursula Stochaj, Timothy E. Kennedy, Anne Debant, Michel Cayouette, Alyson E. Fournier, and Nathalie Lamarche-Vane. "Hsc70 chaperone activity underlies Trio GEF function in axon growth and guidance induced by netrin-1." Journal of Cell Biology 210, no. 5 (August 31, 2015): 817–32. http://dx.doi.org/10.1083/jcb.201505084.

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During development, netrin-1 is both an attractive and repulsive axon guidance cue and mediates its attractive function through the receptor Deleted in Colorectal Cancer (DCC). The activation of Rho guanosine triphosphatases within the extending growth cone facilitates the dynamic reorganization of the cytoskeleton required to drive axon extension. The Rac1 guanine nucleotide exchange factor (GEF) Trio is essential for netrin-1–induced axon outgrowth and guidance. Here, we identify the molecular chaperone heat shock cognate protein 70 (Hsc70) as a novel Trio regulator. Hsc70 dynamically associated with the N-terminal region and Rac1 GEF domain of Trio. Whereas Hsc70 expression supported Trio-dependent Rac1 activation, adenosine triphosphatase–deficient Hsc70 (D10N) abrogated Trio Rac1 GEF activity and netrin-1–induced Rac1 activation. Hsc70 was required for netrin-1–mediated axon growth and attraction in vitro, whereas Hsc70 activity supported callosal projections and radial neuronal migration in the embryonic neocortex. These findings demonstrate that Hsc70 chaperone activity is required for Rac1 activation by Trio and this function underlies netrin-1/DCC-dependent axon outgrowth and guidance.
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Chernikov, V. A., N. V. Gorokhovets, L. V. Savvateeva, and S. E. Severin. "Analysis of complex formation of human recombinant hsp70 with tumor-associated peptides." Biomeditsinskaya Khimiya 58, no. 6 (2012): 651–61. http://dx.doi.org/10.18097/pbmc20125806651.

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Molecular chaperones of HSP70 family assists presentation of exogenous antigenic peptides by antigen-presenting cells (APC). HSP70-peptide complexes are powerful immunotherapeutic agents, which enhance cross-presentation of captured antigen in dendritic cells and macrophages. Several clinical trials have shown that HSP-based cancer vaccines possess good efficacy and safety. However, sometime it is impossible to isolate sufficient amount of vaccine. These make us to pay attention for recombinant HSP70-based vaccines and to optimize in vitro complex formation mechanism. Here we have investigated two human recombinant proteins HSP70HYB and HSC70. Optimal values of ADP concentration, pH, temperature and peptides excess are determined in this work. We have also shown that proposed complex formation method enriches eluted from HSP70-complexes peptide repertoire compared to in vivo assembled ones.
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Tan, Aik-Aun, Wai-Mei Phang, Subash C. B. Gopinath, Onn H. Hashim, Lik Voon Kiew, and Yeng Chen. "Revealing Glycoproteins in the Secretome of MCF-7 Human Breast Cancer Cells." BioMed Research International 2015 (2015): 1–8. http://dx.doi.org/10.1155/2015/453289.

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Breast cancer is one of the major issues in the field of oncology, reported with a higher prevalence rate in women worldwide. In attempt to reveal the potential biomarkers for breast cancer, the findings of differentially glycosylated haptoglobin and osteonectin in previous study have drawn our attention towards glycoproteins of secretome from the MCF-7 cancer cell line. In the present study, further analyses were performed on the medium of MCF-7 cells by subjecting it to two-dimensional analyses followed by image analysis in contrast to the medium of human mammary epithelial cells (HMEpC) as a negative control. Carboxypeptidase A4 (CPA4), alpha-1-antitrypsin (AAT), haptoglobin (HP), and HSC70 were detected in the medium of MCF-7, while only CPA4 and osteonectin (ON) were detected in HMEpC medium. In addition, CPA4 was detected as upregulated in the MCF-7 medium. Further analysis by lectin showed that CPA4, AAT, HP, and HSC70 were secreted as N-glycan in the medium of MCF-7, with HP also showing differentially N-glycosylated isoforms. For the HMEpC, only CPA4 was detected as N-glycan. No O-glycan was detected in the medium of HMEpC but MCF-7 expressed O-glycosylated CPA4 and HSC70. All these revealed that glycoproteins could be used as glycan-based biomarkers for the prognosis of breast cancer.
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Dublang, Leire, Jarl Underhaug, Marte I. Flydal, Lorea Velasco-Carneros, Jean-Didier Maréchal, Fernando Moro, Maria Dolores Boyano, Aurora Martinez, and Arturo Muga. "Inhibition of the Human Hsc70 System by Small Ligands as a Potential Anticancer Approach." Cancers 13, no. 12 (June 11, 2021): 2936. http://dx.doi.org/10.3390/cancers13122936.

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Heat shock protein (Hsp) synthesis is upregulated in a wide range of cancers to provide the appropriate environment for tumor progression. The Hsp110 and Hsp70 families have been associated to cancer cell survival and resistance to chemotherapy. In this study, we explore the strategy of drug repurposing to find new Hsp70 and Hsp110 inhibitors that display toxicity against melanoma cancer cells. We found that the hits discovered using Apg2, a human representative of the Hsp110 family, as the initial target bind also to structural regions present in members of the Hsp70 family, and therefore inhibit the remodeling activity of the Hsp70 system. One of these compounds, the spasmolytic agent pinaverium bromide used for functional gastrointestinal disorders, inhibits the intracellular chaperone activity of the Hsp70 system and elicits its cytotoxic activity specifically in two melanoma cell lines by activating apoptosis. Docking and molecular dynamics simulations indicate that this compound interacts with regions located in the nucleotide-binding domain and the linker of the chaperones, modulating their ATPase activity. Thus, repurposing of pinaverium bromide for cancer treatment appears as a promising novel therapeutic approach.
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Kobayashi, Yukino, Ami Oguro, Yuta Hirata, and Susumu Imaoka. "The regulation of Hypoxia-Inducible Factor-1 (HIF-1alpha) expression by Protein Disulfide Isomerase (PDI)." PLOS ONE 16, no. 2 (February 4, 2021): e0246531. http://dx.doi.org/10.1371/journal.pone.0246531.

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Hypoxia-inducible factor-1alpha (HIF-1alpha), a transcription factor, plays a critical role in adaption to hypoxia, which is a major feature of diseases, including cancer. Protein disulfide isomerase (PDI) is up-regulated in numerous cancers and leads to cancer progression. PDI, a member of the TRX superfamily, regulates the transcriptional activities of several transcription factors. To investigate the mechanisms by which PDI affects the function of HIF-1alpha, the overexpression or knockdown of PDI was performed. The overexpression of PDI decreased HIF-1alpha expression in the human hepatocarcinoma cell line, Hep3B, whereas the knockdown of endogenous PDI increased its expression. NH4Cl inhibited the decrease in HIF-1alpha expression by PDI overexpression, suggesting that HIF-1alpha was degraded by the lysosomal pathway. HIF-1alpha is transferred to lysosomal membranes by heat shock cognate 70 kDa protein (HSC70). The knockdown of HSC70 abolished the decrease, and PDI facilitated the interaction between HIF-1alpha and HSC70. HIF-1alpha directly interacted with PDI. PDI exists not only in the endoplasmic reticulum (ER), but also in the cytosol. Hypoxia increased cytosolic PDI. We also investigated changes in the redox state of HIF-1alpha using PEG-maleimide, which binds to thiols synthesized from disulfide bonds by reduction. An up-shift in the HIF-1alpha band by the overexpression of PDI was detected, suggesting that PDI formed disulfide bond in HIF-1alpha. HIF-1alpha oxidized by PDI was not degraded in HSC70-knockdown cells, indicating that the formation of disulfide bond in HIF-1alpha was important for decreases in HIF-1alpha expression. To the best of our knowledge, this is the first study to show the regulation of the expression and redox state of HIF-1alpha by PDI. We also demonstrated that PDI formed disulfide bonds in HIF-1alpha 1–245 aa and decreased its expression. In conclusion, the present results showed that PDI is a novel factor regulating HIF-1alpha through lysosome-dependent degradation by changes in its redox state.
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Doong, Howard, John Price, Young Sook Kim, Christopher Gasbarre, Julie Probst, Lance A. Liotta, Jay Blanchette, Kathryn Rizzo, and Elise Kohn. "CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-γ and Hsp70/Hsc70." Oncogene 19, no. 38 (September 2000): 4385–95. http://dx.doi.org/10.1038/sj.onc.1203797.

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Tanaka, Masako, Saya Mun, Akihito Harada, Yasuyuki Ohkawa, Azusa Inagaki, Soichi Sano, Katsuyuki Takahashi, et al. "Hsc70 Contributes to Cancer Cell Survival by Preventing Rab1A Degradation under Stress Conditions." PLoS ONE 9, no. 5 (May 6, 2014): e96785. http://dx.doi.org/10.1371/journal.pone.0096785.

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Dissertations / Theses on the topic "HSC70; Cancer"

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Williams, Cory S. M. "The role of heat shock cognate 70 in human breast carcinoma." Thesis, University of Oxford, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365303.

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Koren, John. "The Role of Hsp70 in Cancer: A Study of the Hsp70 / Akt Relationship." Scholar Commons, 2012. http://scholarcommons.usf.edu/etd/4105.

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The Hsp70 family of molecular chaperones is essential for protein folding, re-folding misfolded client proteins, clearance of aberrant client proteins, and can also inhibit programmed cell death. There are two major cytosolic members of this family: the constitutive Hsc70, and the inducible Hsp72. Under stress conditions the Hsp70 family protects the cell from protein related damage by the induction of Hsp72. Hsc70 and Hsp72 are highly homologous with minor differences in substrate binding. In cancers, Hsp72 is commonly induced and this induction is thought to aid in cancer cell survival. In these studies we demonstrate the differential regulation of the prosurvival kinase Akt by Hsc70 and Hsp72. We demonstrate that of the two cytosolic forms, Hsp72 is the primary Akt regulator. Using a phenothiazine class inhibitor of Hsp70-family activity, methylene blue, we demonstrate dose dependent decreases in the levels of Akt; produced breast cancer specific cell death. This cell death could be rescued by the use of an Hsp70 family ATPase stimulating compound, SW02. We also demonstrate a similar phenotype with a rhodacyanine class Hsp70 family inhibitor, YM-1, also capable of reducing Akt and causing cancer specific cytotoxicity. The resulting Akt decreases were sufficient to block a tamoxifen-resistance pathway, allowing previously resistant cells to regain sensitivity to tamoxifen. These results demonstrate the capabilities of Hsp70 family inhibitors as potent compounds for the treatment of breast cancer.
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Gobbo, Jessica. "Inhibition de HSP70 : une nouvelle piste thérapeutique contre le cancer." Thesis, Dijon, 2013. http://www.theses.fr/2013DIJOS088/document.

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Les HSP ou protéines de stress ont été découvertes chez la drosophile par Ritossa en 1962. Hautement conservées entre les espèces, elles sont essentielles à l’homéostasie cellulaire et plus encore à la survie lors de stress d’origine diverse (chimique, physique, métabolique etc…). Actuellement, chez les mammifères, il existe cinq principales familles d'HSPs en fonction de leur poids moléculaires : HSP110, HSP90, HSP70 et HSP60 et les petites HSPs à laquelle appartient HSP27 (Kampinga et al., 2009). Parmi les HSPs, HSP70 est la plus fortement induite que ce soit par des agressions telles que le stress oxydatif, les agents anticancéreux ou les radiations ionisantes. HSP70 est, contrairement aux cellules « normales », fortement exprimée dans les cellules cancéreuses et confère à ces cellules une résistance aux drogues anticancéreuses (Goloudina, Demidov & Garrido, 2012) favorisant ainsi le développement tumoral. Les propriétés cyto-protectrices de HSP70 ont été jusqu’à présent attribuées par ces fonctions intracellulaires, principalement en inhibant le processus apoptotique à différentes étapes clés de la signalisation cellulaire (Ravagnan et al., 2001). Cependant une forme membranaire de HSP70 a été détectée à la surface des exosomes dérivant des cellules tumorales (Kuppner et al., 2001). HSP70 membranaire participerait au processus de tumorigenèse en inhibant l’activation des cellules myéloïdes suppressives (MDSCs) et en conséquence, la réponse immune anti-tumorale (Pfister et al., 2007; Schmitt, Gehrmann, Brunet, Multhoff, & Garrido, 2007). Par cette double facette, HSP70 représente donc une cible thérapeutique de choix pour la thérapie anticancéreuse. Compte tenu du rôle clé de HSP70, à la fois par ses fonctions intracellulaires et extracellulaires dans le développement tumoral, l’un des projets phare de notre groupe a été de développer des inhibiteurs spécifiques de HSP70, notamment des aptamères peptidiques et des peptides. Dans un premier travail, nous avons démontré in vitro que deux aptamères A8 et A17 (et son dérivé P17), interagissent avec HSP70 sur des domaines différents et sensibilisent les cellules cancéreuses à la mort induite par des agents chimiothérapeutiques. Des études in vivo réalisées chez la souris et le rat confirment ces résultats et mettent en évidence une réduction significative de la croissance tumorale par ces aptamères peptidiques. Dans un deuxième travail, nous avons généré un dérivé de l’aptamère A8, le peptide P8.1. Nous avons démontré que ce peptide est capable de neutraliser la forme membranaire de HSP70, présente à la surface des exosomes, bloquant ainsi l’activation des MDSCs et restaurant la réponse immunitaire anti-tumorale. A plus long terme, ce travail vise à mettre au point et à valider en clinique une thérapie anticancéreuse plus efficace, en associant aux traitements anticancéreux actuels, les inhibiteurs de HSP70
Heat shock proteins (HSPs) were first discovered in Drosophila by Ritossa in 1962. As stress proteins, HSPs are induced in response to a wide variety of physiological and environmental insults. HSPs have a cyto-protective function and act as molecular chaperones by assisting the folding of nascent or misfolded proteins and by preventing their aggregation. Mammalian HSPs have been classified into 5 families according to their molecular weight: HSP110, HSP90, HSP70, HSP60 and the family of small HSPs such as HSP27 (Kampinga et al., 2009). The most well-known inducible stress chaperone HSP70 is hardly detectable at basal level in normal “non-stressed” cells, but in cancer cells HSP70 is constitutively highly expressed. In that respect, this HSP play a key role in oncogenesis and in resistance to chemotherapeutic drugs (Goloudina et al., 2012).Until now, the cytoprotective properties of HSP70 were attributed to its intracellular functions mainly via its ability to block the apoptotic process at key points of the signal (Ravagnan et al., 2001). More recently, a membrane bound form of HSP70 was detected but also at the surface of exosomes derived from tumor cells but not non-cancerous cells (Kuppner et al., 2001). Moreover, growing evidence support the critical role of this membrane-bound HSP70 in the process of tumorigenesis (Pfister et al., 2007; Schmitt et al., 2007) via the activation of myeloid suppressor cells (MDSCs), which inhibit the anti-tumor immune response (Chalmin et al., 2010). Thereby, HSP70 by this dual action represents an attractive target for new anti-cancer therapy.In that aim, we developed specific inhibitors of HSP70, including peptide aptamers and peptides. In this work, we demonstrated that two aptamers A8, A17 (and the peptide P17), interact with different domains of HSP70 and, significantly sensitized cancer cells to apoptosis induced by chemotherapeutic drugs. Accordingly, in vivo studies in mice and rats showed a significant reduction of tumor growth by these inhibitors. Finally, we generate an A8 derived peptide called P8.1 that specifically neutralized the extracellular region of HSP70 at the surface of exosomes. Our results demonstrated that this peptide P8.1 inhibits MDSC activation and restored the antitumor immune response in vitro and in vivo, respectively.Overall, our work will help to develop and validate more effective cancer therapy based on the association of conventional chemotherapy with HSP70 inhibitors
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Faure, Olivier. "Hsp70 : un antigène du soi pour l'immunothérapie du cancer." Paris 5, 2003. http://www.theses.fr/2003PA05N106.

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La mise au point d'un vaccin anti-tumoral efficace requiert l'identification de nombreux antigènes associés aux tumeurs, dont l'expression est fréquente dans des tumeurs d'origines histologiques variées. La protéine de choc thermique Hsp70 inductible (ou Hsp72) est fréquemment sur-exprimée dans les tumeurs humaines malignes d'origines variées, telles que le carcinome du sein, du poumon, du colon, du col de l'utérus et les ostéosarcomes. Afin d' établir l'intérêt de Hsp70 comme antigène associé aux tumeurs, trois peptides de Hsp70 ont été sélectionnés pour leur haute affinité pour HLA-A*0201. Ces peptides induisent des lymphocytes T cytotoxiques anti-tumoraux "in vivo" dans des souris transgéniques pour HLA-A*0201 et "in vitro" à partir de PBMC des donneurs sains HLA-A0201+. Ces épitopes sont la cible d'une réponse immunitaire. .
The design of a broad application tumor vaccine requires the identification of tumor antigens expressed in a majority of tumors of various origins. The major stress-induccible heat shock protein Hsp70 (a. K. A Hsp72) is frequently overexpressed in human tumors of various histological origin, such as breast, lung, colorectal, cervical carcinoma and osteosarcoma. To assess the value of Hsp70 as a tumor associated antigen, three peptides from Hsp70 were selected for their high affinity for HLA-A*0201. These peptides were able to trigger anti-tumor cytotoxic T lymphocytes "in vivo" in HLA-A*0201-transgenic HHD mice and "in vitro" in HLA-A*0201+ healthy donors. These epitopes are tagets of an immune reponse in many HLA-A0201+ breast cancer patients. Hsp70 is thus a valuable tumor antigen for broad application tumor immunotherapy
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Chanteloup, Gaetan. "Intérêt de l'étude des HSP70-exosomes dans le diagnostic et le suivi du cancer." Thesis, Bourgogne Franche-Comté, 2020. http://www.theses.fr/2020UBFCI009.

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Le cancer est aujourd’hui une maladie qui fait malheureusement partie de notre quotidien, et bien qu’il soit de mieux en mieux traité, de plus en plus de gens en sont atteints. La recherche s’oriente sur deux pans : la thérapie et le diagnostic. Les nouvelles thérapies présentent des résultats spectaculaires jamais atteints à ce jour, mais l’amélioration du diagnostic peut aussi sauver des vies. Il est établi que plus un cancer est diagnostiqué tôt, plus le patient a de chances de guérir. Idem pour le suivi de la maladie. Dans ce contexte de précision et de précocité, la biopsie liquide émerge et possède un avenir très prometteur. Elle consiste en l’étude d’analytes présents dans les fluides corporels, particulièrement la circulation sanguine. On y retrouve principalement, mais pas exclusivement, l’ADN tumoral circulant, les cellules tumorales circulantes (CTCs) et les exosomes.Ce manuscrit a pour objectif de replacer mon travail de recherche, qui porte sur les exosomes, dans le contexte de la biopsie liquide, afin de laisser libre court aux comparaisons et à la compréhension de leur potentiel diagnostic. Les exosomes sont des nanovésicules libérées par les cellules dans le sang. Elles contiennent du matériel génétique, des lipides et des protéines. Une étape clé pour leur utilisation en tant que biomarqueur est de différencier les exosomes dérivés de tumeur de ceux dérivés d’autres cellules de l’organisme.La protéine de stress Heat shock protein-70 (HSP70) a été décrite comme étant surexprimée dans les cellules cancéreuses et associée à un mauvais pronostic. Nous avons précédemment démontré que seuls les exosomes dérivés de cellules cancéreuses portaient HSP70 à la membrane. Dans ce travail, nous avons ouvert une étude clinique pilote prospective incluant des patients atteints d’un cancer du sein et du poumon afin de déterminer s’il était possible de détecter et quantifier les HSP70-exosomes dans le sang de patients atteints de tumeurs solides malignes.Nous avons montré que le taux de HSP70 dans les exosomes, contrairement à la forme soluble, reflétait le contenu en HSP70 dans la biopsie tumorale. Le taux de HSP70-exosomes circulants est augmenté chez les patients atteints d’un cancer à un stade métastatique comparé aux non-métastatique et aux donneurs sains. Nous avons ensuite démontré que les niveaux de HSP70-exosomes étaient corrélés au statut de la maladie, et étaient potentiellement de meilleurs marqueurs que les CTCs. Enfin, nous avons indiqué que le taux de HSP70-exosomes étaient inversement corrélés à la réponse au traitement, et, par conséquent, que le suivi du taux de HSP70 dans les exosomes pourrait être utile dans la prédiction de la réponse au traitement
Actually, cancer is unfortunately part of our daily life. Although it is better treated, more and more people are affected. Cancer research is working on two side: therapy and diagnosis. The next-generation therapies show wonderful results that were never reached so far, but diagnosis improvement can also save lives. It is well established that the earlier the cancer is diagnosed, the better the survival rate. Idem for the follow-up of the disease. In this context of precision and earliness, liquid biopsy spark interest and seems to have a bright future. It consists in the investigation of liquid analytes, particularly within the bloodstream, such as circulating tumor DNA, circulating tumor cells (CTCs) and exosomes.This manuscript aims to put my research work on exosomes in the context of liquid biopsy, in order to let you compare with other analytes and understand their diagnosis potential. Exosomes are nanovesicles released by all cells that can be found in the blood. They carry genetic material, proteins end lipids. A key point for their use as potential biomarkers in cancer is to differentiate tumor-derived exosomes from other circulating nanovesicles.Heat shock protein-70 (HSP70) has been shown to be abundantly expressed by cancer cells and to be associated with bad prognosis. We previously showed that exosomes derived from cancer cells carried HSP70 in the membrane while those from non- cancerous cells did not. In this work, we opened a prospective clinical pilot study including breast and lung cancer patients to determine whether it was possible to detect and quantify HSP70 exosomes in the blood of patients with solid cancers.We found that circulating exosomal HSP70 levels, but not soluble HSP70, reflected HSP70 content within the tumour biopsies. Circulating HSP70 exosomes increased in metastatic patients compared to non-metastatic patients or healthy volunteers. Further, we demonstrated that HSP70-exosome levels correlated with the disease status and, when compared with circulating tumor cells, were more sensitive tumor dissemination predictors. Finally, our case studies indicated that HSP70-exosome levels inversely correlated with response to the therapy and that, therefore, monitoring changes in circulating exosomal HSP70 might be useful to predict tumor response and clinical outcome
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Schmitt, Élise. "Hsp70 : une cible dans la thérapie anti-cancéreuse." Dijon, 2006. http://www.theses.fr/2006DIJOMU13.

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HSP70 est une protéine de choc thermique surexprimée dans les cellules cancéreuses. Elle inhibe le processus apoptotique permettant la survie des cellules exposées à divers stress. Cette fonction protectrice d’HSP70 implique l’interaction et la neutralisation des protéines Apaf-1 et AIF. Nous avons montré qu’ADD70, un peptide contenant la séquence d’AIF nécessaire à son interaction avec HSP70, se lie et neutralise HSP70 dans le cytosol. Il sensibilise les cellules cancéreuses à la mort induite par une grande variété de stimuli apoptotique. In vivo, l’expression, de ce peptide par les cellules tumorales diminue leur tumorigénicité chez des animaux syngéniques immunocompétents sans affecter leur croissance chez des animaux immunodéficients. De plus, ADD70 sensibilise les cellules cancéreuses coliques de rat et les cellules de mélanome de souris au cisplatine, un agent anti-cancéreux. Ces données nous montrent l’intérêt de cibler l’interaction AIF/HSP70 dans la thérapie anti-cancéreuse
HSP70 is a heat shock protein overexpressed in several cancer cells. It prevents apoptosis, thereby increasing the survival of cells exposed to a wide range of lethal stimuli. These protective functions of HSP70 involve its interaction with and neutralization of Apaf-1, implicated in caspase activation, and AIF, involved in caspase-independent cell death. We have shown that a peptide containing the AIF sequence involved in its interaction with HSP70, binds to and neutralizes HSP70 in the cytosol, thereby sensitizing cancer cells to apoptosis induced by a variety of death stimuli. The expression of ADD70 in tumor cells decreases their tumorigenicity in syngeneic animals without affecting their growth in immunodeficient animals. In addition, ADD70 sensitizes rat colon cancer cells and mouse melanoma cells to the chemotherapeutic agent cisplatin. Altogether, these data indicate the potential interest of targeting the HSP70 interaction with AIF for cancer therapy
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Ciupitu, Anne-Marie T. "Hsp70 in immunotherapy : a potential vector in cancer and viral vaccines /." Stockholm, 2000. http://diss.kib.ki.se/2000/91-628-4093-2/.

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Willmer, Tarryn. "The role of Hsp90/Hsp70 organising protein (Hop) in the Proliferation, Survival and Migration of Breast Cancer Cells." Thesis, Rhodes University, 2012. http://hdl.handle.net/10962/d1015720.

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Hop (the Hsp90/Hsp70 organising protein) is a co-chaperone that acts as an adapter between the major molecular chaperones Hsp90 and Hsp70 during the cellular assembly of the Hsp90 complex. The Hsp90 complex regulates the stability and conformational maturation of a range of important cellular proteins, many of which are deregulated in cancer. In this study, we hypothesised that Hop knockdown inhibits proliferation and migration of cancer cells. We characterised the expression of Hop in cell models of different cancerous status, and provided evidence that Hop was upregulated in tumour cells compared to normal cell counterparts. Using an RNA interference approach, a 60-90% knockdown of Hop was achieved for up to 144 hours in the MDA-MB-231 and Hs578T breast cancer cell lines. Hop knockdown resulted in downregulation of the Hsp90 client proteins, Akt and Stat3, as well as a change in the expression of other Hsp90 co-chaperones, p23, Cdc37 and Aha1, while no change in the levels of Hsp90 or Hsp70 was observed. Silencing of Hop impaired cell proliferation in Hs578T cells but an increase in proliferation in MDA-MB-231, suggesting that the role of Hop in cancer cell proliferation was dependent on type of cancer cell. Hop knockdown in Hs578T and MDA-MB- 231 cells did not lead to any significant changes in the half maximal inhibitory concentrations (IC50) of selected small molecule inhibitors (paclitaxel, geldanamycin and novobiocin) in these cell lines after 72 hours. Hop knockdown cells were however, more sensitive than control cells to the Hsp90 inhibitors geldanamycin and novobiocin at earlier time points and in the presence of the drug transporter inhibitor, verapamil. Hop knockdown caused a decrease in cell migration as measured by the wound healing assay in both Hs578T and MDA-MB-231 cells. Hop was present in purified pseudopodia fractions of migrating cells, and immunofluorescence analysis showed that Hop colocalised with actin at the leading edges of pseudopodia, points of adhesion and at intercellular junctions of cells that have been stimulated to migrate with the chemokine stromal derived factor-1. Hop was able to bind to actin in vitro using actin cosedimentation assays, and silencing of Hop dramatically reduced the capacity of Hs578T cells to form pseudopodia. These results establish a correlation between Hop and actin dynamics, pseudopodia formation and migration in the context of Hop silencing, and collectively suggest that Hop plays a role in cancer cell migration. This study presents experimental evidence for a promising alternative to targeting Hsp90 and Hsp70 chaperones, a novel drug target in cancer therapy.
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Sampson, Iosifina. "The Role of Hsp70 and Nek6 in centrosome clustering in cancer cells." Thesis, University of Leicester, 2017. http://hdl.handle.net/2381/40662.

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Mitosis is an important process for the generation of two genetically identical daughter cells. Formation of a bipolar mitotic spindle requires the presence of two centrosomes as these are required to form each pole of the spindle. However, cancer cells, frequently possess extra centrosomes. Therefore, they have developed mechanisms to cluster them into two poles to enable mitotic pseudo-spindle formation and cell survival. Inhibiting centrosome clustering offers a unique and attractive therapeutic approach to selectively kill cells with amplified centrosomes by promoting formation of multipolar spindle poles and mitotic catastrophe. Centrosome clustering mechanisms include proteins with specific roles in microtubule dynamics, microtubule attachments to centrosomes, kinetochores and the cell cortex, as well as the spindle assembly checkpoint. Here, we identify a new pathway that contributes to centrosome clustering and involves the Nek6 kinase and Hsp72 chaperone. Nek6, as well as its upstream activators Plk1 and Aurora-A, targets Hsp72 to the poles of cells with amplified centrosomes. Blocking Hsp72 or Nek6 activity leads to formation of multipolar spindles with poles that always contain centrosomes, whereas other centrosome de-clustering agents trigger formation of acentrosomal poles. Indeed, inhibition of Hsp72 in ALL cells led to an increase of multipolar spindle frequency that correlated with centrosome amplification. Dynein/dynactin and phospho-Hsp72 colocalise to kinetochores and we suggest that they are required for proper attachment of microtubules to kinetochores to facilitate a stable bipolar mitotic spindle and potentially centrosome clustering. Additionally, loss of Hsp72 or Nek6 function did not disrupt either mitotic spindle formation or mitotic progression in non-cancer derived cells versus cancer cells. Hence, the Nek6-Hsp72 pathway, and its potential downstream target dynein, may act as a novel pathway of centrosome clustering that reveals a new opportunity for targeting centrosome clustering and mitotic progression in cancer cells.
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Weeks, Stacey. "Characterisation of the HSP70-HSP90 organising protein gene and its link to cancer." Thesis, Rhodes University, 2015. http://hdl.handle.net/10962/56006.

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HOP (Heat shock protein 70/ Heat shock protein 90 organising protein) is a co-chaperone essential for client protein transfer from HSP70 to HSP90 within the HSP90 chaperone machine and has been found to be up-regulated in various cancers. However, minimal in vitro information can be found on the regulation of HOP expression. The aim of this study was to analyse the HOP gene structure across known orthologues, identify and characterise the HOP promoter, and identify the regulatory mechanisms influencing the expression of HOP in cancer. We hypothesized that the expression of HOP in cancer cells is likely regulated by oncogenic signalling pathways linked to cis-elements within the HOP promoter. An initial study of the evolution of the HOP gene speciation was performed across identified orthologues using Mega5.2. The evolutionary pathway of the HOP gene was traced from the unicellular organisms to fish, to amphibian and then to land mammal. The synteny across the orthologues was identified and the co-expression profile of HOP analysed. We identified the putative promoter region for HOP in silico and in vitro. Luciferase reporter assays were utilized to demonstrate promoter activity of the upstream region in vitro. Bioinformatic analysis of the active promoter region identified a large CpG island and a range of putative cis-elements. Many of the cis-elements interact with transcription factors which are activated by oncogenic pathways. We therefore tested the regulation of HOP levels by rat sarcoma viral oncogene homologue (RAS). Cancer cell lines were transfected with mutated RAS to observe the effect of constitutively active RAS expression on the production of HOP using qRT-PCR and Western Blot analyses. Additionally, inhibitors of the RAS signalling pathway were utilised to confirm the regulatory effect of mutated RAS on HOP expression. In cancer cell lines containing mutated RAS (Hs578T), HOP was up-regulated via a mechanism involving the MAPK signalling pathway and the ETS-1 and C/EBPβ cis-elements within the HOP promoter. These findings suggest for the first time that Hop expression in cancer may be regulated by RAS activation of the HOP promoter. Additionally, this study allowed us to determine the murine system to be the most suited genetic model organism with which to study the function of human HOP.
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Book chapters on the topic "HSC70; Cancer"

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Workman, Paul. "Reflections and Outlook on Targeting HSP90, HSP70 and HSF1 in Cancer: A Personal Perspective." In Advances in Experimental Medicine and Biology, 163–79. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-40204-4_11.

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Abstract This personal perspective focuses on small-molecule inhibitors of proteostasis networks in cancer—specifically the discovery and development of chemical probes and drugs acting on the molecular chaperones HSP90 and HSP70, and on the HSF1 stress pathway. Emphasis is on progress made and lessons learned and a future outlook is provided. Highly potent, selective HSP90 inhibitors have proved invaluable in exploring the role of this molecular chaperone family in biology and disease pathology. Clinical activity was observed, especially in non small cell lung cancer and HER2 positive breast cancer. Optimal use of HSP90 inhibitors in oncology will likely require development of creative combination strategies. HSP70 family members have proved technically harder to drug. However, recent progress has been made towards useful chemical tool compounds and these may signpost future clinical drug candidates. The HSF1 stress pathway is strongly validated as a target for cancer therapy. HSF1 itself is a ligandless transcription factor that is extremely challenging to drug directly. HSF1 pathway inhibitors have been identified mostly by phenotypic screening, including a series of bisamides from which a clinical candidate has been identified for treatment of ovarian cancer, multiple myeloma and potentially other cancers.
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Ménoret, Antoine. "Immunological significance of hsp70 in tumor rejection." In Cancer Immunology, 157–69. Dordrecht: Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-017-0963-7_9.

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Liu, Tuoen, and Shousong Cao. "Heat Shock Protein 70 and Cancer." In HSP70 in Human Diseases and Disorders, 93–111. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-89551-2_5.

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Sharma, Prakash Chand, and Renu Verma. "Implication of HSP70 in the Pathogenesis of Gastric Cancer." In HSP70 in Human Diseases and Disorders, 113–30. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-89551-2_6.

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Önay Uçar, Evren, Aslıhan Şengelen, Elif Mertoğlu, Murat Pekmez, and Nazlı Arda. "Suppression of HSP70 Expression by Quercetin and Its Therapeutic Potential Against Cancer." In HSP70 in Human Diseases and Disorders, 361–79. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-89551-2_19.

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Datta, Dipamoy, Suparna Banerjee, Anupama Ghosh, Soumyajit Banerjee Mustafi, Prosenjit Sen, and Sanghamitra Raha. "Involvement of Heat Shock Protein 70 (Hsp70) in Gastrointestinal Cancers." In HSP70 in Human Diseases and Disorders, 71–91. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-89551-2_4.

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Saito, Youhei, and Yuji Nakayama. "Mammalian Heat Shock Protein Hsp105: The Hsp70 Inducer and a Potent Target for Cancer Therapy." In HSP70 in Human Diseases and Disorders, 347–59. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-89551-2_18.

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Rérole, Anne Laure, Anne Laure Joly, Dominique Thuringer, and Carmen Garrido. "Hsp70 and Hsp27: Emerging Targets in Cancer Therapy." In Apoptosome, 169–202. Dordrecht: Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3415-1_9.

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Boudesco, Christophe, Sebastien Cause, Gaëtan Jego, and Carmen Garrido. "Hsp70: A Cancer Target Inside and Outside the Cell." In Methods in Molecular Biology, 371–96. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7477-1_27.

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Brunet, M., C. Didelot, S. Subramaniam, A. L. Rérole, A. de Thonel, and C. Garrido. "Hsp70 and Hsp27 as pharmacological targets in apoptosis modulation for cancer therapy." In Heat Shock Proteins in Cancer, 209–30. Dordrecht: Springer Netherlands, 2007. http://dx.doi.org/10.1007/978-1-4020-6401-2_11.

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Conference papers on the topic "HSC70; Cancer"

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Massey, Andrew J., Jennifer Borgognoni, Helen Browne, Zoe Daniels, Pawel Dokurno, Martin J. Drysdale, Geraint L. Francis, et al. "Abstract A212: A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor‐induced apoptosis in HCT116 colon carcinoma cells." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-a212.

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Rodina, Anna, Yanlong Kang, Ronnie Maharaj, Alexander Gozman, Tony Taldone, Leandro Cerchietti, Michael J. H. Wong, et al. "Abstract 5463: YK5, a novel dual Hsc70 and Hsp70 inhibitor, is selective for tumor Hsp70 and has potent but selective activity in cancer cells." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5463.

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Sharif Siam, Mohammad Kawsar, Afsana Karim, and Mohammad Umer Sharif Shohan. "In-Silico Study for Potential Inhibitors of Both HSP72 and HSC70 Proteins in the Treatment of Cancer." In CSBio2020: The 11th International Conference on Computational Systems-Biology and Bioinformatics. New York, NY, USA: ACM, 2020. http://dx.doi.org/10.1145/3429210.3429226.

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Hughes, Edward G., Swee Y. Sharp, and Paul Workman. "Abstract B83: Modulation of the HSP90 cochaperone carboxy‐terminus HSC70‐interacting protein (CHIP) increases cellular sensitivity to heat shock protein 90 (HSP90) inhibition." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-b83.

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Kurozumi, S., Y. Yamaguchi, H. Matsumoto, H. Takei, Y. Kobayashi, S.-I. Hayashi, J. Yanagisawa, J. Horiguchi, I. Takeyoshi, and M. Kurosumi. "Abstract P2-11-18: Immunohistochemical expression of ubiquitin ligase CHIP (carboxyl terminus of Hsc70-interacting protein) as a significant prognostic marker in postmenopausal invasive breast cancer patients." In Abstracts: Thirty-Sixth Annual CTRC-AACR San Antonio Breast Cancer Symposium - Dec 10-14, 2013; San Antonio, TX. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/0008-5472.sabcs13-p2-11-18.

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SHERMAN, MICHAEL. "HSP70 ON THE CROSSROAD BETWEEN STRESS AND CANCER." In HOMO SAPIENS LIBERATUS. TORUS PRESS, 2020. http://dx.doi.org/10.30826/homosapiens-2020-11.

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Sannino, Sara, Christopher J. Guerriero, Amit J. Sabnis, Trever G. Bivona, and Jeffrey L. Brodsky. "Abstract 2325: Protein homeostasis adaptation to Hsp70 inhibition in cancer." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-2325.

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Sannino, Sara, Christopher J. Guerriero, Amit J. Sabnis, and Jeffrey J. Bridsky. "Abstract 4268: Protein folding pathway modulation upon Hsp70 inhibition in cancer cells." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-4268.

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Sannino, Sara, Christopher J. Guerriero, Amit J. Sabnis, and Jeffrey J. Bridsky. "Abstract 4268: Protein folding pathway modulation upon Hsp70 inhibition in cancer cells." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-4268.

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Seo, Ji Hae, So-Jin Shin, Jin Young Kim, Seungmee Lee, Hyewon Chung, and Chi-Heum Cho. "Abstract 2666: ARD1-mediated Hsp70 acetylation protects cancer cells against the cellular stress." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-2666.

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