Relevant bibliographies by topics / Hsp60 and Hsp70

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Academic literature on the topic 'Hsp60 and Hsp70'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Hsp60 and Hsp70"

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Tiwari, Shraddha, Raman Thakur, and Jata Shankar. "Role of Heat-Shock Proteins in Cellular Function and in the Biology of Fungi." Biotechnology Research International 2015 (December 31, 2015): 1–11. http://dx.doi.org/10.1155/2015/132635.

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Stress (biotic or abiotic) is an unfavourable condition for an organism including fungus. To overcome stress, organism expresses heat-shock proteins (Hsps) or chaperons to perform biological function. Hsps are involved in various routine biological processes such as transcription, translation and posttranslational modifications, protein folding, and aggregation and disaggregation of proteins. Thus, it is important to understand holistic role of Hsps in response to stress and other biological conditions in fungi. Hsp104, Hsp70, and Hsp40 are found predominant in replication and Hsp90 is found in transcriptional and posttranscriptional process. Hsp90 and Hsp70 in combination or alone play a major role in morphogenesis and dimorphism. Heat stress in fungi expresses Hsp60, Hsp90, Hsp104, Hsp30, and Hsp10 proteins, whereas expression of Hsp12 protein was observed in response to cold stress. Hsp30, Hsp70, and Hsp90 proteins showed expression in response to pH stress. Osmotic stress is controlled by small heat-shock proteins and Hsp60. Expression of Hsp104 is observed under high pressure conditions. Out of these heat-shock proteins, Hsp90 has been predicted as a potential antifungal target due to its role in morphogenesis. Thus, current review focuses on role of Hsps in fungi during morphogenesis and various stress conditions (temperature, pH, and osmotic pressure) and in antifungal drug tolerance.
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Gurer, Cagan, Andrea Cimarelli, and Jeremy Luban. "Specific Incorporation of Heat Shock Protein 70 Family Members into Primate Lentiviral Virions." Journal of Virology 76, no. 9 (May 1, 2002): 4666–70. http://dx.doi.org/10.1128/jvi.76.9.4666-4670.2002.

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ABSTRACT To determine if any heat shock proteins are incorporated into human immunodeficiency virus type 1 (HIV-1) virions in a manner similar to that of the peptidyl-prolyl isomerase cyclophilin A, we probed purified virions with antibodies against heat shock proteins Hsp27, Hsp40, Hsp60, Hsp70, Hsc70, and Hsp90. Of these proteins, Hsp60, Hsp70, and Hsc70 associated with virions purified based on either particle density or size and were shown to be incorporated within the virion membrane, where they were protected from digestion by exogenous protease. Virion incorporation of Hsp70 was also observed with HIV-2 and with simian immunodeficiency viruses SIVMAC and SIVAGM, but it appears to be specific for primate lentiviruses, since Hsp70 was not detected in association with Moloney murine leukemia virus virions. Of the HIV-1 genes, gag was found to be sufficient for Hsp70 incorporation, though Hsp70 was roughly equimolar with pol-encoded proteins in virions.
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Ziegert, M., S. S. Witkin, I. Sziller, H. Alexander, E. Brylla, and W. Härtig. "Heat Shock Proteins and Heat Shock Protein-Antibody Complexes in Placental Tissues." Infectious Diseases in Obstetrics and Gynecology 7, no. 4 (1999): 180–85. http://dx.doi.org/10.1155/s1064744999000307.

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Objective:The relationship between pregnancy outcome and expression of the heat shock proteins (hsps) or hsp-antibody complexes of 60kD (hsp60), 70kD (hsp70), and 90kD (hsp90) in placental tissue and circulating antibodies to hsps was evaluated.Method:Expression of hsp60, hsp70, and hsp90 in placentae from 12 women with preterm birth, eight with intrauterine growth restriction (IUGR), and 10 with term birth, as well as the presence of the corresponding antibodies, was investigated by a new carbocyanine double fluorescence technique. Results were compared with microbiological findings and circulating antibodies to hsps in sera.Results:In each placental specimen examined, hsp60, hsp70, and hsp90 were identified. However, hsp70-antibody complexes were detected in only four of the preterm labor cases. Similarly, hsp60-antibody complexes were detected in only five preterm labor patients and in one patient with IUGR. None of the placentae contained hsp90-antibody complexes. In the preterm birth group, all patients with hsp60-antibody complexes were also positive for circulating antibodies to hsp60. The presence of hsp70-antibody complexes also correlated with hsp70 antibody in sera.Conclusions:Formation of hsp60- and hsp70-antibody complexes in the placenta may contribute to the induction of preterm birth. Women sensitized to these antibodies may be at increased risk for adverse pregnancy outcome. Infect. Dis. Obstet. Gynecol. 7:180–185, 1999.
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Alexiou, George A., George Vartholomatos, Kalliopi Stefanaki, Amalia Patereli, Lefkothea Dova, Achilleas Karamoutsios, George Lallas, George Sfakianos, Maria Moschovi, and Neofytos Prodromou. "Expression of heat shock proteins in medulloblastoma." Journal of Neurosurgery: Pediatrics 12, no. 5 (November 2013): 452–57. http://dx.doi.org/10.3171/2013.7.peds1376.

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Object Medulloblastoma (MB) is the most common malignant brain tumor in children. Heat shock proteins (HSPs) comprise a superfamily of proteins that serve as molecular chaperones and are overexpressed in a wide range of human cancers. The purpose of the present study was to investigate the expression of HSP27 (pSer82), HSP27 (pSer15), HSP40, HSP60, HSP70, HSP90-α, Akt, and phospho-Akt by multiplex bead array assay of MBs. The results of HSP and Akt expression were correlated with MB subtype; immunohistochemical expression of Ki-67 index, bcl-2, and p53; and patients' prognosis. Methods The authors retrospectively evaluated 25 children with MB who underwent surgery. Immunohistochemical analysis of Ki-67, p53, and bcl-2 expression was performed in all cases. By using multiplex bead array assay, a simultaneous detection of HSP27 (pSer82), HSP27 (pSer15), HSP40, HSP60, HSP70, HSP90-α, Akt, and phospho-Akt was performed. Results Medulloblastoma with extensive nodularity had significantly lower HSP27 (pSer15) expression (p = 0.039) but significantly higher HSP60 expression (p = 0.021) than classic MB. Large-cell MB had significantly higher HSP70 expression (p = 0.028) than classic MB. No significant difference was found between HSP27 (pSer82), HSP40, HSP90-α, Akt, or phospho-Akt expression and MB subtype. Large-cell MBs had significantly higher Ki-67 index compared with classic MBs (p = 0.033). When analyzing all MBs, there was a significant negative correlation between HSP27 (pSer15) and Ki-67 index (r = −0.475, p = 0.016); a significant positive correlation between HSP70 expression and Ki-67 index (r = 0.407, p = 0.043); and a significant positive correlation between HSP70 expression and bcl-2 index (r = 0.491, p = 0.023). Patients with large-cell MB had a worse survival than those with classic MB, but the difference did not reach statistical significance (p = 0.076). Conclusions A substantial expression of several HSPs in MB was observed. Given that HSPs represent an attractive strategy for anticancer therapy, further studies, involving larger series of patients, are obviously necessary to clarify the relationship of HSPs with tumor aggressiveness and prognosis.
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Pitruzzella, Alessandro, Letizia Paladino, Alessandra Vitale, Stefania Martorana, Calogero Cipolla, Giuseppa Graceffa, Daniela Cabibi, et al. "Quantitative Immunomorphological Analysis of Heat Shock Proteins in Thyroid Follicular Adenoma and Carcinoma Tissues Reveals Their Potential for Differential Diagnosis and Points to a Role in Carcinogenesis." Applied Sciences 9, no. 20 (October 15, 2019): 4324. http://dx.doi.org/10.3390/app9204324.

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Hsp27, Hsp60, Hsp70, and Hsp90 are chaperones that play a crucial role in cellular homeostasis and differentiation, but they may be implicated in carcinogenesis. Follicular neoplasms of the thyroid include follicular adenoma and follicular carcinoma. The former is a very frequent benign encapsulated nodule, whereas the other is a nodule that infiltrates the capsule, blood vessels and the adjacent parenchyma, with a tendency to metastasize. The main objective was to assess the potential of the Hsps in differential diagnosis and carcinogenesis. We quantified by immunohistochemistry Hsp27, Hsp60, Hsp70, and Hsp90 on thin sections of human thyroid tissue with follicular adenoma or follicular carcinoma, comparing the tumor with the adjacent peritumoral tissue. Hsp60, Hsp70, and Hsp90 were increased in follicular carcinoma compared to follicular adenoma, while Hsp27 showed no difference. Histochemical quantification of Hsp60, Hsp70, and Hsp90 allows diagnostic distinction between follicular adenoma and carcinoma, and between tumor and adjacent non-tumoral tissue. The quantitative variations of these chaperones in follicular carcinoma suggest their involvement in tumorigenesis, for instance in processes such as invasion of thyroid parenchyma and metastasization.
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Cheng, Yunfeng, Yong Tang, and Neal S. Young. "T Cells Response and Autoantibodies to Human Heat Shock Proteins in Aplastic Anemia Patients." Blood 106, no. 11 (November 16, 2005): 2403. http://dx.doi.org/10.1182/blood.v106.11.2403.2403.

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Abstract Heat shock proteins (HSP) have been implicated in autoimmune diseases such as type I diabetes mellitus, systemic lupus erythematosus, and multiple sclerosis, in which T cell proliferative responses or autoantibodies towards endogenous HSP have been detected (Journal of Autoimmunity2003;20:313). HSP70 can function as an endogenous ‘danger’ signal, acting on antigen-presenting cells and critically influencing the decision between induction of tolerance and immunity upon antigen encounter (Millar et al. Nature Medicine2003; 9:1469). We studied T-cell proliferative responses and auto-antibodies to human HSP60, HSP70 and HSP90 proteins in 20 newly diagnosed aplastic anemia patients, peripheral blood was obtained (11 females, 9 males; age average 36.1±19 years). A non-isotopic immunoassay was used for BrdU incorporation into proliferative T cells and ELISA to measure HSP antibody titer. T cell proliferation was measured as the Eu-fluorescence in a time-resolved fluorometer. A positive result was defined as > 2 standard deviations (SD) from the mean of the controls. T-cell responses to HSP70 in the patient group (N=20; mean±SD Eu-fluorescence= 47,129±36,248) were significantly greater than those of the control group (N=18 healthy adult; mean Eu-fluorescence= 23,941±12,996; p=0.01). Fifty percent of the patients showed increased T cell proliferation after HSP70 stimulation compared to 5% in the control group (p=0.03). T-cell responses of the patient group to HSP90 and HSP60 were similar to those of the control group. Twenty percent of patients showed increased T cell proliferation to HSP 60 and HSP 90 stimulation compared to 5% in the control group (p=0.363). HSP antibody (IgG/A/M) seropositivity was 25% to HSP60, 50% to HSP70, and 5% to HSP90 in patients and 8% to HSP60, 0% to HSP70, and 0% to HSP90 in controls. Heightened autoimmunity to HSP70, but not to HSP60 and HSP90, is a feature of acquired aplastic anemia at presentation.
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Barutta, Federica, Silvia Pinach, Sara Giunti, Ferdinando Vittone, Josephine M. Forbes, Roberto Chiarle, Maryann Arnstein, et al. "Heat shock protein expression in diabetic nephropathy." American Journal of Physiology-Renal Physiology 295, no. 6 (December 2008): F1817—F1824. http://dx.doi.org/10.1152/ajprenal.90234.2008.

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Heat shock protein (HSP) HSP27, HSP60, HSP70, and HSP90 are induced by cellular stresses and play a key role in cytoprotection. Both hyperglycemia and glomerular hypertension are crucial determinants in the pathogenesis of diabetic nephropathy and impose cellular stresses on renal target cells. We studied both the expression and the phosphorylation state of HSP27, HSP60, HSP70, and HSP90 in vivo in rats made diabetic with streptozotocin and in vitro in mesangial cells and podocytes exposed to either high glucose or mechanical stretch. Diabetic and control animals were studied 4, 12, and 24 wk after the onset of diabetes. Immunohistochemical analysis revealed an overexpression of HSP25, HSP60, and HSP72 in the diabetic outer medulla, whereas no differences were seen in the glomeruli. Similarly, exposure neither to high glucose nor to stretch altered HSP expression in mesangial cells and podocytes. By contrast, the phosphorylated form of HSP27 was enhanced in the glomerular podocytes of diabetic animals, and in vitro exposure of podocytes to stretch induced HSP27 phosphorylation via a P38-dependent mechanism. In conclusion, diabetes and diabetes-related insults differentially modulate HSP27, HSP60, and HSP70 expression/phosphorylation in the glomeruli and in the medulla, and this may affect the ability of renal cells to mount an effective cytoprotective response.
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Caruso Bavisotto, Celeste, Calogero Cipolla, Giuseppa Graceffa, Rosario Barone, Fabio Bucchieri, Donatella Bulone, Daniela Cabibi, et al. "Immunomorphological Pattern of Molecular Chaperones in Normal and Pathological Thyroid Tissues and Circulating Exosomes: Potential Use in Clinics." International Journal of Molecular Sciences 20, no. 18 (September 11, 2019): 4496. http://dx.doi.org/10.3390/ijms20184496.

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The thyroid is a major component of the endocrine system and its pathology can cause serious diseases, e.g., papillary carcinoma (PC). However, the carcinogenic mechanisms are poorly understood and clinical useful biomarkers are scarce. Therefore, we determined if there are quantitative patterns of molecular chaperones in the tumor tissue and circulating exosomes that may be useful in diagnosis and provide clues on their participation in carcinogenesis. Hsp27, Hsp60, Hsp70, and Hsp90 were quantified by immunohistochemistry in PC, benign goiter (BG), and normal peritumoral tissue (PT). The same chaperones were assessed in plasma exosomes from PC and BG patients before and after ablative surgery, using Western blotting. Hsp27, Hsp60, and Hsp90 were increased in PC in comparison with PT and BG but no differences were found for Hsp70. Similarly, exosomal levels of Hsp27, Hsp60, and Hsp90 were higher in PC than in BG, and those in PC were higher before ablative surgery than after it. Hsp27, Hsp60, and Hsp90 show distinctive quantitative patterns in thyroid tissue and circulating exosomes in PC as compared with BG, suggesting some implication in the carcinogenesis of these chaperones and indicating their potential as biomarkers for clinical applications.
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Lebret, Thierry, R. William G. Watson, Vincent Molinié, Amanda O'Neill, Christophe Gabriel, John M. Fitzpatrick, and Henry Botto. "Heat shock proteins HSP27, HSP60, HSP70, and HSP90." Cancer 98, no. 5 (July 16, 2003): 970–77. http://dx.doi.org/10.1002/cncr.11594.

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Wu, Reen, Yu Hua Zhao, Charles G. Plopper, Mary Mann-Jong Chang, Ken Chmiel, John J. Cross, Alison Weir, Jerold A. Last, and Brian Tarkington. "Differential expression of stress proteins in nonhuman primate lung and conducting airway after ozone exposure." American Journal of Physiology-Lung Cellular and Molecular Physiology 277, no. 3 (September 1, 1999): L511—L522. http://dx.doi.org/10.1152/ajplung.1999.277.3.l511.

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The presence of seven stress proteins including various heat shock proteins [27-kDa (HSP27), 60-kDa (HSP60), 70-kDa (HSP70) and its constitutive form HSC70, and 90-kDa (HSP90) HSPs] and two glucose-regulated proteins [75-kDa (GRP75) and 78-kDa (GRP78) GRPs] in ozone-exposed lungs of nonhuman primates and in cultured tracheobronchial epithelial cells was examined immunohistochemically by various monoclonal antibodies. Heat treatment (42°C) resulted in increased HSP70, HSP60, and HSP27 and slightly increased HSC70 and GRP75 but no increase in GRP78 in primary cultures of monkey tracheobronchial epithelial cells. Ozone exposure did not elevate the expression of these HSPs and GRPs. All of these HSPs including HSP90, which was undetectable in vitro, were suppressed in vivo in monkey respiratory epithelial cells after ozone exposure. Both GRP75 and GRP78 were very low in control cells, and ozone exposure in vivo significantly elevated these proteins. These results suggest that the stress mechanism exerted on pulmonary epithelial cells by ozone is quite different from that induced by heat. Furthermore, differences between in vitro and in vivo with regard to activation of HSPs and GRPs suggest a secondary mechanism in vivo, perhaps related to inflammatory response after ozone exposure.
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Dissertations / Theses on the topic "Hsp60 and Hsp70"

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D'Souza, Sandra Maria. "Constitutive expression of heat shock proteins hsp90, hsc70, hsp70 and hsp60 in the rat during postnatal development." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp01/MQ34098.pdf.

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Gomes, Francisco Edvan Rodrigues. "Clonagem, expressão e estudo de 3 co-chaperonas de Leishmania braziliensis." Universidade de São Paulo, 2011. http://www.teses.usp.br/teses/disponiveis/75/75132/tde-16092011-160310/.

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A leishmaniose é uma enfermidade infecciosa causada por várias espécies de parasitas do gênero Leishmania e representa um dos principais problemas de saúde pública nos países subdesenvolvidos. No hospedeiro, a sobrevivência do protozoário causador dessa doença depende de uma classe especial de proteínas, as chaperonas moleculares ou proteínas de choque térmico como também são conhecidas. A função dessas proteínas é auxiliar no processo de enovelamento protéico, no transporte de proteínas entre as membranas e em muitas outras importantes funções celulares. Neste processo, as chaperonas moleculares são auxiliadas pelas suas co-chaperonas que desempenham função de destaque. Dentre as principais famílias de chaperonas moleculares temos as Hsp70 e as Hsp90 com suas respectivas co-chaperonas, as Hsp40 e a Aha1. O presente trabalho pretendeu inicialmente expressar e purificar as co-chaperonas moleculares Hsp40I e Hsp40II de L. braziliensis para realizar estudos de caracterização estrutural por meio das técnicas de dicroísmo circular e fluorescência. Contudo, a insolubilidade dessas proteínas, que pode ter sido causada pela presença de mutações nas sequências de DNA, motivou a caracterização de outra co-chaperona, a Aha1 de L. braziliensis (LbAha1). A LbAha1 foi expressa no sobrenadante celular e purificada por três etapas cromatográficas (troca aniônica, afinidade por íons cálcio e gel filtração). A análise da sequência de aminoácidos dessa proteína mostra que ela possui 9 resíduos de triptofano distribuídos nos dois domínios característicos da LbAha1. Estudos de desnaturação química por uréia, monitorados pelas técnicas de dicroísmo circular e fluorescência, mostram que os dois domínios da LbAha1 apresentam estabilidades diferentes. Os estudos estruturais realizados permitiram identificar as transições com o respectivo domínio.
Leishmaniasis is an infectious disease caused by several species of Leishmania species and represents major public health problems in developing countries. In the harborer, the survival of the parasite that cause this disease depends on a special class of proteins, molecular chaperones or heat shock proteins as they are also known. The function of these proteins is to assist in protein folding, transport of proteins and many other important cellular functions. In this process the molecular chaperones are helped by their co-chaperones that play a prominent role. Among the main families of molecular chaperones, there are Hsp70 and Hsp90 with their respective co-chaperones, Hsp40 and the Aha1. The present work, initially pretended to express and purify the molecular co-chaperones Hsp40I and Hsp40II of the L. braziliensis for structural characterization by spectroscopic techniques like fluorescence and circular dichroism. However, the insolubility of these proteins, possibly caused by the presence of mutations in their DNA sequences, led to the characterization of another co-chaperone, the Aha1 of the L. braziliensis. These proteins were expressed in the cell supernatant and purified by three chromatographic steps (anion exchange, affinity for calcium ions and gel filtration). The analysis of the DNA sequence of this protein shows that it has nine Trp residues distributed between the two domains and by urea denaturation studies monitored by fluorescence techniques and circular dichroism show that they have different stabilities.
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EL, YAAGOUBI ABDELHAMID. "Role des proteines de choc thermique (dont dnak/hsp70 et groel/hsp60) dans l'expression des proteines chez escherichia coli." Paris 11, 1995. http://www.theses.fr/1995PA112423.

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Cette these a ete consacree a l'etude du role des proteines de choc thermique (hsps) d'e. Coli dans l'expression de proteines chez e. Coli. D'abord, nous avons montre que le chaperon dnak/hsp70, chez e. Coli, est implique dans l'exportation de la galactose binding protein, mglb, ainsi que dans la stabilite de son arm mglb. Par ailleurs nous avons localise dnak au niveau des jonctions de bayer (sites d'adhesion des membranes interne et externe chez e. Coli). Alors que groel interagit preferentiellement avec les chaines laterales des acides amines hydrophobes et affiche une interaction moindre avec les acides amines polaires, nous avons montre que groes reduit la specificite de groel pour les acides amines hydrophobes et augmente sa specificite pour les hydrophiles. Cette modulation par groes de l'affinite de groel pour les chaines laterales des acides amines du substrat proteique pourrait avoir une implication importante dans le repliement de proteines. Nous avons montre egalement que l'activite atpase de groel est stimulee specifiquement par la forme liee au ligand de la galactose binding protein d'escherichia coli, tandis ce qu'elle est faiblement affectee par sa forme non liee. Cette interaction est refletee par la stimulation de l'activite atpase de groel par la galactose binding protein. La troisieme partie decrit la purification d'une nouvelle proteine de choc thermique membranaire de 29 kda, chez e. Coli, qui est en cours de caracterisation. La derniere partie decrit la ca racterisation du systeme de transport galactose binding protein-dependant de s. Thyphimurium dont l'expression est etudie dans la premiere partie de la these. Nous avons purifie et caracterise la proteine mgla comme etant une atpase galactose-dependante. Nous avons reconstitue ce systeme de transport de galactose dans des proteoliposomes
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Schwindel, Uwe. "Prognosefaktoren beim nichtkleinzelligen Bronchialkarzinom Inzidenz von p53, bcl-2, HER-2, HSP27, HSP60 und HSP70 in nichtkleinzelligen Bronchialkarzinomen des Stadiums IIIA /." [S.l.] : [s.n.], 2003. http://archiv.ub.uni-marburg.de/diss/z2003/0697/.

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Brinker, Achim. "Proteininteraktionsdomänen in Hsp70-Hsp90-Multichaperonkomplexen." [S.l. : s.n.], 2001. http://deposit.ddb.de/cgi-bin/dokserv?idn=963295527.

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Silva, Luciana Pugliese da. "Estudo da expressão dos genes de choque térmico hsp90, hsp60 e hsp10 do fungo aquático Blastocladiella emersonii." Universidade de São Paulo, 2003. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-14052018-120842/.

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A proteína de choque térmico Hsp90 é uma chaperone molecular encontrada no citosol. O cDNA incompleto desta proteína foi isolado de uma biblioteca construída a partir de mRNA de células de esporulação de B. emersonii submetidas a choque térmico. Um clone genômico contendo a seqüência completa do gene hsp90 também foi isolado, seqüenciado e caracterizado. A região codificadora do gene hsp90 é interrompida por um único íntron de 184 nucleotídeos. A seqüência de aminoácidos deduzida indicou uma proteína de 71 O resíduos, com massa molecular calculada de 80.792 Da e um pl médio de 4,85. Experimentos de extensão de oligonucleotídeo e RACE-PCR demonstraram um sítio único de início de transcrição localizado a -65 e -70 nucleotídeos do ATG da metionina iniciadora, respectivamente. Motivos similares ao consenso do elemento de choque térmico eucariótico (HSE) e do elemento responsivo a estresse (STRE) foram encontrados na região promotora do gene a -395 e -98 nucleotídeos do ATG, respectivamente. Experimentos de \"Northern blot\" revelaram que o mRNA para a Hsp90 apresenta níveis máximos aos 90 minutos da fase de esporulação do fungo. Análise por \"western blot\" mostrou que a proteína Hsp90 está presente durante todo o ciclo de vida do fungo e os níveis máximos de acúmulo foram observados aos 90 minutos da esporulação, indicando um controle transcricional do gene. Tanto a proteína quanto o mRNA são altamente induzidos quando as células são submetidas a choque térmico e a cádmio. As proteínas Hsp60 e Hsp10 são chaperones moleculares mitocondriais (chaperoninas). Os cDNAs completos destas proteínas foram isolados e totalmente seqüenciados. A seqüência de aminoácidos deduzida da Hsp60 corresponde a uma proteína de 559 resíduos, com massa molecular calculada em 58.741 Da e um pl médio de 8, 7. Experimentos de \"Northern blot\" revelaram que o mRNA para Hsp60 tem níveis máximos de expressão aos 90 minutos da esporulação. Análise por \"western blot\" mostrou que a Hsp60 está presente durante todo o ciclo de vida do fungo, com níveis máximos da proteína 90 minutos após a indução da esporulação. Tanto a proteína quanto o mRNA são bastante induzidos quando as células são submetidas ao choque térmico. A seqüência de aminoácidos deduzida da Hsp10 corresponde um polipeptídeo de 101 resíduos com massa molecular calculada em 10.688 Da e um pl médio de 6,25. Experimentos de \"Northern blot\" revelaram que o mRNA para Hsp10 tem níveis máximos de expressão aos 120 minutos da germinação e é bastante induzido quando as células são submetidas ao choque térmico.
The heat shock protein 90 (Hsp90) is a cytosolic molecular chaperone. The incomplete cDNA of this protein was isolated by immunoblot screening of a heat shock cDNA expression library. The complete genomic clone was also isolated and completely sequenced and characterized. The coding sequence is interrupted by a single intron with 184 nucleotides. The deduced amino acid sequence corresponds to a 710-residue polypeptide with a calculated molecular mass of 80,792 Da and an average pl of 4.85. Primer extension and RACE-PCR experiments demonstrated a single transcription start site localized -65 and -70 nucleotides from de ATG of the initiator methionine, respectively. Sequence motifs resembling the standard eukaryotic heat shock element (HSE) and the stress responsive element (STRE) were evident in the regulatory region -395 and -98 nucleotides from de ATG, respectively. Northern blot analysis revealed that the Hsp90 mRNA presents maximum levels by 90 minutes of the sporulation stage. Immunoblot analysis indicated that the Hsp90 is present during the entire life cycle of the fungus and maximum levels were observed 90 minutes after the induction of sporulation, indicating a transcriptional control. During heat shock both the mRNA and the Hsp90 protein are highly induced. Proteins Hsp60 and Hsp10, are mitochondrial molecular chaperones (chaperonines). The complete cDNAs encoding these proteins were and completely sequenced. The deduced amino acid sequence for Hsp60 corresponds to a 559-residue polypeptide with a calculated molecular mass of 58,741 Da and an average pl of 8.7. Immunoblot analysis showed that Hsp60 is present during the entire life cycle of the fungus and presents maximum levels by 90 minutes of the sporulation. Northern blot analysis indicated maximum levels of the Hsp60 mRNA by 90 minutes of sporulation too. Both mRNA and the protein are highly induced during heat shock. The deduced amino acid sequence for Hsp10 corresponds to a 101-residue polypeptide with a calculated molecular mass of 10,688 Da and an average pl of 6.25. Northern blot analysis indicated maximum mRNA levels by 120 minutes of germination and high levels of expression when the cells are exposed to heat shock.
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De, Simone Andrea Stefano. "Daily modulation of the Heat shock proteins (Hsps) in three different species of scleractinian corals." Master's thesis, Alma Mater Studiorum - Università di Bologna, 2015. http://amslaurea.unibo.it/8401/.

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Temperature and light intensity is the most important environmental parameters that influence circadian cycle of scleractinian corals. In this context, modulation of the biomarkers Hsp60 and Hsp70 in situ was investigated by three different healthy coral species (Acropora tenuis, Echinopora lamellosa and Porites lobata) not stress induced during time course of 24h. Significance species-specific modulation under natural conditions is displayed by all corals under study. A strong fluctuation in Hsps expression is shown by the most susceptible, branched coral A. tenuis, instead of fine and low modulation is shown by the massive coral P. lobata. From the results match between morphology difference and physiological difference response its suggest and similarity pattern between Hsps with different cellular compartments location is suggested too. Starting from this study health of coral reefs could be able to be investigated in the future with a set of biomarkers composed also by Hsps which will be set up.
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Coto, Amanda Laís de Souza. "Estudo estrutural e funcional da co-chaperona SGT de Leishmania braziliensis." Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/75/75133/tde-17112016-135653/.

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As chaperonas moleculares são ativas em muitos processos celulares envolvendo o enovelamento e a homeostase de proteínas. Essas características fazem das chaperonas alvos potenciais para o tratamento de diversas doenças. As Hsp70 e as Hsp90, em especial, são proteínas ubíquas altamente conservadas biologicamente que atuam no enovelamento de proteínas nascentes, prevenção da agregação proteica, recuperação de proteínas de agregados, sinalização e crescimento celular, dentre outros. Contudo, para que essas proteínas cumpram eficientemente suas funções, elas devem ser moduladas por co-chaperonas moleculares. A SGT é uma co-chaperona que pode ser dividida em três regiões: domínio N-terminal, domínio TPR e domínio C-terminal, sendo que a região do domínio TPR é a responsável pela interação com o motivo EEVD no C-terminal das Hsp90 e Hsp70 citoplasmáticas. A SGT é encontrada em vários organismos, dentre eles os protozoários do gênero Leishmania spp.. Estes organismos são responsáveis pela leishmaniose, uma doença negligenciada que afeta milhares de pessoas todos os anos, principalmente em países subdesenvolvidos. Evidências indicam que a SGT em protozoários é essencial para o crescimento e viabilidade da forma promastigota. Diante disso, nesse trabalho foi feito o estudo estrutural e funcional da co-chaperona SGT de Leishmania braziliensis (LbSGT). A LbSGT recombinante foi produzida e purificada. A caracterização estrutural indica que a LbSGT é uma proteína rica em estrutura secundária do tipo hélice α que se comporta como um dímero alongado em solução. Dados de estabilidade térmica e química indicam que a LbSGT é uma proteína formada por domínios com diferentes estabilidades. A LbSGT foi identificada in vivo e o western blotting indicou sua presença cognata nas formas promastigotas do protozoário. Os ensaios de interação indicam que as interações entre a LbSGT e a Hsp90 de L. braziliensis (LbHsp90) e a LbSGT e Hsp70-1A humana (usada como proteína modelo) são diferentes da interação da LbSGT com o peptídeo MEEVD. Sendo assim, esses dados sugerem que a interação da LbSGT com a Hsp70-1A e LbHsp90 envolvem mais regiões das proteínas do que somente o motivo de interação da Hsp70-1A e da LbHsp90 com o domínio TPR da LbSGT. Em conjunto, as propriedades estruturais e funcionais da LbSGT observadas estão de acordo com a possível função da SGT como proteína adaptadora entre os sistemas Hsp70 e Hsp90 no foldossoma.
The molecular chaperones are active in many cellular processes involving protein folding and homeostasis. These characteristics make the chaperones potential targets to the treatment of many diseases. Hsp70 and Hsp90, in special, are highly conserved ubiquitous proteins that act in the folding of nascent proteins, protein aggregation prevention, aggregate recovering, signaling and cellular growth, among others. However, for these proteins to effectively fulfill their function, they must be modulated by molecular co-chaperones. SGT is a co-chaperone that can be divided into three domains: a N-terminal domain, a TPR domain and a C-terminal domain, being the TPR domain responsible for the interaction with the EEVD motif at the C-terminus of cytoplasmic Hsp90 and Hsp70. SGT is found in various organisms; among they are the protozoans of Leishmania spp.. These organisms are responsible for leishmaniasis, a neglected disease that affects thousands people every year, mainly at underdeveloped countries. Evidences indicate that SGT in protozoans are essential to the growth and viability of promastigote form. Therefore, the structural and functional study of the Leishmania braziliensis SGT (LbSGT) is presented. Recombinant LbSGT was produced and purified. The structural characterization points that LbSGT is rich in α-helix secondary structure and behaves as an elongated dimer in solution. Chemical and thermal stability data suggest that LbSGT is formed by domains of different stabilities. LbSGT was identified in vivo and the western blotting indicates its cognate presence in the protozoan promastigote forms. The interaction assays show that the interaction between LbSGT and Hsp90 of L. braziliensis (LbHsp90) or human Hsp70-1A (used as model protein) were different from the interaction between LbSGT with MEEVD peptide. Moreover, these data suggests that the interaction between LbSGT and Hsp70-1A and LbHsp90 involves additional protein regions besides the Hsp70-1A and LbHsp90 interaction motif. Altogether, the observed functional and structural proprieties of LbSGT accord to the SGT possible function as an adapter protein between the Hsp70 and Hsp90 systems in the foldossome.
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Njunge, James Mwangi. "Characterization of the Hsp40 partner proteins of Plasmodium falciparum Hsp70." Thesis, Rhodes University, 2014. http://hdl.handle.net/10962/d1013186.

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Human malaria is an economically important disease caused by single-celled parasites of the Plasmodium genus whose biology displays great evolutionary adaptation to both its mammalian host and transmitting vectors. This thesis details the 70 kDa heat shock protein (Hsp70) and J protein chaperone complements in malaria parasites affecting humans, primates and rodents. Heat shock proteins comprise a family of evolutionary conserved and structurally related proteins that play a crucial role in maintaining the structural integrity of proteins during normal and stress conditions. They are considered future therapeutic targets in various cellular systems including Plasmodium falciparum. J proteins (Hsp40) canonically partner with Hsp70s during protein synthesis and folding, trafficking or targeting of proteins for degradation. However, in P. falciparum, these classes of proteins have also been implicated in aiding the active transport of parasite proteins to the erythrocyte cytosol following erythrocyte entry by the parasite. This host-parasite “cross-talk” results in tremendous modifications of the infected erythrocyte, imparting properties that allow it to adhere to the endothelium, preventing splenic clearance. The genome of P. falciparum encodes six Hsp70 homologues and a large number of J proteins that localize to the various intracellular compartments or are exported to the infected erythrocyte cytosol. Understanding the Hsp70-J protein interactions and/or partnerships is an essential step for drug target validation and illumination of parasite biology. A review of these chaperone complements across the Plasmodium species shows that P. falciparum possesses an expanded Hsp70-J protein complement compared to the rodent and primate infecting species. It further highlights how unique the P. falciparum chaperone complement is compared to the other Plasmodium species included in the analysis. In silico analysis showed that the genome of P. falciparum encodes approximately 49 J proteins, 19 of which contain a PEXEL motif that has been implicated in routing proteins to the infected erythrocyte. Most of these PEXEL containing J proteins are unique with no homologues in the human system and are considered as attractive drug targets. Very few of the predicted J proteins in P. falciparum have been experimentally characterized. To this end, cell biological and biochemical approaches were employed to characterize PFB0595w and PFD0462w (Pfj1) J proteins. The uniqueness of Pfj1 and the controversy in literature regarding its localization formed the basis for the experimental work. This is the first study showing that Pfj1 localizes to the mitochondrion in the intraerythrocytic stage of development of P. falciparum and has further proposed PfHsp70-3 as a potential Hsp70 partner. Indeed, attempts to heterologously express and purify Pfj1 for its characterization are described. It is also the first study that details the successful expression and purification of PfHsp70-3. Further, research findings have described for the first time the expression and localization of PFB0595w in the intraerythrocytic stages of P. falciparum development. Based on the cytosolic localization of both PFB0595w and PfHsp70-1, a chaperone – cochaperone partnership was proposed that formed the basis for the in vitro experiments. PFB0595w was shown for the first time to stimulate the ATPase activity of PfHsp70-1 pointing to a functional interaction. Preliminary surface plasmon spectroscopy analysis has revealed a potential interaction between PFB0595w and PfHsp70-1 but highlights the need for further related experiments to support the findings. Gel filtration analysis showed that PFB0595w exists as a dimer thereby confirming in silico predictions. Based on these observations, we conclude that PFB0595w may regulate the chaperone activity of PfHsp70-1 in the cytosol while Pfj1 may play a co-chaperoning role for PfHsp70-3 in the mitochondrion. Overall, this data is expected to increase the knowledge of the Hsp70-J protein partnerships in the erythrocytic stage of P. falciparum development, thereby enhancing the understanding of parasite biology.
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Daniel, Sheril. "Molecular characterization of the Hsp70/Hsp90 organizing protein (Hop) phosphorylation, subcellular localization and interaction with Hsp90." Thesis, Rhodes University, 2008. http://hdl.handle.net/10962/d1004056.

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Hop (Hsp70-Hsp90 Organizing Protein) is a co-chaperone of two major molecular chaperones, Hsp70 and Hsp90, and acts by transferring substrates from Hsp70 to Hsp90. Although under normal conditions Hop is predominantly localized within the cytosol, Hop has been detected in the nucleus under certain conditions including cell cycle arrest. A putative nuclear localization signal (NLS) has been identified within Hop, which overlaps with the TPR2A domain (previously shown to be critical for Hop-Hsp90 interactions). Hop is phosphorylated in vitro by two cell cycle kinases, namely, casein kinase II (CKII) at S189 and cdc2-kinase at T198; both residues are found upstream of the putative NLS and TPR2A domain. Mimicking phosphorylation at either phosphorylation site appeared to affect the subcellular localization of Hop. The aim of this study was to characterize Hop with respect to its phosphorylation status in vivo, as well as its subcellular localization pattern under heat stress and determine how these properties affected its interaction with Hsp90 as a co-chaperone. Dephosphorylation of proteins under normal and heat shock conditions changed the isoform composition of Hop, providing strong evidence that Hop was phosphorylated in vivo. Surface plasmon resonance (SPR) and glutatione-S-transferase (GST) co-precipitation studies showed that a cdc2-kinase phosphorylated mimic of Hop disrupted Hop-Hsp90 binding. A full length Hop-EGFP construct, as well as substitution mutants of the predicted NLS residues within the Hop-EGFP construct, were transfected into baby hamster kidney (BHK)-21 cells in order to establish the subcellular localization of Hop under heat stress and to test whether predicted residues were critical for nuclear localization of Hop. Under normal conditions, both Hop-EGFP and the NLS mutants were predominantly cytosolic, but when the cells were subjected to heat stress, Hop and its NLS-mutants were localized to both the cytosol and the nucleus. SPR and GST co-precipitation studies showed that substitution of the residues within the major arm of the putative NLS abrogated Hop-Hsp90 interactions. The data obtained from this study, showed for the first time, that Hop was phosphorylated in vivo and suggested that phosphorylation of Hop by cdc2-kinase could inhibit Hop-Hsp90 interactions. Moreover, these results suggested that the subcellular localization of Hop was dependent on stress levels of the cell, particularly heat stress. We propose that the nuclear localization of Hop may be primarily regulated by stress and secondarily by cell cycle arrest. The major arm of the putative NLS did not affect the localization of Hop directly, but was shown to be critical for Hop-Hsp90 binding in vitro. The results of this study suggested that binding of Hop to Hsp90 sequestered Hop within the cytosol and that Hsp90 acted as a cytosolic retention factor for Hop. Both phosphorylation of Hop, and its subcellular localization, appeared to be intimately related to its interaction with Hsp90 as a co-chaperone.
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Books on the topic "Hsp60 and Hsp70"

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D'Souza, Sandra Maria. Constitutive expression of heat shock proteins HSP90, HSP70 and HSP60 in the rat during postnatal developemnt. Ottawa: National Library of Canada, 1998.

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Bross, Peter. The Hsp60 Chaperonin. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-26088-4.

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Asea, Alexzander A. A., and Punit Kaur, eds. HSP70 in Human Diseases and Disorders. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-89551-2.

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Manzerra, Pasquale. Expression of constitutive hsc70 and stress-inducible hsp70 mRNA and protein in the rabbit central nervous system. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1997.

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Malyshev, Igor. Immunity, Tumors and Aging: The Role of HSP70. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-5943-5.

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Kociuba, Katarzyna. An examination of chromatin-associated hsp70 during heat shock in Drosophila. Ottawa: National Library of Canada, 1999.

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Balasubramaniam, Janani. Identification of anoxia-induced expression of HSP70 in Chrysemys picta belli hepatocytes. Ottawa: National Library of Canada, 1999.

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Borkar, Monica. Cloning and characterization of an hsp70 genomic sequence in the steroid responsive fungus Achlya ambisexualis. Ottawa: National Library of Canada, 1994.

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Belay, Hiwote Taddes. Spatial analysis of cell death and Hsp70 induction in brain, thymus, bone marrow and testis of the hyperthermic rat. Ottawa: National Library of Canada, 2004.

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Khan, Vania Rhea. The effect of hyperthermia on the induction of cell death and HSP70 in neural and non-neural tissues of the rat. Ottawa: National Library of Canada, 2001.

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Book chapters on the topic "Hsp60 and Hsp70"

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Gupta, Radhey S., Nallur B. Ramachandra, Timothy Bowes, and Bhag Singh. "Unusual Cellular Disposition of the Mitochondrial Molecular Chaperones Hsp60, Hsp70 and Hsp10." In Novartis Foundation Symposia, 59–73. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/9780470754030.ch5.

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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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Martin, Jörg, and F. Ulrich Hartl. "Molecular Chaperones HSP70 and HSP60 in Protein Folding and Membrane Translocation." In Molecular Mechanisms of Membrane Traffic, 81–90. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-02928-2_16.

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Hartl, Franz Ulrich. "The Role of Molecular Chaperones Hsp70 And Hsp60 in Protein Folding." In Post-transcriptional Control of Gene Expression, 193–206. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-60929-9_17.

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Cappello, Francesco, Antonino Di Stefano, Everly Conway De Macario, and Alberto J. L. Macario. "Hsp60 and Hsp10 in Ageing." In Heat Shock Proteins and Whole Body Physiology, 401–26. Dordrecht: Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3381-9_23.

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Langer, T., and W. Neupert. "Heat Shock Proteins hsp60 and hsp70: Their Roles in Folding, Assembly and Membrane Translocation of Proteins." In Heat Shock Proteins and Immune Response, 3–30. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-75875-1_1.

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Daniel, Sheril, Csaba Söti, Peter Csermely, Graeme Bradley, and Gregory L. Blatch. "Hop: An Hsp70/Hsp90 Co-Chaperone That Functions Within and Beyond Hsp70/Hsp90 Protein Folding Pathways." In Networking of Chaperones by Co-Chaperones, 26–37. New York, NY: Springer New York, 2007. http://dx.doi.org/10.1007/978-0-387-49310-7_3.

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Bross, Peter. "Variations in Hsp60 and Hsp10 in Humans." In SpringerBriefs in Molecular Science, 55–56. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-26088-4_12.

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Faust, Ofrah, and Rina Rosenzweig. "Structural and Biochemical Properties of Hsp40/Hsp70 Chaperone System." In Advances in Experimental Medicine and Biology, 3–20. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-40204-4_1.

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Howe, Matthew K., and Timothy A. J. Haystead. "New Indications for HSP90 and HSP70 Inhibitors as Antiviral Drugs." In Heat Shock Proteins, 175–96. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-17211-8_10.

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Conference papers on the topic "Hsp60 and Hsp70"

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Wang, Sihong, Kenneth R. Diller, and Shanti J. Aggarwal. "Heat Shock Protein 70 Expression Kinetics." In ASME 2002 International Mechanical Engineering Congress and Exposition. ASMEDC, 2002. http://dx.doi.org/10.1115/imece2002-33678.

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HSP70 is well known for its major role in cardiac ischemia protection. The purpose of this study was to determine the HSP70 expression kinetics for new protocol design in cardiac surgery, based on HSP70 protection function in clinical applications. Bovine aortic endothelial cells (BAEC) were used in experiments. Cells were heated at 42°C at different time intervals up to 5 hours and subsequently incubated at 37°C for up to 48 hours. Western blot and quantitative protein analysis were performed to measure HSP70 expression. The expression kinetics is a function of thermal stress time as well as poststress time. At least three stages were identified for the kinetics curve: increasing, maximum plateau and decreasing regions. The peak HSP70 concentration is 10 times the basal level for western blot analysis in BAECs. Two hours incubator heating followed by twelve hours post-heating falls in the plateau region. This research result provides information applicable to evaluation of energy sources and heating methods to induce optimal HSP70 expression in a target tissue.
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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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Rylander, M. Nichole, Kenneth R. Diller, Sihong Wang, and Shanti J. Aggarwal. "Correlation of HSP70 Expression and Cell Viability Following Thermal Stimulation of Aortic Endothelial Cells." In ASME 2004 Heat Transfer/Fluids Engineering Summer Conference. ASMEDC, 2004. http://dx.doi.org/10.1115/ht-fed2004-56383.

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The goal of this study was to determine the kinetics of HSP70 expression and variations in cell viability resulting from thermal preconditioning of the heart. Experiments were conducted to determine combinations of elevated temperatures and brief heating durations that could produce enhanced HSP70 levels while maintaining high cell viability. Bovine aortic endothelial cells were heated with a water bath at temperatures ranging from 44–50°C and periods of 1–30 min consistent with anticipated protocols for cardiac preconditioning prior to surgery. Western blot and cell adhesion analysis in culture following heating were employed to determine HSP70 level and cell viability respectively. The results demonstrate that HSP70 expression and cell viability are not maximized simultaneously. To ensure cell viability greater than 90% required a heating protocol for which HSP70 expression was less than its maximum level. HSP70 expression increments from 2.3 to 3.6 times the value of the control can be achieved for thermal stimulation protocols varying from T = 46°C for 10 min to T = 50°C for 1 min while maintaining a cell viability of 90% or greater. An Arrhenius injury model was fit to the cell damage data yielding values for scaling and activation energy terms of A = 1.4×1066 s−1 and Ea = 4.1×105 J/mole.
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Zaman, Khalequz, Nadzeya V. Marozkina, Sean Yemen, Phillip Clapp, Marko Todorovic, Lisa A. Palmer, Scott H. Randell, and Benjamin M. Gaston. "Nitrosonium Corrects DF508 CFTR Expression By S-nitrosylation Of Hsp70/Hsp90 Organizing Protein Cysteine 403." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a6852.

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Moses, Michael A., Genesis Rivera-Marquez, Isabelle Taylor, Hao Shao, Jason Gestwicki, Jane Trepel, and Len Neckers. "Abstract 2901: Identifying synthetic lethal interactions in castration-resistant prostate cancer using HSP40 and HSP70 inhibitors." 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.am2018-2901.

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Shimp, Samuel K., Christopher M. Reilly, and Marissa Nichole Rylander. "Empirical Modeling the Effect of Hsp90 Inhibition on Cytokines Associated With Impaired Biotransport of Apoptotic Debris." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19572.

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Systemic lupus erythematosus (SLE) is a chronic inflammatory autoimmune disorder that can affect nearly every organ in the body. A link has been established between abnormal biotransport of apoptotic cell debris and pathogenesis of SLE [1]. Lupus mice are hyper-responsive to immune stimulation and overproduce inflammatory mediators including IL-6, IL-12, and nitric oxide (NO) [2]. Extracellular expression and transport of inflammatory cytokines are thought to be involved with the inhibited clearance of cellular debris [1]. Hsp90 has a prominent role in folding and conformational regulation of several client proteins, including proteins involved with production of inflammatory mediators [3]. Hsp90 readily binds ATP at the amino (N-) terminal domain. This binding event causes a conformational change in Hsp90 making it “clamp down” on its client protein [3]. Geldanamycin (Geld) is a known inhibitor of Hsp90 that out competes ATP binding at the N-terminal. This prevents chaperone capability and ultimately leads to client protein deactivation, destabilization, and degradation [3]. Hsp90 inhibitors have been shown to suppress immune stimulated release of interleukin 6 (IL-6), IL-12, tumor necrosis factor alpha (TNF-α), and nitric oxide (NO) [4].
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Moses, Michael A., Yeong Sang Kim, Genesis Rivera-Marquez, Matthew J. Watson, Sunmin Lee, Andrea Kravats, Sue Wickner, Jason Gestwicki, Jane Trepel, and Len Neckers. "Abstract 1180: Targeting the HSP40/HSP70 chaperone axis as a novel strategy to treat castration-resistant prostate cancer." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-1180.

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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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Zhang, Dongyun, Tongjian Cai, Jingxia Li, Max Costa, and Chuanshu Huang. "Abstract 4373: JNK1 participates in the VHL-independent HIF-1α degradation pathway by regulating Hsp90/Hsp70 turnover and the HDAC6-dependent chaperone activity." 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.am10-4373.

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Colunga Biancatelli, R. M. L., P. A. Solopov, P. E. Marik, and J. D. Catravas. "Hydrocortisone, Ascorbic Acid and Thiamine (HAT) Treatment Modulates Intracellular HSP90 and HSP70 Levels and Reduces Peripheral Blood Mononuclear Cell (PBMNC) Death in Septic Patients." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a3491.

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Reports on the topic "Hsp60 and Hsp70"

1

Madaeva, I. M., N. A. Kurashova, N. V. Semenova, E. B. Uhinov, S. I. Kolesnikov, and L. I. Kolesnikova. HSP70 HEAT SHOCK PROTEIN IN OXIDATIVE STRESS APNEA PATIENTS. Publishing house of the Russian Academy of Medical Sciences, 2020. http://dx.doi.org/10.18411/1695-1978-2020-62730.

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Madaev, I. M., N. A. Kurashova, N. V. Semenova, E. B. Ukhinov, S. I. Kolesnikov, and L. I. Kolesnikova. Heat shock protein HSP70 for oxidative stress in patients with apnea. Federal State Budgetary Institution Scientific Center, 2020. http://dx.doi.org/10.18411/1695-2608-2020-62730.

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Wang, Zhou. Role of Hsp90 in Androgen-Refractory Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, March 2010. http://dx.doi.org/10.21236/ada526578.

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Wang, Zhou. Role of Hsp90 in Androgen-Refractory Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, March 2009. http://dx.doi.org/10.21236/ada505267.

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Wang, Zhou. Role of Hsp90 in Androgen-Refractory Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, March 2008. http://dx.doi.org/10.21236/ada483027.

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Altieri, Dario C. Clinical Development of Gamitrinib, a Novel Mitochondrial-Targeted Small Molecule Hsp90 Inhibitor. Fort Belvoir, VA: Defense Technical Information Center, September 2014. http://dx.doi.org/10.21236/ada610693.

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Niu, Gang. Imaging Heat Shock Protein 90 (Hsp90) Activity in Hormone-Refractory Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, March 2009. http://dx.doi.org/10.21236/ada506361.

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Yao, Tso-Pang. Modulating EGFR Signaling by Targeting the Deacetylase HDAC6-Hsp90 Complex in Breast Tumors. Fort Belvoir, VA: Defense Technical Information Center, June 2007. http://dx.doi.org/10.21236/ada473895.

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Yao, Tso-Pang. Modulating EGFR Signaling by Targeting the Deacetylase HDAC6-Hsp90 Complex in Breast Tumors. Fort Belvoir, VA: Defense Technical Information Center, June 2006. http://dx.doi.org/10.21236/ada469574.

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Isaacs, Jennifer S. Extracellular Hsp90 as a Novel Epigenetic of EMT and Metastatic Risk in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 2014. http://dx.doi.org/10.21236/ada614029.

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