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Статті в журналах з теми "Hsp31"
Rasouly, Aviram, Yotam Shenhar, and Eliora Z. Ron. "Thermoregulation of Escherichia coli hchA Transcript Stability." Journal of Bacteriology 189, no. 15 (May 25, 2007): 5779–81. http://dx.doi.org/10.1128/jb.00453-07.
Повний текст джерелаMujacic, Mirna, and Fran�ois Baneyx. "Chaperone Hsp31 Contributes to Acid Resistance in Stationary-Phase Escherichia coli." Applied and Environmental Microbiology 73, no. 3 (December 8, 2006): 1014–18. http://dx.doi.org/10.1128/aem.02429-06.
Повний текст джерелаSubedi, Krishna P., Dongwook Choi, Insook Kim, Bumchan Min, and Chankyu Park. "Hsp31 of Escherichia coli K-12 is glyoxalase III." Molecular Microbiology 81, no. 4 (July 6, 2011): 926–36. http://dx.doi.org/10.1111/j.1365-2958.2011.07736.x.
Повний текст джерелаHansberg, Wilhelm, Teresa Nava-Ramírez, Pablo Rangel-Silva, Adelaida Díaz-Vilchis, and Aydé Mendoza-Oliva. "Large-Size Subunit Catalases Are Chimeric Proteins: A H2O2 Selecting Domain with Catalase Activity Fused to a Hsp31-Derived Domain Conferring Protein Stability and Chaperone Activity." Antioxidants 11, no. 5 (May 17, 2022): 979. http://dx.doi.org/10.3390/antiox11050979.
Повний текст джерелаZhang, Kai, Kuikui Jiang, Ruoxi Hong, Fei Xu, Wen Xia, Ge Qin, Kaping Lee, et al. "Identification and characterization of critical genes associated with tamoxifen resistance in breast cancer." PeerJ 8 (December 4, 2020): e10468. http://dx.doi.org/10.7717/peerj.10468.
Повний текст джерелаKim, Jihong, Dongwook Choi, Chankyu Park, and Kyoung-Seok Ryu. "Backbone resonance assignments of the Escherichia coli 62 kDa protein, Hsp31." Biomolecular NMR Assignments 11, no. 2 (March 3, 2017): 159–63. http://dx.doi.org/10.1007/s12104-017-9739-6.
Повний текст джерелаKim, Jihong, Dongwook Choi, So-Young Cha, Young-Mee Oh, Eunha Hwang, Chankyu Park, and Kyoung-Seok Ryu. "Zinc-mediated Reversible Multimerization of Hsp31 Enhances the Activity of Holding Chaperone." Journal of Molecular Biology 430, no. 12 (June 2018): 1760–72. http://dx.doi.org/10.1016/j.jmb.2018.04.029.
Повний текст джерелаChoi, Dongwook, Kyoung-Seok Ryu, and Chankyu Park. "Structural alteration of Escherichia coli Hsp31 by thermal unfolding increases chaperone activity." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1834, no. 2 (February 2013): 621–28. http://dx.doi.org/10.1016/j.bbapap.2012.11.006.
Повний текст джерелаHasim, Sahar, Nur Ahmad Hussin, Fadhel Alomar, Keshore R. Bidasee, Kenneth W. Nickerson, and Mark A. Wilson. "A Glutathione-independent Glyoxalase of the DJ-1 Superfamily Plays an Important Role in Managing Metabolically Generated Methylglyoxal in Candida albicans." Journal of Biological Chemistry 289, no. 3 (December 3, 2013): 1662–74. http://dx.doi.org/10.1074/jbc.m113.505784.
Повний текст джерелаNava-Ramírez, Teresa, Sammy Gutiérrez-Terrazas, and Wilhelm Hansberg. "The Molecular Chaperone Mechanism of the C-Terminal Domain of Large-Size Subunit Catalases." Antioxidants 12, no. 4 (March 30, 2023): 839. http://dx.doi.org/10.3390/antiox12040839.
Повний текст джерелаДисертації з теми "Hsp31"
Quigley, Paulene. "Structural studies of the chaperone Hsp31 from Escherichia coli /." Thesis, Connect to this title online; UW restricted, 2003. http://hdl.handle.net/1773/8696.
Повний текст джерелаMujacic, Mirna. "Characterization of regulation and expression patterns of Escherichia coli Hsp31 protein /." Thesis, Connect to this title online; UW restricted, 2006. http://hdl.handle.net/1773/8119.
Повний текст джерелаAndrade, Warne Pedro de. "Análise da expressão dos genes TRAP1, HSPB1, HSPD1, HSPA1L e HSPA1A em amostras de câncer epitelial de ovário implicações no prognóstico e na resistência a quimioterapia baseada em platina /." Botucatu, 2018. http://hdl.handle.net/11449/154391.
Повний текст джерелаResumo: Introdução: As proteínas de choque térmico (“Heat Shock Proteins”) são produzidas em resposta ao estresse patofisiológico nas células animais e não só fazem parte de várias etapas da carcinogênese, atuando principalmente como agentes antiapoptóticos, como também estão implicadas em mecanismos de resistência à quimioterapia em vários tipos de tumores. Objetivo: O presente estudo visa comparar a expressão dos genes TRAP1, HSPB1, HSPD1, HSPA1L e HSPA1A nas amostras de CEO (no tumor primário ou na metástase) com a expressão dos mesmos em amostras de tumores ovarianos benignos e tecido ovariano normal e correlacionar a expressão gênica com o prognóstico das pacientes e com a resistência ao tratamento com platina. Métodos: Foram avaliadas amostras de 51 pacientes operadas no Hospital Vera Cruz, entre os anos de 2008 a 2011, divididas em quatro grupos: CEO primário (n = 14), CEO metastático (n = 11), cistoadenoma seroso ovariano (n = 07) e ovário normal (n = 19). Utilizou-se a técnica de qRT-PCR para determinar o perfil de expressão dos genes. Resultados: As pacientes incluídas neste estudo apresentavam idade média de 56,75 anos. Não houve diferença significativa (valor-P> 0,050) na comparação entre a expressão dos genes e os grupos estudados. Os genes HSPA1A, HSPA1L e TRAP1 foram subexpressos e se diferiram significativamente dos genes em indivíduos com ovário normal. A expressão dos genes analisados não correlacionou se com as variáveis quantitativas, como idade, menarca, e tempo ... (Resumo completo, clicar acesso eletrônico abaixo)
Abstract: Heat Shock Proteins are produced in response to pathophysiological stress and take part in several stages of carcinogenesis, acting primarily as anti-apoptotic agents. They are also implicated in resistance to chemotherapy in several types of tumors. Herein we correlated the expression of genes encoding these proteins and the clinical and pathological aspects of patients with ovarian cancer (OC). METHODS: 51 patients included in the study were divided into four groups: those with primary EOC (n = 14), metastatic EOC (n = 11), ovarian serous cystadenoma (n = 7), with no evidence of ovarian malignancy or control (n = 11). The 57 tumor samples obtained were submitted to RNA extraction and reverse transcription. qRT-PCR was performed to compare the expression of TRAP1, HSPB1, HSPD1, HSPA1A and HSPA1L in primary and HSP60, HSP70, HSPA1L genes did not differ among the groups (p-value> 0.050) .HSPA1A, HSPA1L and TRAP1 we underexpressed in the primary and metastatic EOC groups with HSPA1L showing the lowest expression with compare with normal ovary tissue. TRAP1 expression was higher in tumors at stage I/II than at stages III/IV. Grade II subjects showed higher HSPB1 expression. There was no correlation between HSPs expression and age, menarche, parity, period after menopause initiation and CA-125. HSPA1A gene was negatively correlated with the risk of dying of OC. There was no differences between HSP expression gene evaluated and overall and disease-free survival. In conclusion, we ... (Complete abstract click electronic access below)
Mestre
Smith, Carly M. "HSPC1 inhibitors and their use in Chronic Lymphocytic Leukaemia." Thesis, University of Chester, 2015. http://hdl.handle.net/10034/617678.
Повний текст джерелаPATEL, VIJAY LAXMAN. "ARABIDOPSIS HSP21 AND MSRB1/MSRB2 IN PLANT STRESS TOLERANCE." Thesis, The University of Arizona, 2008. http://hdl.handle.net/10150/192201.
Повний текст джерелаSilva, Fábio Fernando Alves da. "Avaliação do papel de HSPB1 na modulação da autofagia induzida por PRL em células-beta." Universidade de São Paulo, 2018. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-24082018-092045/.
Повний текст джерелаType 1 diabetes mellitus is a metabolic disease characterized by glycemic dysregulation, which occurs due to an autoimmune destruction of beta-cells. Insulin therapy is the gold standard treatment for DM1. However, some DM1 patients do not respond efficiently to this treatment and suffer frequent episodes of severe hypoglycemia unawareness. Since this complication jeopardizes the quality of life of these people, Islet transplantation is a therapeutic alternative indicated to treat these patients. However, besides the lack of enough organ donors, the loss of beta cells during both the isolation as well as the infusion of islets into the recipient induce a great estresse and thus a significant cell death is one of the drawbacks of this procedure. Autophagy is a mechanism of recycling cytoplasmic components and is essential for cellular homeostasis. Under estresse conditions, this mechanism is activated above basal levels, promoting the degradation of protein aggregates and defective organelles, thus avoiding cell damage that could compromise cell viability. Studies carried out by our group have shown not only that PRL promotes cytoprotection in beta-cells, reducing pro-inflammatory cytokines-induced apoptosis, but also that HSPB1 plays an essential role in this inhibition of apoptosis mediated by PRL after treatment with cytokines. Moreover, recent results from our laboratory showed an increase in autophagy levels in beta-cells after exposure to cytokines, as well as a restauration to normal levels in the presence of PRL. In order to better understand the role of PRL in the modulation of autophagy in these cells, the aim of this project is to study whether HSPB1 is also essential in the mechanism of autophagy regulation induced by PRL. Using MIN6 beta cell models where HSPB1 was silenced (MIN6-shHSPB1) or not (MIN6-SsC), we studied cell death by viability assays. Moreover, western blot assays were performed in order to assess levels of autophagy and autophagic flux markers in the cells.Our results showed that HSPB1 in one of the mediators of PRL-induced modulation of autophagy. Nevertheless, since hormonal treatment was still able to inhibit cytokinesinduced cell death even in the presence of chloroquin, an autophagy blocker, we conclude that autophagy is not a signaling pathway involved in PRl-induced beta-cell cytoprotection. Altogether, the results shown in this study may help to increase the knowledge of the molecular events induced by PRL in beta-cells, and may allow to infer new approaches to improve cytoprotection, culture and transplantation of these cells into type 1 diabetic patients.
Bissonnette, Lyne. "Identification de déterminants moléculaires impliqués dans l'activation et le largage de hSPC1/furine." Mémoire, Université de Sherbrooke, 2003. http://savoirs.usherbrooke.ca/handle/11143/3327.
Повний текст джерелаSamsel, Kara Ann. "The Role of Chloroplast-localized HSP21 in the Stress Responses of Arabidopsis Thaliana." Thesis, The University of Arizona, 2010. http://hdl.handle.net/10150/146645.
Повний текст джерелаAlmeida, Breno Fernando Martins de. "O papel da heme oxigenase-1 na leishmaniose visceral canina /." Araçatuba, 2016. http://hdl.handle.net/11449/143430.
Повний текст джерелаCoorientador: Paulo César Ciarlini
Banca:Luiz Daniel de Barros
Banca:Flavia Lombardi Lopes
Banca:Suely Regina Mogami Bomfim
Banca; Rosimeri de Oliveira Vasconcelos
Resumo: A leishmaniose visceral canina (LVC) é uma doença crônica que causa imunossupressão nos animais doentes, principalmente por prejudicar a resposta imunológica celular, diminuindo a proliferação linfocitária e a capacidade fagocítica das células de defesa. Recentemente, a enzima heme oxigenase-1 (HO-1) vem ganhando destaque por estar envolvida na regulação da resposta imune celular em algumas condições patológicas, sendo uma enzima induzível por condições de estresse, como o estresse oxidativo que sabidamente ocorre na LVC. Nesse contexto, esse trabalho teve por objetivo determinar o papel da HO-1 na LVC, determinando sua concentração e expressão em cães infectados e saudáveis, correlacionando-a com o estresse oxidativo, carga parasitária e IL-10. Objetivou-se também avaliar o efeito da indução e inibição da enzima sobre a resposta linfoproliferativa de células de linfonodo de cães doentes e sobre a taxa de infecção macrofágica por promastigotas de Leishmania infantum, determinando as citocinas envolvidas. Os cães com LVC apresentaram marcante estresse oxidativo e aumento da concentração e expressão de HO-1, obtendo-se correlação positiva entre HO-1e estresse oxidativo e IL-10 de acordo com o tecido analisado. A inibição de HO-1 aumentou a taxa de proliferação celular na presença de antígeno solúvel de L. infantum, enquanto a indução de HO-1 diminuiu a taxa de proliferação antígeno-específica e aumentou a taxa de infecção macrofágica e o número de amastigotas por macrófago. Con... (Resumo completo, clicar acesso eletrônico abaixo)
Abstract: Canine visceral leishmaniasis (CVL) is a chronic disease that causes immunosuppression by reducing the cellular response of infected animals, impairing the cell proliferation and the phagocytic ability of defense cells. Recently, heme oxygenase-1 (HO-1) has been highlighted for being involved in regulation of cell response in certain pathological conditions, and for being an enzyme that can be induced by stress conditions, such as oxidative stress, that is known to occur in CVL. In this context, this study aimed to determine the role of HO-1 in CVL, determining its levels and expression in infected and healthy dogs, correlating these findings with oxidative stress, parasite load and IL-10. The effect of induction and inhibition of HO-1 on lymphoproliferative response by lymph node cells of infected dogs and macrophage infection rate by promastigotes of Leishmania infantum were also evaluated. Dogs with CVL showed marked oxidative stress and increased levels and expression of HO-1, obtaining a positive correlation between HO-1 and oxidative stress and IL-10 in a tissue-dependent way. Inhibition of HO-1 increased proliferation rate in the presence of L. infantum soluble antigen, while induction of HO-1 decreased antigen-specific proliferation and increased macrophage infection rate and number of amastigotes per macrophage. The increase in HO-1 metabolism observed in CVL is associated to oxidative stress present in these dogs and could be one of the mechanisms involved in the in... (Complete abstract click electronic access below)
Doutor
Gibert, Benjamin. "La protéine de stress Hsp27 / HspB1, une cible de choix en thérapie anti-cancéreuse." Phd thesis, Université Claude Bernard - Lyon I, 2010. http://tel.archives-ouvertes.fr/tel-00733751.
Повний текст джерелаКниги з теми "Hsp31"
Public District School Board Writing Partnership (Ontario) and Ontario Ministry of Education, eds. Introduction to anthropology, psychology, and sociology: Course profile, grade 11, university/college preparation HSP3M. [Ontario]: Queen's Printer for Ontario, 2001.
Знайти повний текст джерелаEsquisse de cours 11e année: Introduction à la psychologie, à la sociologie et à l'anthropologie hsp3m cours préuniversitaire. Vanier, Ont: CFORP, 2001.
Знайти повний текст джерелаЧастини книг з теми "Hsp31"
Arrigo, André Patrick. "HspB1." In Encyclopedia of Signaling Molecules, 2451–58. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101690.
Повний текст джерелаArrigo, André Patrick. "HspB1." In Encyclopedia of Signaling Molecules, 1–8. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101690-1.
Повний текст джерелаIwamoto, Ryo, Eisuke Mekada, Thomas G. Hofmann, Eva Krieghoff-Henning, Masaaki Kobayashi, Ken Takamatsu, Jennifer Defren, et al. "Hspb1-Kinase." In Encyclopedia of Signaling Molecules, 886. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100627.
Повний текст джерелаArrigo, André-Patrick. "Structure–Functions of HspB1 (Hsp27)." In Methods in Molecular Biology, 105–19. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-295-3_9.
Повний текст джерелаBenndorf, Rainer, and Peter R. Jungblut. "Reconsidering Old Data: Non-canonical HspB1 Species and the Enigma of the Cytoskeletal Function of HspB1." In Heat Shock Proteins, 471–85. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16077-1_20.
Повний текст джерелаPanneerselvam, Lakshmikanthan, Azhwar Raghunath, Kiruthika Sundarraj, and Ekambaram Perumal. "HO-1/HSP32 and Cardiac Stress Signaling." In Heat Shock Proteins, 139–59. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-03952-3_8.
Повний текст джерелаDoshi, Bindi M., Lawrence E. Hightower, and Juliet Lee. "Heat Shock Alters Keratocyte Movement and Morphology: Exploring a Role for HSP27 (HSPB1)." In Heat Shock Proteins, 457–69. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16077-1_19.
Повний текст джерелаArrigo, André-Patrick. "Analysis of HspB1 (Hsp27) Oligomerization and Phosphorylation Patterns and Its Interaction with Specific Client Polypeptides." In Methods in Molecular Biology, 163–78. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7477-1_12.
Повний текст джерелаMusiani, Daniele, John David Konda, Simona Pavan, Erica Torchiaro, Jessica Erriquez, Martina Olivero, and Maria Flavia Di Renzo. "Heat Shock Protein 27 (HSP27, HSPB1) Is Up-Regulated by Targeted Agents and Confers Resistance to Both Targeted Drugs and Chemotherapeutics." In Heat Shock Proteins, 17–25. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-17211-8_2.
Повний текст джерелаArrigo, Andre-Patrick. "Anti-apoptotic, Tumorigenic and Metastatic Potential of Hsp27 (HspB1) and αB-crystallin (HspB5): Emerging Targets for the Development of New Anti-Cancer Therapeutic Strategies." In Heat Shock Proteins in Cancer, 73–92. Dordrecht: Springer Netherlands, 2007. http://dx.doi.org/10.1007/978-1-4020-6401-2_4.
Повний текст джерелаТези доповідей конференцій з теми "Hsp31"
Song, Yan, Yi-ling Hou, Wan-ru Hou, Guang-fu Wu, and Tian Zhang. "cDNA, Genomic Sequence Cloning and Sequence Analysis of Heat Shock Protein Beta-1 Gene (HSPB1) from the Giant Panda (Ailuropoda melanoleuca)." In 2010 4th International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2010. http://dx.doi.org/10.1109/icbbe.2010.5517383.
Повний текст джерелаЗвіти організацій з теми "Hsp31"
McElwain, Terry F., Eugene Pipano, Guy H. Palmer, Varda Shkap, Stephn A. Hines, and Wendy C. Brown. Protection of Cattle against Babesiosis: Immunization against Babesia bovis with an Optimized RAP-1/Apical Complex Construct. United States Department of Agriculture, September 1999. http://dx.doi.org/10.32747/1999.7573063.bard.
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