Littérature scientifique sur le sujet « HspSO »
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Articles de revues sur le sujet "HspSO"
Bala, Nurudeen Muhammad, et Suhailan Bin Safei. « A Hybrid Harmony Search and Particle Swarm Optimization Algorithm (HSPSO) for Testing Non-functional Properties in Software System ». Statistics, Optimization & ; Information Computing 10, no 3 (9 janvier 2021) : 968–82. http://dx.doi.org/10.19139/soic-2310-5070-1039.
Texte intégralXu, Ji, Hong Zhou, Yanjun Fang et Lan Liu. « Data-Driven Approach for the Short-Term Business Climate Forecasting Based on Power Consumption ». Wireless Communications and Mobile Computing 2022 (27 avril 2022) : 1–11. http://dx.doi.org/10.1155/2022/4037053.
Texte intégralBanu, P. K. Nizar, et S. Andrews. « Harmony Search PSO Clustering for Tumor and Cancer Gene Expression Dataset ». International Journal of Swarm Intelligence Research 5, no 3 (juillet 2014) : 1–21. http://dx.doi.org/10.4018/ijsir.2014070101.
Texte intégralKaneda, F., et P. G. Kwiat. « High-efficiency single-photon generation via large-scale active time multiplexing ». Science Advances 5, no 10 (octobre 2019) : eaaw8586. http://dx.doi.org/10.1126/sciadv.aaw8586.
Texte intégralTower, John. « Hsps and aging ». Trends in Endocrinology & ; Metabolism 20, no 5 (juillet 2009) : 216–22. http://dx.doi.org/10.1016/j.tem.2008.12.005.
Texte intégralChen, Wei, Pengmian Feng, Tao Liu et Dianchuan Jin. « Recent Advances in Machine Learning Methods for Predicting Heat Shock Proteins ». Current Drug Metabolism 20, no 3 (22 mai 2019) : 224–28. http://dx.doi.org/10.2174/1389200219666181031105916.
Texte intégralBaszczynski, Chris L. « Immunochemical analysis of heat-shock protein synthesis in maize (Zea mays L.) ». Canadian Journal of Genetics and Cytology 28, no 6 (1 décembre 1986) : 1076–87. http://dx.doi.org/10.1139/g86-151.
Texte intégralSong, Xueming, Zhiqiang Chen, Chunbo Wu et Shiguang Zhao. « Abrogating HSP Response Augments Cell Death Induced by As2O3 in Glioma Cell Lines ». Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 37, no 4 (juillet 2010) : 504–11. http://dx.doi.org/10.1017/s0317167100010544.
Texte intégralVierling, Elizabeth. « MOLECULAR ANALYSIS OF HEAT STRESS PROTEINS IN HIGHER PLANTS ». HortScience 25, no 9 (septembre 1990) : 1175e—1175. http://dx.doi.org/10.21273/hortsci.25.9.1175e.
Texte intégralRodríguez-Iturbe, B., et RJ Johnson. « Heat shock proteins and cardiovascular disease ». Physiology International 105, no 1 (mars 2018) : 19–37. http://dx.doi.org/10.1556/2060.105.2018.1.4.
Texte intégralThèses sur le sujet "HspSO"
Foglia, Antonio. « Design, synthesis and biological evaluation of new anticancer and/or anti-inflammatory agents ». Doctoral thesis, Universita degli studi di Salerno, 2017. http://hdl.handle.net/10556/2484.
Texte intégralOne of the main goal of modern medicinal chemistry is the development of new agents able to modulate biological targets involved in inflammation and cancer processes. In this context, my PhD project was focused on the exploration and structural optimization of various chemical moieties able to interfere with two targets involved in both processes. In particular, two biological targets were selected: Heat shock protein 90 (Hsp90) and microsomal Prostaglandin E2 Synthase-1 (mPGES-1). The results obtained can be divided into two sections in accordance with the target of interest. a) Exploration and structural optimization of DHPM core in order to guide the synthesis of new and more potent Hsp90 C-terminal inhibitors. Hsp90 is a molecular chaperone involved in the maturation and stabilization of a wide range of client proteins that play a crucial role in the development, survival and proliferation of cancer cells. In the literature there are several compounds capable of inhibiting this molecular chaperone. The most part of these compounds inhibit the protein through modulation of the N-terminal domain. However, this type of modulation involves a well-known heat shock response, a cytoprotective mechanism that as a final result leads to the increase of cytosolic levels of heat shock proteins with consequent cell survival. Therefore, the modulation of C-terminal domain of Hsp90 represents a better strategy for the development of new antitumor agents, since, they do not induce heat shock response. In an attempt to discover new modulators of the C-terminal domain of Hsp90 and taking into account the structure of the first synthetic inhibitor of this domain, a 3,4-dyhidropyrimidin-2(1H)-one (DHPM) derivative, two more generations of DHPM derivatives have been synthesized. Relatively to the second generation of DHPM derivatives, the synthesis was focused on the influence of the chemical functionalization of aromatic ring at C4 position of DHPM core, while the third generation has been designed with the aim to functionalize the C2 position of the core. The exploration and optimization processes of DHPM core led to the identification of novel and more potent inhibitors of the C-terminal domain of Hsp90. b) Identification of new mPGES-1 inhibitors. mPGES-1 is an inducible enzyme that catalyzes the terminal step of the biosynthesis of PGE2 from the PGH2 precursor. The inhibition of this enzyme appears to be a promising strategy for the identification of novel anti-inflammatory agents, because, the use of selective inhibitors would allow to overcome the classical side effects of traditional anti-inflammatory drugs. Moreover, mPGES-1 is overexpressed in a wide variety of human cancers and for this reason it has emerged as an attractive biological target for anticancer drug discovery. In order to identify new molecular platforms able to interact with the target protein three collections of compounds (carbazoles, biaryl compounds and 5-pyrazolones) were synthesized. Biological evaluation revealed the identification of five biaryl compounds (60-64) as new chemical entities that inhibit mPGES-1 activity with promising IC50 values (ranging 0.18-1.64 μM). [edited by author]
XIV n.s.
Bourrelle-Langlois, Maxime. « Caractérisation des petites protéines de stess/small heat shock proteins du cyanophage S-ShM2 (HspSP-ShM2) et de son hôte Synechococcus WH7803 (HspS-WH7803) ». Master's thesis, Université Laval, 2016. http://hdl.handle.net/20.500.11794/26763.
Texte intégralSmall heat shock proteins (sHsps) are ubiquitous ATP-independent molecular chaperones found in prokaryotes and eukaryotes. They are structurally dynamic and most of them have the ability to form large oligomeric complexes and to protect cells from proteotoxic stresses by preventing aggregation of non-native proteins and promoting their refolding via ATP-dependent chaperones such as Hsp70/DnaK. Recently, the presence of a sHsp gene (HspSP-ShM2) in marine viruses has been reported using bioinformatics tools. More precisely, the gene has been found in cyanophages infecting cyanobacteria of the genre Synechococcus sp. and Prochlorococcus sp. The Synechococcus phage sHSP has a MW of 18 kDa and shows the highly conserved core alpha crystalline domain of 92 amino acids and relatively short N- and C-terminal arms, the later containing the classical CAM domain (L-X-I/L/V). We established its oligomeric profile using a size exclusion chromatography (SEC) and Fast Protein Liquid Chromatography (FPLC) system and demonstrated its ability to form large oligomeric complexes in native conditions (600 kDa and 200kDa). Furthermore, we report its capacity to prevent the aggregation of citrate synthase, malate dehydrogenase and luciferase suggesting that it has a weak specificity and wide range of protein substrates. The complete prevention of aggregation was achieved at different ratios (sHsp:substrate) depending on the substrate indicating that the sHSP may have different and unique interactions with each of its clients. We also showed the formation of a stable and soluble hetero-oligomeric complex of the phage sHSP and its substrates under heat stress, which is in accordance with the characteristics of sHSP in general. The cyanobacteria Synechococcus WH7803 15 kDa sHSP (HspS-WH7803) shows the ability to form tetramers in the presence of Triton™X-100 for the maintenance of its solubility using the SEC/FPLC method. For its capability to prevent the aggregation of different substrates, HspS-WH7803 demonstrates no chaperon like activity in all the assays and molar ratios used. Finally, SEC/FPLC results indicate the possible formation of a hetero-oligomeric complex between the sHSP of the phage and the one from its host Synechococcus WH7803 (HspS-WH7803). This interaction could either optimize the chaperone activity and the stress response of its host or inhibit the host sHSP to facilitate the viral life cycle.
Gaborit, Nadège. « Intérêt de la vectorisation et/ou de l’induction des protéines de stress dans les modèles expérimentaux de pathologies ostéoarticulaires : Validation de l’électroporation biphasique ». Thesis, Nancy 1, 2008. http://www.theses.fr/2008NAN10127/document.
Texte intégralDuring articular diseases, chondrocytes suffer different mechanisms which take part in the degradation of the cartilage, either by generating cell death by apoptosis (without renewal of extracellular matrix components), or by protease activation which destroy matrix components. Based on the cytoprotective potential of Heat Shock proteins (Hsp70 and Hsp27) during degenerative diseases, we evaluated the therapeutic interest of these proteins induced by a transient proteasome inhibitor (MG132), in an experimental model, by transection of the anterior cruciate ligament (ACLT). During this study, we have evaluated a new electroporation system to overexpress HSPs in articular cartilage. This technique is based on two sets of electric pulses, wich have two roles, to permeabilize the target and to transport DNA across the permeabilized membrane. We have developed expression vectors to generate a fusion protein (Hsps linked to GFP). Effectively, GFP permit to detect simply the fusion protein in the targeted tissue by fluorescence. Besides, we have evaluated safety and efficiency of electric pulses on healthy and alterated tissues (degenerative and inflammatory). We have reported that this technique could limit articular tissue damages and, moreover, could offer the ability to target more specifically this tissue. Indeed, this apparatus allows a great number of electrics pulses combinations (number, frequency, intensity). Finally, the effects of the induction via MG132 of Hsps in a physiopathological ACLT model, have been evaluated and we have shown a decrease of severity of joint lesions, in cartilage and synovial tissues. This molecule has the advantage to reinforce the resistance of chondrocytes at stressful stimuli and moreover, to limite the amplitude of inflammatory response which contribute to the magnification of extracellular matrix destruction
Guzha, Delroy Tapiwa. « Investigating the biological roles of the HSPRO genes in Arabidopsis thaliana ». Doctoral thesis, University of Cape Town, 2015. http://hdl.handle.net/11427/15503.
Texte intégralWillis, Dean. « The role of heat shock proteins in models of acute inflammation ». Thesis, Queen Mary, University of London, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.265943.
Texte intégralFritah, Sabrina. « Implications des histones deacetylases de I et II dans la réponse au stress ». Université Joseph Fourier (Grenoble), 2008. http://www.theses.fr/2008GRE10270.
Texte intégralLn response to environmental stress (heat shock, hypoxia, heavy metals exposure), cells have developed rapid and transitory mechanisms to protect themselves from the stress-induced damages. This stress response is characterized by the activation of HSF1 (Heat Shock Factor1), a key factor involved in the induction of the HSP (Heat Shock Proteins) encoded genes. Ln contrast toheat shock genes induction, most of the genome is repressed du ring stress. If the mechanisms involved in the activation of HSP genes have been investigated in details, less is known about the global repression of the genome. We started to investigate the epigenetic mechanisms that underline this genome repression and identify the molecular basis of this phenomenon. By molecular and in situ approaches, we showed that HDACs (Histone Deacetylases) are new regulators of stress response. Heat shock induces major epigenetic changes, specially a global deacetylation of core histones. We showed that class 1 HDAC, HDACl and HDAC2 mediates the heat-induced deacetylation. This event is regulated by HSF1, probably through its interaction with HDACl and HDAC2. Ln the cytoplasm, HDACS are also able to regulate stress response. Indeed, upon proteotoxic stress for example, proteasome inhibition, we showed that HDAC6 play a critical role in initiating the stress response. It mediates the dissociation of HSFl from its repressor complex and HDAC6 has an impact in HSP induction in response to stress. Ln conclusion, we identify HDACs as new important factors of stress response. Thanks to this work, we have linked two classes of proteins that are targeted by anti-cancer therapy: HSPs and HDACs
Jacob, Tiago Rinaldi. « Expressão, regulação e funcionalidade de genes HSPs no dermatófito Trichophyton rubrum ». Universidade de São Paulo, 2014. http://www.teses.usp.br/teses/disponiveis/17/17135/tde-15052014-105536/.
Texte intégralThe dermatophyte Trichophyton rubrum is a filamentous, keratinophilic, and anthrophophilic fungi, being the major etiologic agent of cutaneous mycoses in humans. Its cosmopolitan distribution and the severe infection in immunocompromised patients make it one of the challenges to be faced by public health agencies worldwide. Hostpathogen interactions involve different processes related to keratin degradation and metabolic changes that allow adhesion and subsequent penetration of the infected tissue. These changes are important to the success of the infectious process and involve mechanisms that modulate gene expression, secretion of specific proteins, and metabolic adaptation, and cutaneous pH changes, essential to the establishment of the infection. Among the proteins that participate in the host-pathogen interaction are the heat shoch proteins (HSPs), related to diverse cellular processes. Thus, the hypothesis of this work was to evaluate whether T. rubrum hsp genes, as well as their major transcription factor (Hsf1), are involved in the response to adverse situations and in the interaction with the host microenvironment, and if these genes are regulated by the transcription fator PacC, a regulator of the pH signaling pathway. The expression of the hsp genes was evaluated in response to the cultivation of T. rubrum in different culture medium, during exposure to antifungal drugs, heat stress, and interaction with human nail and skin. The involvement of T. rubrum Hsp90 in the modulation of gene expression, susceptibility to antifungal drugs, and interaction with human nails was evaluated by using a chemical inhibitor, specific to this protein. Our results indicate a variable expression of the hsp genes, even among members of the same HSP family, in response to each environmental condition or interaction, to which the fungus was exposed. Furthermore, we have evidence that the hsp gene expression is modulated by the PacC transcription factor, by modulating the expression of the Hsf1 coding gene. We also found that Hsp90 is involved in T. rubrum susceptibility to the drugs Itraconazole and Micafungin, and in the development of this dermatophyte in human nails. These results reveal the involvement of HSPs in several aspects of T. rubrum metabolism, suggesting a role for Hsp90 in the pathogenicity and drug susceptibility in this dermatophyte
Monteiro, Janaína Munuera. « Imunolocalização das Heat Shock Proteins (HSPs) 60 e 70 na placenta bovina ». Universidade de São Paulo, 2005. http://www.teses.usp.br/teses/disponiveis/10/10132/tde-27062006-105146/.
Texte intégralHeat Shock Proteins (HSP) can be found in any kind of cell. These proteins are classified according to their molecular weight and their known families include the HSP 27, 60, 70, 90 and 110 kDa. Among these, HSP 60 and 70 are the ones of interest in reproduction. They were known as chaperonines because of their capacity to fold and unfold other proteins into the cell, without changing their own conformation. They are expressed during several stress conditions likes virus and bacteria infections, hormones, heat, cellular differentiation, etc, and also take part signalizing for innate and acquired immune responses. Heat shock proteins are expressed in several tissues and organs, including the placenta. In this study we have evaluated the expression of these proteins in the bovine placenta, using thirty samples from different animais with distinct gestational periods, fixed in 10% formalin and processed for immunohistochemistry. The same numbers of samples were processed for immunoelectron microscopy using freeze-substitution and post embedding labeling techniques. The immunohistochemistry results show the expression of HSP 60 and 70 in trophoblasts, maternal epithelia and binucleated cells. The HSP 60 expression was higher in the beginning of gestation, becoming lower during the second and third trimester. Heat shock protein 70 expression were practically constant throughout the gestation. The immunoelectron microscopy analysis revealed that both HSP 60 and 70 were located in the cytoplasm and nucleio binucleated cells and maternal epithelia from the beginning to the end of pregnancy. The immunolocalization of HSP 60 and 70 in the bovine placenta were distinct from the ones found in studies on women, probably due to the differences of the placentation type and to the fact that those samples were collected from abnormal or discontinuous pregnancy. Beef production in Brazil is an important economical activity and studies to improve the bovine reproductive characteristics are necessary and must be expended, therefore our results certainly contributes for further studies on HSP function during pregnancy in this species.
Champagne, Marie-Josée. « Caractérisation de la relation possible entre les protéines de stress (HSPs) et l'hypertension ». Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape10/PQDD_0002/NQ39728.pdf.
Texte intégralCoelho, Danielle Letícia Martins. « Estresse hídrico com diferentes osmóticos em sementes de feijão e expressão diferencial de proteínas durante a germinação ». Universidade do Oeste Paulista, 2008. http://bdtd.unoeste.br:8080/tede/handle/tede/349.
Texte intégralSnap Beans (Phaseolus vulgaris L) are highly valuable nutritionally, and it is cultivated by small, medium and big farmers. It represents a significant parcel of Brazilian economy concerning to the society. Culture emergency is a critical point in the production process and it is affected mainly by the water deficiency at this phase. The objective of this work was to simulate water deficiency in the germination beginning at the laboratory on seeds of snap beans ´Pérola´, using mannitol, CaCl2, MgCl2 and NaCl as osmotic in the potential of 0; -0.3; -0.6; -0.9 and -1.2MPa calculated with the aim of Van´t Hoff s equation and to evaluate the electrophorectical protein patterns of total soluble proteins by SDS-PAGE. Germination, vigour classification, roots and shoot dry weight and differential protein expression response was evaluated as parameters. The experimental design was completely randomized. Data was analysed by F test (ANOVA) and polynomial regression for the osmotic potential for each parameter evaluated. Banding pattern was evaluated by gel image. Simulation of deficiency, in laboratory, allowed the perception of the stress originated by NaCl in all parameter evaluated, validating the harsh of the NaCl and the lack of expression of low molecular weight proteins in this osmotic. 110 and 30kDa proteins were indicative of water stress, but not of salinity.
O feijão (Phaseolus vulgaris L) é uma cultura de grande expressão alimentícia. A emergência da cultura é dependente de água, sendo considerada a fase mais crítica. O objetivo deste foi simular deficiência de água no início da germinação em laboratório, em sementes de feijão Pérola , utilizando-se: manitol, CaCl2, MgCl2 e NaCl em potenciais de 0; -0,3; -0,6; -0,9 e -1,2MPa estabelecidos pela equação de Van´t Hoff e avaliar o perfil eletroforético de proteínas totais solúveis através de SDS-PAGE. Foram avaliados: germinação, classificação de vigor, massa seca de raiz e de parte aérea e resposta diferencial de expressão de proteínas. O delineamento experimental foi inteiramente casualizado. Os dados foram analisados através da aplicação do teste F, para análise de variância, regressão polinomial para os níveis de potencial osmóticos para cada uma das variáveis fisiológicas estudadas. O bandeamento eletroforético foi avaliado visualmente através da imagem dos géis. A simulação do estresse permitiu avaliar a drasticidade do NaCl em todos os parâmetros avaliados e a ausência de proteínas de baixo peso molecular neste osmótico. As proteínas de 110 e 30kDa foram indicativas de estresse hídrico, mas não do salino.
Livres sur le sujet "HspSO"
Berkeley. Office for History of Science and Technology University of California. Historical studies in the physical and biological sciences : HSPS. Berkeley : University of California Press, 1986.
Trouver le texte intégralCalderwood, Stuart Keith, Ayesha Murshid et Thiago J. Borges, dir. HSPs - Ambiguous Mediators of Immunity. Frontiers Media SA, 2017. http://dx.doi.org/10.3389/978-2-88945-152-4.
Texte intégralRPV, droner & andre platforme : OPTRONK/HSPS. [København : Faggruppe OPTRONIK, 1989.
Trouver le texte intégralNewport, Natalie. Navigating All Those Assholes : : A Guidebook for Empaths and HSPs. Independently Published, 2017.
Trouver le texte intégralNewport, Natalie. Navigating All Those A**holes : : A Guidebook for Empaths and HSPs. Independently Published, 2017.
Trouver le texte intégralHill, Silvia. Highly Sensitive People : What You Need to Know about HSPs and Their Gifts. EH Jolen, 2022.
Trouver le texte intégralChapitres de livres sur le sujet "HspSO"
Harr, Jeffrey N., Philip F. Stahel, Phillip D. Levy, Antoine Vieillard-Baron, Yang Xue, Muhammad N. Iqbal, Jeffrey Chan et al. « HSPs ». Dans Encyclopedia of Intensive Care Medicine, 1152. Berlin, Heidelberg : Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-00418-6_1713.
Texte intégralTomita, Misao, et Koki Shimoji. « Heterosegmental SCPs (HSPs) ». Dans Evoked Spinal Cord Potentials, 82–89. Tokyo : Springer Japan, 2006. http://dx.doi.org/10.1007/4-431-30901-2_8.
Texte intégralGearhart, Christopher C. « Highly Sensitive Person Scale (HSPS) ». Dans The Sourcebook of Listening Research, 299–305. Hoboken, NJ, USA : John Wiley & Sons, Inc., 2017. http://dx.doi.org/10.1002/9781119102991.ch28.
Texte intégralRui, Zhiqing, Jingzheng Wu, Yanjie Shao, Tianyue Luo, Mutian Yang, Yanjun Wu et Bin Wu. « PassEye : Sniffing Your Password from HTTP Sessions by Deep Neural Network ». Dans Communications in Computer and Information Science, 3–15. Singapore : Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-33-4922-3_1.
Texte intégralFecek, Ronald J., Subhara Raveendran, Manoj Chelvanambi et Walter J. Storkus. « Inhibition of HSPs for Enhanced Immunity ». Dans Heat Shock Proteins in the Immune System, 157–80. Cham : Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-69042-1_9.
Texte intégralGonçalves, Conrado C., et Carlos H. I. Ramos. « Molecular Chaperones and HSPs in Sugarcane and Eucalyptus ». Dans Heat Shock Proteins and Plants, 245–82. Cham : Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-46340-7_13.
Texte intégralHaslbeck, Martin, Sevil Weinkauf et Johannes Buchner. « Regulation of the Chaperone Function of Small Hsps ». Dans Heat Shock Proteins, 155–78. Cham : Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16077-1_6.
Texte intégralKim, Jong Youl, Jong Eun Lee et Midori A. Yenari. « Neuroprotection of Heat Shock Proteins (HSPs) in Brain Ischemia ». Dans Translational Medicine Research, 383–95. Singapore : Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-5804-2_17.
Texte intégralHerbert, Kate Reed, Afshin Samali et Adrienne Gorman. « The Role of Hsps in Neuronal Differentiation and Development ». Dans Heat Shock Proteins in Neural Cells, 25–37. New York, NY : Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-39954-6_3.
Texte intégralMoreno, Andrés Rodríguez, Óscar Torreño Tirado et Oswaldo Trelles Salazar. « Out of Core Computation of HSPs for Large Biological Sequences ». Dans Advances in Computational Intelligence, 189–99. Berlin, Heidelberg : Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-38682-4_22.
Texte intégralActes de conférences sur le sujet "HspSO"
Dogru, Nuran. « Increasing the Mode-Locking Range of HSPS ». Dans Frontiers in Optics. Washington, D.C. : OSA, 2006. http://dx.doi.org/10.1364/fio.2006.jsua29.
Texte intégralSong, Alfred S., et Kenneth R. Diller. « Modeling Heat Shock Protein Expression While Wearing a Therapeutic Heat Wrap ». Dans ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192823.
Texte intégralDogru, Nuran. « Grating parameters effect on actively mode-locked HSPS ». Dans LEOS 2009 -22nd Annuall Meeting of the IEEE Lasers and Electro-Optics Society (LEO). IEEE, 2009. http://dx.doi.org/10.1109/leos.2009.5343173.
Texte intégralBraga, Vinícius Lopes, Wladimir Bocca Vieira de Rezende Pinto, Bruno de Mattos Lombardi Badia, José Marcos Vieira de Albuquerque Filho, Igor Braga Farias, Paulo Victor Sgobbi de Souza et Acary Souza Bulle Oliveira. « Spastic paraplegia type 73 : expanding phenotype of the first two Brazilian families ». Dans XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.552.
Texte intégralChung, Eunna, et Marissa Nichole Rylander. « Effects of Growth Factors and Stress Conditioning on the Induction of Heat Shock Proteins and Osteogenesis ». Dans ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206662.
Texte intégralDe Silvestre Perrucio, Ligia, et Jaime Amaya-Farfan. « EFEITO DO CONSUMO DE AMINOÁCIDOS NAS HEAT SHOCK PROTEINS (HSPS) EM RATOS ». Dans XXIV Congresso de Iniciação Científica da UNICAMP - 2016. Campinas - SP, Brazil : Galoa, 2016. http://dx.doi.org/10.19146/pibic-2016-51284.
Texte intégralHosseini-Beheshti, Elham, Amina Zoubeidi, ka Mun Nip, Martin E. Gleave et Emma S. (Tomlinson) Guns. « Abstract 4150 : Exploration of the role of Hsps in exosome derived from prostate cancer cells ». Dans 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.am10-4150.
Texte intégralChung, Eunna, et Marissa Nichole Rylander. « Multi-Stress Conditioning Can Synergisticly Enhance Production of Osteogenic Markers and Heat Shock Proteins ». Dans ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19511.
Texte intégralHavlik, Nico, et Michael Lutz. « Optimization of Tilting-Pad Journal Bearings for Integrally Geared Compressors ». Dans ASME Turbo Expo 2015 : Turbine Technical Conference and Exposition. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/gt2015-42483.
Texte intégralRapports d'organisations sur le sujet "HspSO"
Miller, Gad, et Jeffrey F. Harper. Pollen fertility and the role of ROS and Ca signaling in heat stress tolerance. United States Department of Agriculture, janvier 2013. http://dx.doi.org/10.32747/2013.7598150.bard.
Texte intégralBlum, Abraham, Henry T. Nguyen et N. Y. Klueva. The Genetics of Heat Shock Proteins in Wheat in Relation to Heat Tolerance and Yield. United States Department of Agriculture, août 1993. http://dx.doi.org/10.32747/1993.7568105.bard.
Texte intégral