Littérature scientifique sur le sujet « Stress response protein p66ShcA »
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Articles de revues sur le sujet "Stress response protein p66ShcA"
Hu, Yuanyu, Xueying Wang, Li Zeng, De-Yu Cai, Kanaga Sabapathy, Stephen P. Goff, Eduardo J. Firpo et Baojie Li. « ERK Phosphorylates p66shcA on Ser36 and Subsequently Regulates p27kip1 Expression via the Akt-FOXO3a Pathway : Implication of p27kip1 in Cell Response to Oxidative Stress ». Molecular Biology of the Cell 16, no 8 (août 2005) : 3705–18. http://dx.doi.org/10.1091/mbc.e05-04-0301.
Texte intégralHusain, Mohammad, Leonard G. Meggs, Himanshu Vashistha, Sonia Simoes, Kevin O. Griffiths, Dileep Kumar, Joanna Mikulak et al. « Inhibition of p66ShcA Longevity Gene Rescues Podocytes from HIV-1-induced Oxidative Stress and Apoptosis ». Journal of Biological Chemistry 284, no 24 (21 avril 2009) : 16648–58. http://dx.doi.org/10.1074/jbc.m109.008482.
Texte intégralCanedo, Eduardo Cepeda, Sonia Del Rincon, Peter Siegel, Michael Witcher et Josie Ursini-Siegel. « Abstract 131 : The role of p66ShcA in the melanoma oncogenesis process ». Cancer Research 82, no 12_Supplement (15 juin 2022) : 131. http://dx.doi.org/10.1158/1538-7445.am2022-131.
Texte intégralMalhotra, Ashwani, Himanshu Vashistha, Virendra S. Yadav, Michael G. Dube, Satya P. Kalra, Maha Abdellatif et Leonard G. Meggs. « Inhibition of p66ShcA redox activity in cardiac muscle cells attenuates hyperglycemia-induced oxidative stress and apoptosis ». American Journal of Physiology-Heart and Circulatory Physiology 296, no 2 (février 2009) : H380—H388. http://dx.doi.org/10.1152/ajpheart.00225.2008.
Texte intégralVashistha, H., L. Marrero, K. Reiss, A. J. Cohen, A. Malhotra, T. Javed, A. Bradley et al. « Aging phenotype(s) in kidneys of diabetic mice are p66ShcA dependent ». American Journal of Physiology-Renal Physiology 315, no 6 (1 décembre 2018) : F1833—F1842. http://dx.doi.org/10.1152/ajprenal.00608.2017.
Texte intégralMiyazawa, Masaki, et Yoshiaki Tsuji. « Evidence for a novel antioxidant function and isoform-specific regulation of the human p66Shc gene ». Molecular Biology of the Cell 25, no 13 (juillet 2014) : 2116–27. http://dx.doi.org/10.1091/mbc.e13-11-0666.
Texte intégralBetts, Dean H., Nathan T. Bain et Pavneesh Madan. « The p66Shc Adaptor Protein Controls Oxidative Stress Response in Early Bovine Embryos ». PLoS ONE 9, no 1 (24 janvier 2014) : e86978. http://dx.doi.org/10.1371/journal.pone.0086978.
Texte intégralPacini, Sonia, Michela Pellegrini, Enrica Migliaccio, Laura Patrussi, Cristina Ulivieri, Andrea Ventura, Fabio Carraro et al. « p66SHC Promotes Apoptosis and Antagonizes Mitogenic Signaling in T Cells ». Molecular and Cellular Biology 24, no 4 (15 février 2004) : 1747–57. http://dx.doi.org/10.1128/mcb.24.4.1747-1757.2004.
Texte intégralMigliaccio, Enrica, Marco Giorgio, Simonetta Mele, Giuliana Pelicci, Paolo Reboldi, Pier Paolo Pandolfi, Luisa Lanfrancone et Pier Giuseppe Pelicci. « The p66shc adaptor protein controls oxidative stress response and life span in mammals ». Nature 402, no 6759 (novembre 1999) : 309–13. http://dx.doi.org/10.1038/46311.
Texte intégralSun, Lin, Li Xiao, Jing Nie, Fu-you Liu, Guang-hui Ling, Xue-jing Zhu, Wen-bin Tang et al. « p66Shc mediates high-glucose and angiotensin II-induced oxidative stress renal tubular injury via mitochondrial-dependent apoptotic pathway ». American Journal of Physiology-Renal Physiology 299, no 5 (novembre 2010) : F1014—F1025. http://dx.doi.org/10.1152/ajprenal.00414.2010.
Texte intégralThèses sur le sujet "Stress response protein p66ShcA"
Covington, Sean M. « The Stress Protein Response of Pimephales promelas to Copper ». Thesis, University of North Texas, 1992. https://digital.library.unt.edu/ark:/67531/metadc500868/.
Texte intégralGonçalves, Nuno M. « Insights into the rice response to abiotic stress : ». Doctoral thesis, Universidade Nova de Lisboa, Instituto de Tecnologia Química e Biológica António Xavier, 2019. http://hdl.handle.net/10362/95814.
Texte intégralN/A
Fogl, Claudia Liliane Fiona. « Structure and function of the cardiac stress response protein MS1 ». Thesis, University of Leicester, 2011. http://hdl.handle.net/2381/9408.
Texte intégralMalakasi, Panagiota. « The regulation of oxidative stress response by a conserved response regulator protein in yeast ». Thesis, University of Newcastle Upon Tyne, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.273360.
Texte intégralJenkins, Mark 1979. « A role for the Drosophila eIF4E binding protein during stress response / ». Thesis, McGill University, 2004. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=82256.
Texte intégralThe Drosophila forkhead transcription factor dFOXO is a transcriptional activator of d4E-BP. There is a strong reduction of d4E-BP peptide in a dFOXO null background. dFOXO null flies are also sensitive to oxidative stress, and rescue of this sensitivity through ectopic expression of UAS-d4E-BP(wt) in a dFOXO null background suggests d4E-BP is a downstream mediator of dFOXO oxidative stress resistance.
Mahmood, Ahsan. « Role of SLMAP in Endoplasmic Reticulum Stress and Unfolded Protein Response ». Thèse, Université d'Ottawa / University of Ottawa, 2013. http://hdl.handle.net/10393/24399.
Texte intégralHearne, Catherine Mary. « A study of the heat shock response of Bacillus subtilis ». Thesis, University of Cambridge, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.334111.
Texte intégralChalmers, Fiona. « Improving protein yield from mammalian cells by manipulation of stress response pathways ». Thesis, University of Glasgow, 2016. http://theses.gla.ac.uk/7666/.
Texte intégralMuthevhuli, Mpho. « Investigation of the role of AtNOGC1, a guanylyl cyclase protein in response to abiotic and biotic stress ». University of the Western Cape, 2018. http://hdl.handle.net/11394/6763.
Texte intégralAgricultural production is one of the most important sectors which provide food for the growing world population which is estimated to reach 9.7 billion by 2050, thus there is a need to produce more food. Climate change, on the other hand, is negatively affecting major global crops such as maize, sorghum, wheat and barley. Environmental factors such as salinity, drought, high temperatures and pathogens affect plant production by oxidatively damaging the physiological processes in plants, leading to plant death. Poor irrigation used to combat drought result in salinasation, which is estimated to affect 50% of arable land by 2050. Plants have developed several mechanisms that protect them against stress and these include overexpression of stress responsive genes and altered signal transduction to change the expression of stress responsive genes, among others. Cyclic 3’5’ guanosine monophosphate (cGMP), a second messenger that is synthesised by guanylyl cyclase (GC), transmit signals to various cellular functions in plants during plant development, growth and response to abiotic and biotic stresses. Arabidopsis thaliana nitric oxide guanylyl cyclase 1 (AtNOGC1) is a guanylyl cyclase which upon activation by nitric oxide (NO) leads to the production of more cGMP. Cyclic GMP further activates protein kinases, ion gated channels and phosphodiesterase which mediate response to various stresses. In this project the role of AtNOGC1 was investigated in response to abiotic and biotic stresses through analysis of its evolutionary relationships, promoter, gene expression and functional analysis via the viability assays in Escherichia coli (E.coli). Phylogenetic tree, exon-intron structure and conserved motifs were analysed using the Molecular Evolutionary Genetics Analysis (MEGA V.7), Gene Structure Display Server 2.0 (GSDS 2.0), and Multiple Expectation Maximisation for Motif Elicitation (MEME) tools respectively. AtNOGC1’s gene expression was analysed by the Real-Time Quantitative Reverse Transcription Polymerase Reaction (qRT-PCR), whereas functional analysis was carried out using the cell viability (liquid and spot) assays to determine its ability to confer stress tolerance to E. coli.
Nájar, Durán Elena. « Characterization of the maize protein ZmSTOP1 and its role in drought stress response ». Doctoral thesis, Universitat Autònoma de Barcelona, 2015. http://hdl.handle.net/10803/327875.
Texte intégralWater deficit has become a very important threat to agricultural yield worldwide. The identification of new players in drought stress response among crop plants is vital to understand their adaptation to increasing environmental challenges. Abscisic acid (ABA) is a plant hormone known to mediate drought adaptative responses such as seed dormancy, stomatal closure and root growth arrest. In the case of stomatal regulation, ABA drives the activation of OST1 kinase, which phosphorylates different substrates, for example NADPH oxidases, ionic channels and transcription factors, which will finally lead to stomatal closure. Although stomatal closure in response to ABA is essential to avoid desiccation, and thus, the death of the plant, a certain level of stomatal conductivity must be maintained to permit gas exchange and transpiration, essential to drive water and solutes uptake through the roots. We identified and characterized a new maize C2H2 zinc-finger putative transcription factor that presents homology to the Arabidopsis Sensitive to Proton Rhizotoxicity (STOP)1, which is critical for aluminum and proton tolerance in acidic soils. We determined that ZmSTOP1 is a well-conserved protein between plant species, especially in its four zinc-finger domains, which are characteristic of the STOP1-like proteins in plants. ZmSTOP1 is one of a five-members family of STOP1-like proteins in maize. It localizes in the nucleus, and has the ability to bind DNA, though no specific DNA targets were identified. In this work we show how ZmSTOP1 can complement AtSTOP1 phenotype in low pH conditions. Moreover, we detected that ZmSTOP1 overexpression promotes a differential response to ABA in roots and shoots. Root growth is over-inhibited whereas stomata present insensitivity to the ABA signal, remaining more open than the wild type after ABA treatment. Through microarray analyses we determine that the genes affected by ZmSTOP1 are classified mainly in signaling, regulation of transcription and stress. Its overexpression promotes changes in the expression pattern of several genes that are important for ionic homeostasis and signaling in cells, like the potassium channel KT2/3, the calcium transporter CAX7, the NADPH oxidase RBOHD, or the plasma membrane proton pump ATPase HA2, and it can induce ectopic expression of these genes in roots or shoots. The deregulation of these genes can affect the global behavior of the plant before drought stress conditions, as ABA effects depend deeply on ionic homeostasis, and could represent a possible explanation for the phenotypes observed. Additionally, we established that this protein is an interactor and a substrate of OST1 kinase. The phosphorylation by this kinase modulates ZmSTOP1 effect on stomatal regulation. In summary, by characterizing ZmSTOP1 protein we have shed light into the complex network regulating drought tolerance in a crucial plant for human and animal consumption like maize. These results can be important for focusing further genetic improvement of the plant, by either genetic engineering or classic breeding.
Livres sur le sujet "Stress response protein p66ShcA"
The unfolded protein response und cellular stress. Amsterdam [etc.] : Elsevier, 2011.
Trouver le texte intégralConn, P. Michael. The unfolded protein response and cellular stress. Amsterdam [etc.] : Elsevier, 2011.
Trouver le texte intégralConn, P. Michael. Methods in enzymology : The unfolded protein response and cellular stress. Amsterdam : Elsevier, 2011.
Trouver le texte intégralConn, P. Michael. Unfolded Protein Response and Cellular Stress, Part C. Elsevier Science & Technology Books, 2011.
Trouver le texte intégralConn, P. Michael. Unfolded Protein Response and Cellular Stress, Part B. Elsevier Science & Technology Books, 2011.
Trouver le texte intégralConn, P. Michael. Unfolded Protein Response and Cellular Stress, Part A. Elsevier Science & Technology Books, 2011.
Trouver le texte intégralThe Unfolded Protein Response and Cellular Stress, Part A. Elsevier, 2011. http://dx.doi.org/10.1016/c2010-0-66637-5.
Texte intégralThe Unfolded Protein Response and Cellular Stress, Part B. Elsevier, 2011. http://dx.doi.org/10.1016/c2010-0-66638-7.
Texte intégralThe Unfolded Protein Response and Cellular Stress, Part C. Elsevier, 2011. http://dx.doi.org/10.1016/c2010-0-66908-2.
Texte intégralCsermely, Peter, et László Vígh. Molecular Aspects of the Stress Response : Chaperones, Membranes and Networks. Springer London, Limited, 2007.
Trouver le texte intégralChapitres de livres sur le sujet "Stress response protein p66ShcA"
Liao, Nan, et Linda M. Hendershot. « Unfolded Protein Response : Contributions to Development and Disease ». Dans Cell Stress Proteins, 57–88. New York, NY : Springer New York, 2007. http://dx.doi.org/10.1007/978-0-387-39717-7_4.
Texte intégralNorberg, Åke, Felix Liebau et Jan Wernerman. « Protein Metabolism ». Dans The Stress Response of Critical Illness : Metabolic and Hormonal Aspects, 95–106. Cham : Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27687-8_9.
Texte intégralMohanta, Tapan Kumar, et Alok Krishna Sinha. « Role of Calcium-Dependent Protein Kinases during Abiotic Stress Tolerance ». Dans Abiotic Stress Response in Plants, 185–206. Weinheim, Germany : Wiley-VCH Verlag GmbH & Co. KGaA, 2016. http://dx.doi.org/10.1002/9783527694570.ch9.
Texte intégralLhomond, Stéphanie, et Eric Chevet. « Signaling the Unfolded Protein Response in cancer ». Dans Endoplasmic Reticulum Stress in Health and Disease, 357–82. Dordrecht : Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-4351-9_16.
Texte intégralDeka, Kamalakshi, et Sougata Saha. « Regulation of Mammalian HSP70 Expression and Stress Response ». Dans Regulation of Heat Shock Protein Responses, 3–25. Cham : Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-74715-6_1.
Texte intégralDamaris, Rebecca Njeri, et Pingfang Yang. « Protein Phosphorylation Response to Abiotic Stress in Plants ». Dans Plant Phosphoproteomics, 17–43. New York, NY : Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1625-3_2.
Texte intégralMukhopadhyay, Adhip, et Manoj Kumar. « Phage Shock Protein-Mediated Stress Response in Bacteria ». Dans ACS Symposium Series, 43–57. Washington, DC : American Chemical Society, 2023. http://dx.doi.org/10.1021/bk-2023-1434.ch003.
Texte intégralKumari, Supriya, et Nandula Raghuram. « Protein Phosphatases in N Response and NUE in Crops ». Dans Protein Phosphatases and Stress Management in Plants, 233–44. Cham : Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-48733-1_12.
Texte intégralGerlach, Jared Q., Shashank Sharma, Kirk J. Leister et Lokesh Joshi. « A Tight-Knit Group : Protein Glycosylation, Endoplasmic Reticulum Stress and the Unfolded Protein Response ». Dans Endoplasmic Reticulum Stress in Health and Disease, 23–39. Dordrecht : Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-4351-9_2.
Texte intégralBeckerman, Martin. « Chaperones, Endoplasmic Reticulum Stress, and the Unfolded Protein Response ». Dans Cellular Signaling in Health and Disease, 391–410. New York, NY : Springer US, 2009. http://dx.doi.org/10.1007/978-0-387-98173-4_18.
Texte intégralActes de conférences sur le sujet "Stress response protein p66ShcA"
Kryvenko, V., W. Seeger et I. Vadász. « Hypercapnia impairs protein translation by activating integrated stress response ». Dans Herbsttagung der Sektionen Zellbiologie und Infektiologie und Tuberkulose der Deutschen Gesellschaft für Pneumologie und Beatmungsmedizin e.V. Georg Thieme Verlag KG, 2018. http://dx.doi.org/10.1055/s-0037-1615334.
Texte intégralGewandter, JS, et MA O'Reilly. « Loss of the ER Stress Sensor Protein, BiP, in Hyperoxia Does Not Activate the Classic ER Stress Response. » Dans American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a4183.
Texte intégralBanerjee, Aditi, Elizabeth Duran, Javier Couto, Zhenbo Zhang, Lydia A. Espinoza, Marina Torres, Sushanta K. Banerjee, Krishna Baksi et Dipak K. Banerjee. « Abstract 2313 : ER stress-mediated unfolded protein response inhibits angiogenesis and breast tumor growth ». Dans Proceedings : AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012 ; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-2313.
Texte intégralKawahara, Kohichi, Takuto Kawahata, Fumito Horikuchi, Yohei Kamijo, Masatatsu Yamamoto, Yoshinari Shinsato, Kentaro Minami, Kazunari Arima, Toshiyuki Hamada et Tatsuhiko Furukawa. « Abstract 5420 : Ribosomal protein-p53-MDM2 signaling by nucleolar stress response and drug discovery ». Dans Proceedings : AACR 106th Annual Meeting 2015 ; April 18-22, 2015 ; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-5420.
Texte intégralHammond, Ester M. « Abstract IA-015 : Hypoxia-induced SETX links replication stress with the unfolded protein response ». Dans Abstracts : AACR Virtual Special Conference on Radiation Science and Medicine ; March 2-3, 2021. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1557-3265.radsci21-ia-015.
Texte intégralWang, Yugang, Yu Ning, Goleeta Alam, Fernanda Visioli, Jacques E. Nör et Peter J. Polverini. « Abstract 2081 : The unfolded protein response relieves stress in tumor cells by stimulating angiogenesis ». Dans Proceedings : AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011 ; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2081.
Texte intégralLiu, Xian-De, Soyoung Ko, Qian Xiang et Tony N. Eissa. « Alis Formation Is A Cytosolic Unfolded Protein Response To Inflammation And Endoplasmic Reticulum Stress ». Dans American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2127.
Texte intégralKemeny, Steven F., et Alisa Morss Clyne. « High Glucose Alters Endothelial Cell Response to Shear Stress ». Dans ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206531.
Texte intégralConn, Crystal S., Hao G. Nguyen, Yae Kye, John T. Cunningham, Charles Truillet, Michael Evans, Tony L. Huynh, Peter Walters et Davide Ruggero. « Abstract A25 : Sensing stress in cancer : a novel therapy targeting protein synthesis through the unfolded protein response in prostate cancer development ». Dans Abstracts : AACR Special Conference on Translational Control of Cancer : A New Frontier in Cancer Biology and Therapy ; October 27-30, 2016 ; San Francisco, CA. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.transcontrol16-a25.
Texte intégralCheung, Tracy M., et George A. Truskey. « Aging Endothelial Cells Exhibit Decreased Response to Atheroprotective Shear Stress ». Dans ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14402.
Texte intégralRapports d'organisations sur le sujet "Stress response protein p66ShcA"
Dyer, Scott D., Kenneth L. Dickson et Earl G. Zimmerman. Evaluation of the Efficacy of the Stress Protein Response as a Biochemical Water Quality Biomonitoring Method. Fort Belvoir, VA : Defense Technical Information Center, décembre 1990. http://dx.doi.org/10.21236/ada231966.
Texte intégralBray, Elizabeth, Zvi Lerner et Alexander Poljakoff-Mayber. The Role of Phytohormones in the Response of Plants to Salinity Stress. United States Department of Agriculture, septembre 1994. http://dx.doi.org/10.32747/1994.7613007.bard.
Texte intégralLocy, Robert D., Hillel Fromm, Joe H. Cherry et Narendra K. Singh. Regulation of Arabidopsis Glutamate Decarboxylase in Response to Heat Stress : Modulation of Enzyme Activity and Gene Expression. United States Department of Agriculture, janvier 2001. http://dx.doi.org/10.32747/2001.7575288.bard.
Texte intégralSela, Shlomo, et Michael McClelland. Investigation of a new mechanism of desiccation-stress tolerance in Salmonella. United States Department of Agriculture, janvier 2013. http://dx.doi.org/10.32747/2013.7598155.bard.
Texte intégralGuy, Charles, Gozal Ben-Hayyim, Gloria Moore, Doron Holland et Yuval Eshdat. Common Mechanisms of Response to the Stresses of High Salinity and Low Temperature and Genetic Mapping of Stress Tolerance Loci in Citrus. United States Department of Agriculture, mai 1995. http://dx.doi.org/10.32747/1995.7613013.bard.
Texte intégralBarash, Itamar, et Robert Rhoads. Translational Mechanisms Governing Milk Protein Levels and Composition. United States Department of Agriculture, 2006. http://dx.doi.org/10.32747/2006.7696526.bard.
Texte intégralHansen, Peter J., Zvi Roth et Jeremy J. Block. Improving oocyte competence in dairy cows exposed to heat stress. United States Department of Agriculture, janvier 2014. http://dx.doi.org/10.32747/2014.7598163.bard.
Texte intégralPorat, Ron, Gregory T. McCollum, Amnon Lers et Charles L. Guy. Identification and characterization of genes involved in the acquisition of chilling tolerance in citrus fruit. United States Department of Agriculture, décembre 2007. http://dx.doi.org/10.32747/2007.7587727.bard.
Texte intégralSela, Shlomo, et Michael McClelland. Desiccation Tolerance in Salmonella and its Implications. United States Department of Agriculture, mai 2013. http://dx.doi.org/10.32747/2013.7594389.bard.
Texte intégralBercovier, Herve, Raul Barletta et Shlomo Sela. Characterization and Immunogenicity of Mycobacterium paratuberculosis Secreted and Cellular Proteins. United States Department of Agriculture, janvier 1996. http://dx.doi.org/10.32747/1996.7573078.bard.
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