Статті в журналах з теми "Stress response protein p66ShcA"
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Hu, Yuanyu, Xueying Wang, Li Zeng, De-Yu Cai, Kanaga Sabapathy, Stephen P. Goff, Eduardo J. Firpo, and 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 (August 2005): 3705–18. http://dx.doi.org/10.1091/mbc.e05-04-0301.
Повний текст джерелаHusain, 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 (April 21, 2009): 16648–58. http://dx.doi.org/10.1074/jbc.m109.008482.
Повний текст джерелаCanedo, Eduardo Cepeda, Sonia Del Rincon, Peter Siegel, Michael Witcher, and Josie Ursini-Siegel. "Abstract 131: The role of p66ShcA in the melanoma oncogenesis process." Cancer Research 82, no. 12_Supplement (June 15, 2022): 131. http://dx.doi.org/10.1158/1538-7445.am2022-131.
Повний текст джерелаMalhotra, Ashwani, Himanshu Vashistha, Virendra S. Yadav, Michael G. Dube, Satya P. Kalra, Maha Abdellatif, and 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 (February 2009): H380—H388. http://dx.doi.org/10.1152/ajpheart.00225.2008.
Повний текст джерелаVashistha, 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 (December 1, 2018): F1833—F1842. http://dx.doi.org/10.1152/ajprenal.00608.2017.
Повний текст джерелаMiyazawa, Masaki, and 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 (July 2014): 2116–27. http://dx.doi.org/10.1091/mbc.e13-11-0666.
Повний текст джерелаBetts, Dean H., Nathan T. Bain, and Pavneesh Madan. "The p66Shc Adaptor Protein Controls Oxidative Stress Response in Early Bovine Embryos." PLoS ONE 9, no. 1 (January 24, 2014): e86978. http://dx.doi.org/10.1371/journal.pone.0086978.
Повний текст джерелаPacini, 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 (February 15, 2004): 1747–57. http://dx.doi.org/10.1128/mcb.24.4.1747-1757.2004.
Повний текст джерелаMigliaccio, Enrica, Marco Giorgio, Simonetta Mele, Giuliana Pelicci, Paolo Reboldi, Pier Paolo Pandolfi, Luisa Lanfrancone, and Pier Giuseppe Pelicci. "The p66shc adaptor protein controls oxidative stress response and life span in mammals." Nature 402, no. 6759 (November 1999): 309–13. http://dx.doi.org/10.1038/46311.
Повний текст джерелаSun, 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 (November 2010): F1014—F1025. http://dx.doi.org/10.1152/ajprenal.00414.2010.
Повний текст джерелаRen, Chaoxing, Xiaowei Zhou, Xiaowen Bao, Jie Zhang, Jun Tang, Zhiming Zhu, Nan Zhang, et al. "Dioscorea zingiberensis ameliorates diabetic nephropathy by inhibiting NLRP3 inflammasome and curbing the expression of p66Shc in high-fat diet/streptozotocin-induced diabetic mice." Journal of Pharmacy and Pharmacology 73, no. 9 (June 1, 2021): 1218–29. http://dx.doi.org/10.1093/jpp/rgab053.
Повний текст джерелаChintapalli, Janaki, Shuo Yang, David Opawumi, Sunita Ray Goyal, Nazia Shamsuddin, Ashwani Malhotra, Krzysztof Reiss, and Leonard G. Meggs. "Inhibition of wild-type p66ShcA in mesangial cells prevents glycooxidant-dependent FOXO3a regulation and promotes the survival phenotype." American Journal of Physiology-Renal Physiology 292, no. 2 (February 2007): F523—F530. http://dx.doi.org/10.1152/ajprenal.00215.2006.
Повний текст джерелаSalhan, Divya, Shresh Pathak, Mohammad Husain, Pranai Tandon, Dileep Kumar, Ashwani Malhotra, Leonard G. Meggs, and Pravin C. Singhal. "HIV gene expression deactivates redox-sensitive stress response program in mouse tubular cells both in vitro and in vivo." American Journal of Physiology-Renal Physiology 302, no. 1 (January 1, 2012): F129—F140. http://dx.doi.org/10.1152/ajprenal.00024.2011.
Повний текст джерелаDi Stefano, Valeria, Chiara Cencioni, Germana Zaccagnini, Alessandra Magenta, Maurizio C. Capogrossi, and Fabio Martelli. "p66ShcA modulates oxidative stress and survival of endothelial progenitor cells in response to high glucose." Cardiovascular Research 82, no. 3 (March 4, 2009): 421–29. http://dx.doi.org/10.1093/cvr/cvp082.
Повний текст джерелаRattanavich, Rungwasee, Andrei Plagov, Dileep Kumar, Partab Rai, Rivka Lederman, Divya Salhan, Himanshu Vashistha, Ashwani Malhotra, Leonard G. Meggs, and Pravin C. Singhal. "Deficit of p66ShcA restores redox-sensitive stress response program in cisplatin-induced acute kidney injury." Experimental and Molecular Pathology 94, no. 3 (June 2013): 445–52. http://dx.doi.org/10.1016/j.yexmp.2013.03.001.
Повний текст джерелаRai, Partab, Andrei Plagov, Xiqian Lan, Nirupama Chandel, Tejinder Singh, Rivka Lederman, Kamesh R. Ayasolla, et al. "mTOR plays a critical role in p53-induced oxidative kidney cell injury in HIVAN." American Journal of Physiology-Renal Physiology 305, no. 3 (August 1, 2013): F343—F354. http://dx.doi.org/10.1152/ajprenal.00135.2013.
Повний текст джерелаYoshida, Hiderou. "ER stress response, peroxisome proliferation, mitochondrial unfolded protein response and Golgi stress response." IUBMB Life 61, no. 9 (September 2009): 871–79. http://dx.doi.org/10.1002/iub.229.
Повний текст джерелаFlick, Karin, and Peter Kaiser. "Protein degradation and the stress response." Seminars in Cell & Developmental Biology 23, no. 5 (July 2012): 515–22. http://dx.doi.org/10.1016/j.semcdb.2012.01.019.
Повний текст джерелаLittle, Tom J., Lenny Nelson, and Ted Hupp. "Adaptive Evolution of a Stress Response Protein." PLoS ONE 2, no. 10 (October 10, 2007): e1003. http://dx.doi.org/10.1371/journal.pone.0001003.
Повний текст джерелаSchröder, Martin, and Randal J. Kaufman. "ER stress and the unfolded protein response." Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis 569, no. 1-2 (January 2005): 29–63. http://dx.doi.org/10.1016/j.mrfmmm.2004.06.056.
Повний текст джерелаDietrich, C. J., I. S. Richards, T. E. Bernard, and Y. Y. Hammad. "Human stress protein response to formaldehyde exposure." Experimental and Toxicologic Pathology 48, no. 6 (November 1996): 518–19. http://dx.doi.org/10.1016/s0940-2993(96)80071-6.
Повний текст джерелаSheppard, Terry L. "Unfolded protein response: Letting go of stress." Nature Chemical Biology 10, no. 11 (October 17, 2014): 877. http://dx.doi.org/10.1038/nchembio.1676.
Повний текст джерелаSolé, M., Y. Morcillo, and C. Porte. "StressProtein Response in Tributyltin-Exposed Clams." Bulletin of Environmental Contamination and Toxicology 64, no. 6 (June 30, 2000): 852–58. http://dx.doi.org/10.1007/s001280000081.
Повний текст джерелаSolé, M., Y. Morcillo, and C. Porte. "Stress–Protein Response in Tributyltin-Exposed Clams." Bulletin of Environmental Contamination and Toxicology 64, no. 6 (June 2000): 852–58. http://dx.doi.org/10.1007/s0012800081.
Повний текст джерелаZhang, Guangyu, Xiaoding Wang, Chao Li, Qinfeng Li, Yu A. An, Xiang Luo, Yingfeng Deng, Thomas G. Gillette, Philipp E. Scherer, and Zhao V. Wang. "Integrated Stress Response Couples Mitochondrial Protein Translation With Oxidative Stress Control." Circulation 144, no. 18 (November 2, 2021): 1500–1515. http://dx.doi.org/10.1161/circulationaha.120.053125.
Повний текст джерелаGower, David J., Carol Hollman, K. Stuart Lee, and Michael Tytell. "Spinal cord injury and the stress protein response." Journal of Neurosurgery 70, no. 4 (April 1989): 605–11. http://dx.doi.org/10.3171/jns.1989.70.4.0605.
Повний текст джерелаMoore, J., R. Flynn, R. C. Dwyer, and E. Duly. "Stress protein response and analgesic treatment during labour." Journal of Obstetrics and Gynaecology 11, no. 6 (January 1991): 414–16. http://dx.doi.org/10.3109/01443619109013580.
Повний текст джерелаGötz, Claudia, and Mathias Montenarh. "Protein kinase CK2 in the ER stress response." Advances in Biological Chemistry 03, no. 03 (2013): 1–5. http://dx.doi.org/10.4236/abc.2013.33a001.
Повний текст джерелаLai, Elida, Tracy Teodoro, and Allen Volchuk. "Endoplasmic Reticulum Stress: Signaling the Unfolded Protein Response." Physiology 22, no. 3 (June 2007): 193–201. http://dx.doi.org/10.1152/physiol.00050.2006.
Повний текст джерелаShao, Chunhong, Qunye Zhang, Yundong Sun, Zhifang Liu, Jiping Zeng, Yabin Zhou, Xiuping Yu, and Jihui Jia. "Helicobacter pylori protein response to human bile stress." Journal of Medical Microbiology 57, no. 2 (February 1, 2008): 151–58. http://dx.doi.org/10.1099/jmm.0.47616-0.
Повний текст джерелаOfenstein, John P., Sabrina M. Heidemann, Amy M. Juett, and Ashok P. Sarnaik. "ENDOTOXEMIA INDUCES THE STRESS RESPONSE PROTEIN HSP70. † 210." Pediatric Research 41 (April 1997): 37. http://dx.doi.org/10.1203/00006450-199704001-00230.
Повний текст джерелаKapoor, Ashwani, and Arun J. Sanyal. "Endoplasmic Reticulum Stress and the Unfolded Protein Response." Clinics in Liver Disease 13, no. 4 (November 2009): 581–90. http://dx.doi.org/10.1016/j.cld.2009.07.004.
Повний текст джерелаThede, G. L., D. C. Arthur, R. A. Edwards, D. R. Buelow, J. L. Wong, T. L. Raivio, and J. N. M. Glover. "Structure of the Periplasmic Stress Response Protein CpxP." Journal of Bacteriology 193, no. 9 (February 11, 2011): 2149–57. http://dx.doi.org/10.1128/jb.01296-10.
Повний текст джерелаAbbondanzieri, Elio A., Natalia Vtyurina, and Anne Meyer. "Nucleoid Reorganization by the Stress Response Protein Dps." Biophysical Journal 106, no. 2 (January 2014): 79a. http://dx.doi.org/10.1016/j.bpj.2013.11.511.
Повний текст джерелаUckelmann, Hannah, Sandra Blaszkiewicz, and Marieke Essers. "Extracellular matrix protein Matn4 regulates HSC stress response." Experimental Hematology 43, no. 9 (September 2015): S45. http://dx.doi.org/10.1016/j.exphem.2015.06.051.
Повний текст джерелаWong, H. R., and J. R. Wispe. "The stress response and the lung." American Journal of Physiology-Lung Cellular and Molecular Physiology 273, no. 1 (July 1, 1997): L1—L9. http://dx.doi.org/10.1152/ajplung.1997.273.1.l1.
Повний текст джерелаJiang, Mengxi, Susan M. Sullivan, Patrice K. Wout, and Janine R. Maddock. "G-Protein Control of the Ribosome-Associated Stress Response Protein SpoT." Journal of Bacteriology 189, no. 17 (July 6, 2007): 6140–47. http://dx.doi.org/10.1128/jb.00315-07.
Повний текст джерелаJohnston, Benjamin P., and Craig McCormick. "Herpesviruses and the Unfolded Protein Response." Viruses 12, no. 1 (December 21, 2019): 17. http://dx.doi.org/10.3390/v12010017.
Повний текст джерелаAdachi, Masaaki, Yaohua Liu, Kyoko Fujii, Stuart K. Calderwood, Akira Nakai, Kohzoh Imai, and Yasuhisa Shinomura. "Oxidative Stress Impairs the Heat Stress Response and Delays Unfolded Protein Recovery." PLoS ONE 4, no. 11 (November 11, 2009): e7719. http://dx.doi.org/10.1371/journal.pone.0007719.
Повний текст джерелаHetz, Claudio, Fabio Martinon, Diego Rodriguez та Laurie H. Glimcher. "The Unfolded Protein Response: Integrating Stress Signals Through the Stress Sensor IRE1α". Physiological Reviews 91, № 4 (жовтень 2011): 1219–43. http://dx.doi.org/10.1152/physrev.00001.2011.
Повний текст джерелаLee, Jaemin, and Umut Ozcan. "Unfolded Protein Response Signaling and Metabolic Diseases." Journal of Biological Chemistry 289, no. 3 (December 9, 2013): 1203–11. http://dx.doi.org/10.1074/jbc.r113.534743.
Повний текст джерелаRzymski, Tomasz, and Adrian L. Harris. "The Unfolded Protein Response and Integrated Stress Response to Anoxia: Fig. 1." Clinical Cancer Research 13, no. 9 (May 1, 2007): 2537–40. http://dx.doi.org/10.1158/1078-0432.ccr-06-2126.
Повний текст джерелаWang, Yijie, and Jose Ramón Botella. "Heterotrimeric G Protein Signaling in Abiotic Stress." Plants 11, no. 7 (March 25, 2022): 876. http://dx.doi.org/10.3390/plants11070876.
Повний текст джерелаXu, Delin, Bo Yu, Yan Zhang, Miao Cui, and Qizhong Zhang. "Metallothionein Protein Expression ofCrassostrea hongkongensisin Response to Cadmium Stress." Journal of Shellfish Research 34, no. 2 (August 2015): 311–18. http://dx.doi.org/10.2983/035.034.0213.
Повний текст джерелаSmirnova, E. V., T. V. Rakitina, O. V. Bogatova, D. L. Ivanova, E. E. Vorobyeva, A. V. Lipkin, I. A. Kostanyan, and V. M. Lipkin. "Novel protein haponin regulates cellular response to oxidative stress." Doklady Biochemistry and Biophysics 440, no. 1 (October 2011): 225–27. http://dx.doi.org/10.1134/s1607672911050097.
Повний текст джерелаOosthuizen, I. B., H. A. Snyman, and J. C. Pretorius. "Protein concentration in response to water stress inThemeda triandraForsk." South African Journal of Plant and Soil 23, no. 1 (January 2006): 43–48. http://dx.doi.org/10.1080/02571862.2006.10634728.
Повний текст джерелаRoy, Anirban, and Ashok Kumar. "ER Stress and Unfolded Protein Response in Cancer Cachexia." Cancers 11, no. 12 (December 3, 2019): 1929. http://dx.doi.org/10.3390/cancers11121929.
Повний текст джерелаGardner, B. M., D. Pincus, K. Gotthardt, C. M. Gallagher, and P. Walter. "Endoplasmic Reticulum Stress Sensing in the Unfolded Protein Response." Cold Spring Harbor Perspectives in Biology 5, no. 3 (February 6, 2013): a013169. http://dx.doi.org/10.1101/cshperspect.a013169.
Повний текст джерелаBalodimos, I. A., E. Rapaport, and E. R. Kashket. "Protein phosphorylation in response to stress in Clostridium acetobutylicum." Applied and Environmental Microbiology 56, no. 7 (1990): 2170–73. http://dx.doi.org/10.1128/aem.56.7.2170-2173.1990.
Повний текст джерелаHetz, Claudio, and Smita Saxena. "ER stress and the unfolded protein response in neurodegeneration." Nature Reviews Neurology 13, no. 8 (July 21, 2017): 477–91. http://dx.doi.org/10.1038/nrneurol.2017.99.
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