Статті в журналах з теми "Calpain system"
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GOLL, DARREL E., VALERY F. THOMPSON, HONGQI LI, WEI WEI, and JINYANG CONG. "The Calpain System." Physiological Reviews 83, no. 3 (July 2003): 731–801. http://dx.doi.org/10.1152/physrev.00029.2002.
Повний текст джерелаTheopold, U., M. Pintér, S. Daffre, Y. Tryselius, P. Friedrich, D. R. Nässel, and D. Hultmark. "CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells." Molecular and Cellular Biology 15, no. 2 (February 1995): 824–34. http://dx.doi.org/10.1128/mcb.15.2.824.
Повний текст джерелаFontenele, Marcio, Bomyi Lim, Danielle Oliveira, Márcio Buffolo, David H. Perlman, Trudi Schupbach та Helena Araujo. "Calpain A modulates Toll responses by limited Cactus/IκB proteolysis". Molecular Biology of the Cell 24, № 18 (15 вересня 2013): 2966–80. http://dx.doi.org/10.1091/mbc.e13-02-0113.
Повний текст джерелаGoll, Darrel E., Valery F. Thompson, Richard G. Taylor, and Ahmed Ouali. "The calpain system and skeletal muscle growth." Canadian Journal of Animal Science 78, no. 4 (December 1, 1998): 503–12. http://dx.doi.org/10.4141/a98-081.
Повний текст джерелаIlian, M. A., and N. E. Forsberg. "Gene expression of calpains and their specific endogenous inhibitor, calpastatin, in skeletal muscle of fed and fasted rabbits." Biochemical Journal 287, no. 1 (October 1, 1992): 163–71. http://dx.doi.org/10.1042/bj2870163.
Повний текст джерелаPánico, Pablo, Marcia Hiriart, Patricia Ostrosky-Wegman, and Ana María Salazar. "TUG is a calpain-10 substrate involved in the translocation of GLUT4 in adipocytes." Journal of Molecular Endocrinology 65, no. 3 (October 2020): 45–57. http://dx.doi.org/10.1530/jme-19-0253.
Повний текст джерелаMiller, John A., Domenica E. Drouet, Leonid M. Yermakov, Mahmoud S. Elbasiouny, Fatima Z. Bensabeur, Michael Bottomley, and Keiichiro Susuki. "Distinct Changes in Calpain and Calpastatin during PNS Myelination and Demyelination in Rodent Models." International Journal of Molecular Sciences 23, no. 23 (December 6, 2022): 15443. http://dx.doi.org/10.3390/ijms232315443.
Повний текст джерелаWeber, Jonasz J., Eva Haas, Yacine Maringer, Stefan Hauser, Nicolas L. P. Casadei, Athar H. Chishti, Olaf Riess, and Jeannette Hübener-Schmid. "Calpain-1 ablation partially rescues disease-associated hallmarks in models of Machado-Joseph disease." Human Molecular Genetics 29, no. 6 (January 21, 2020): 892–906. http://dx.doi.org/10.1093/hmg/ddaa010.
Повний текст джерелаMellgren, Ronald L., and Xinhua Huang. "Fetuin A Stabilizes m-Calpain and Facilitates Plasma Membrane Repair." Journal of Biological Chemistry 282, no. 49 (October 17, 2007): 35868–77. http://dx.doi.org/10.1074/jbc.m706929200.
Повний текст джерелаBevers, Matthew B., and Robert W. Neumar. "Mechanistic Role of Calpains in Postischemic Neurodegeneration." Journal of Cerebral Blood Flow & Metabolism 28, no. 4 (December 12, 2007): 655–73. http://dx.doi.org/10.1038/sj.jcbfm.9600595.
Повний текст джерелаCoria, María Sumampa, Dario Pighin, Gabriela Grigioni, and Gustavo Adolfo Palma. "Feeding strategies and ageing time alter calpain system proteins activities and meat quality of Braford steers." Animal Bioscience 35, no. 2 (February 1, 2022): 272–80. http://dx.doi.org/10.5713/ab.21.0227.
Повний текст джерелаBaudry, Michel. "Calpain-1 and Calpain-2 in the Brain: Dr. Jekill and Mr Hyde?" Current Neuropharmacology 17, no. 9 (August 22, 2019): 823–29. http://dx.doi.org/10.2174/1570159x17666190228112451.
Повний текст джерелаPintér, M., and P. Friedrich. "The calcium-dependent proteolytic system calpain-calpastatin in Drosophila melanogaster." Biochemical Journal 253, no. 2 (July 15, 1988): 467–73. http://dx.doi.org/10.1042/bj2530467.
Повний текст джерелаKuchay, Shafi, Rafael Nunez, Amelia M. Bartholomew, and Athar H. Chishti. "Calpain I Null Mice Display Lymphoid Hyperplasia." Blood 104, no. 11 (November 16, 2004): 1268. http://dx.doi.org/10.1182/blood.v104.11.1268.1268.
Повний текст джерелаEnnes-Vidal, Vítor, Marta Helena Branquinha, André Luis Souza dos Santos, and Claudia Masini d’Avila-Levy. "The Diverse Calpain Family in Trypanosomatidae: Functional Proteins Devoid of Proteolytic Activity?" Cells 10, no. 2 (February 1, 2021): 299. http://dx.doi.org/10.3390/cells10020299.
Повний текст джерелаKalbe, L., A. Leunda, T. Sparre, C. Meulemans, M. T. Ahn, T. Orntoft, M. Kruhoffer, B. Reusens, J. Nerup, and C. Remacle. "Nutritional regulation of proteases involved in fetal rat insulin secretion and islet cell proliferation." British Journal of Nutrition 93, no. 3 (March 2005): 309–16. http://dx.doi.org/10.1079/bjn20041313.
Повний текст джерелаMacqueen, Daniel J., and Alexander H. Wilcox. "Characterization of the definitive classical calpain family of vertebrates using phylogenetic, evolutionary and expression analyses." Open Biology 4, no. 4 (April 2014): 130219. http://dx.doi.org/10.1098/rsob.130219.
Повний текст джерелаKemp, C. M., T. Parr, R. G. Bardsley, and P. J. Buttery. "Comparison of the relative expression of caspase isoforms across muscle types." Proceedings of the British Society of Animal Science 2005 (2005): 107. http://dx.doi.org/10.1017/s1752756200010188.
Повний текст джерелаHata, Shoji, Naoko Doi, Fujiko Kitamura, and Hiroyuki Sorimachi. "Stomach-specific Calpain, nCL-2/Calpain 8, Is Active without Calpain Regulatory Subunit and Oligomerizes through C2-like Domains." Journal of Biological Chemistry 282, no. 38 (July 23, 2007): 27847–56. http://dx.doi.org/10.1074/jbc.m703168200.
Повний текст джерелаYamaura, Ikuya, Eiichi Tani, Takaomi C. Saido, Koichi Suzuki, Nobutaka Minami, and Yukio Maeda. "Calpain-calpastatin system of canine basilar artery in vasospasm." Journal of Neurosurgery 79, no. 4 (October 1993): 537–43. http://dx.doi.org/10.3171/jns.1993.79.4.0537.
Повний текст джерелаAlexa, Anita, Zoltán Bozóky, Attila Farkas, Peter Tompa, and Peter Friedrich. "Contribution of Distinct Structural Elements to Activation of Calpain by Ca2+Ions." Journal of Biological Chemistry 279, no. 19 (February 19, 2004): 20118–26. http://dx.doi.org/10.1074/jbc.m311969200.
Повний текст джерелаYajima, Yukiko, Mayumi Sato, Hiroyuki Sorimachi, Mitsushi Inomata, Masatoshi Maki, and Seiichi Kawashima. "Calpain System Regulates the Differentiation of Adult Primitive Mesenchymal ST-13 Adipocytes." Endocrinology 147, no. 10 (October 1, 2006): 4811–19. http://dx.doi.org/10.1210/en.2005-1647.
Повний текст джерелаYeh, J.-Y., B.-R. Ou, and N. E. Forsberg. "Effects of dexamethasone on muscle protein homeostasis and on calpain and calpastatin activities and gene expression in rabbits." Journal of Endocrinology 141, no. 2 (May 1994): 209–17. http://dx.doi.org/10.1677/joe.0.1410209.
Повний текст джерелаMiyazaki, Takuro, and Akira Miyazaki. "Impact of Dysfunctional Protein Catabolism on Macrophage Cholesterol Handling." Current Medicinal Chemistry 26, no. 9 (May 21, 2019): 1631–43. http://dx.doi.org/10.2174/0929867325666180326165234.
Повний текст джерелаSensky, P. L., T. Parr, S. N. Brown, R. G. Bardsley, P. J. Buttery, and J. D. Wood. "Relationship between pigmeat toughness and the calpain proteolytic system." Proceedings of the British Society of Animal Science 1996 (March 1996): 156. http://dx.doi.org/10.1017/s1752756200593521.
Повний текст джерелаSensky, P. L., T. Parr, S. N. Brown, R. G. Bardsley, P. J. Buttery, and J. D. Wood. "Relationship between pigmeat toughness and the calpain proteolytic system." Proceedings of the British Society of Animal Science 1996 (March 1996): 156. http://dx.doi.org/10.1017/s0308229600031238.
Повний текст джерелаWeber, Heike, Ludwig Jonas, Saskia Hühns, and Peter Schuff-Werner. "Dysregulation of the calpain-calpastatin system plays a role in the development of cerulein-induced acute pancreatitis in the rat." American Journal of Physiology-Gastrointestinal and Liver Physiology 286, no. 6 (June 2004): G932—G941. http://dx.doi.org/10.1152/ajpgi.00406.2003.
Повний текст джерелаHaim, K., I. Ben-Aharon, and R. Shalgi. "Expression and immunolocalization of the calpain–calpastatin system during parthenogenetic activation and fertilization in the rat egg." Reproduction 131, no. 1 (January 2006): 35–43. http://dx.doi.org/10.1530/rep.1.00697.
Повний текст джерелаOno, Yasuko, Kazumi Kakinuma, Fukuyo Torii, Akihiro Irie, Kazuhiro Nakagawa, Siegfried Labeit, Keiko Abe, Koichi Suzuki, and Hiroyuki Sorimachi. "Possible Regulation of the Conventional Calpain System by Skeletal Muscle-specific Calpain, p94/Calpain 3." Journal of Biological Chemistry 279, no. 4 (November 1, 2003): 2761–71. http://dx.doi.org/10.1074/jbc.m308789200.
Повний текст джерелаPandurangan, Muthuraman, Inho Hwang, Chinzorio Orhirbat, Yang Jieun, and Soo-Hyun Cho. "The calpain system and diabetes." Pathophysiology 21, no. 2 (June 2014): 161–67. http://dx.doi.org/10.1016/j.pathophys.2014.01.003.
Повний текст джерелаStorr, Sarah J., Neil O. Carragher, Margaret C. Frame, Tim Parr, and Stewart G. Martin. "The calpain system and cancer." Nature Reviews Cancer 11, no. 5 (April 21, 2011): 364–74. http://dx.doi.org/10.1038/nrc3050.
Повний текст джерелаKar, Pulak, Krishna Samanta, Soni Shaikh, Animesh Chowdhury, Tapati Chakraborti, and Sajal Chakraborti. "Mitochondrial calpain system: An overview." Archives of Biochemistry and Biophysics 495, no. 1 (March 2010): 1–7. http://dx.doi.org/10.1016/j.abb.2009.12.020.
Повний текст джерелаHopkins, D. L., and J. M. Thompson. "Factors contributing to proteolysis and disruption of myofibrillar proteins and the impact on tenderisation in beef and sheep meat." Australian Journal of Agricultural Research 53, no. 2 (2002): 149. http://dx.doi.org/10.1071/ar01079.
Повний текст джерелаYang, Jie, Fei Xiang, Peng-Cheng Cai, Yu-Zhi Lu, Xiao-Xiao Xu, Fan Yu, Feng-Zhi Li, et al. "Activation of calpain by renin-angiotensin system in pleural mesothelial cells mediates tuberculous pleural fibrosis." American Journal of Physiology-Lung Cellular and Molecular Physiology 311, no. 1 (July 1, 2016): L145—L153. http://dx.doi.org/10.1152/ajplung.00348.2015.
Повний текст джерелаSchneider, Martha, Kerstin Ackermann, Melissa Stuart, Claudia Wex, Ulrike Protzer, Hermann M. Schätzl, and Sabine Gilch. "Severe Acute Respiratory Syndrome Coronavirus Replication Is Severely Impaired by MG132 due to Proteasome-Independent Inhibition of M-Calpain." Journal of Virology 86, no. 18 (July 11, 2012): 10112–22. http://dx.doi.org/10.1128/jvi.01001-12.
Повний текст джерелаBenetti, Roberta, Tamara Copetti, Stefania Dell'Orso, Edon Melloni, Claudio Brancolini, Martin Monte та Claudio Schneider. "The Calpain System Is Involved in the Constitutive Regulation of β-Catenin Signaling Functions". Journal of Biological Chemistry 280, № 23 (7 квітня 2005): 22070–80. http://dx.doi.org/10.1074/jbc.m501810200.
Повний текст джерелаMEYER, Sheryl L., Donna BOZYCZKO-COYNE, Satish K. MALLYA, Chrysanthe M. SPAIS, Ron BIHOVSKY, John K. KAWOOYA, Diane M. LANG, Richard W. SCOTT, and Robert SIMAN. "Biologically active monomeric and heterodimeric recombinant human calpain I produced using the baculovirus expression system." Biochemical Journal 314, no. 2 (March 1, 1996): 511–19. http://dx.doi.org/10.1042/bj3140511.
Повний текст джерелаCunha, Telma F., Jose B. N. Moreira, Nathalie A. Paixão, Juliane C. Campos, Alex W. A. Monteiro, Aline V. N. Bacurau, Carlos R. Bueno, Julio C. B. Ferreira, and Patricia C. Brum. "Aerobic exercise training upregulates skeletal muscle calpain and ubiquitin-proteasome systems in healthy mice." Journal of Applied Physiology 112, no. 11 (June 1, 2012): 1839–46. http://dx.doi.org/10.1152/japplphysiol.00346.2011.
Повний текст джерелаZaman, Vandana, Kelsey P. Drasites, Ali Myatich, Ramsha Shams, Donald C. Shields, Denise Matzelle, Azizul Haque, and Narendra L. Banik. "Inhibition of Calpain Attenuates Degeneration of Substantia Nigra Neurons in the Rotenone Rat Model of Parkinson’s Disease." International Journal of Molecular Sciences 23, no. 22 (November 10, 2022): 13849. http://dx.doi.org/10.3390/ijms232213849.
Повний текст джерелаNian, Hong, and Binyun Ma. "Calpain–calpastatin system and cancer progression." Biological Reviews 96, no. 3 (January 20, 2021): 961–75. http://dx.doi.org/10.1111/brv.12686.
Повний текст джерелаThompson, Valery F., Sandra Saldaña, Jinyang Cong, Dennis M. Luedke, and Darrel E. Goll. "The calpain system in human placenta." Life Sciences 70, no. 21 (April 2002): 2493–508. http://dx.doi.org/10.1016/s0024-3205(02)01506-0.
Повний текст джерелаSultan, Karim R., Bernd T. Dittrich, Elmi Leisner, Nina Paul, and Dirk Pette. "Fiber type-specific expression of major proteolytic systems in fast- to slow-transforming rabbit muscle." American Journal of Physiology-Cell Physiology 280, no. 2 (February 1, 2001): C239—C247. http://dx.doi.org/10.1152/ajpcell.2001.280.2.c239.
Повний текст джерелаCarragher, N. O., M. A. Westhoff, D. Riley, D. A. Potter, P. Dutt, J. S. Elce, P. A. Greer, and M. C. Frame. "v-Src-Induced Modulation of the Calpain-Calpastatin Proteolytic System Regulates Transformation." Molecular and Cellular Biology 22, no. 1 (January 1, 2002): 257–69. http://dx.doi.org/10.1128/mcb.22.1.257-269.2002.
Повний текст джерелаSmith, Ira J., Stewart H. Lecker, and Per-Olof Hasselgren. "Calpain activity and muscle wasting in sepsis." American Journal of Physiology-Endocrinology and Metabolism 295, no. 4 (October 2008): E762—E771. http://dx.doi.org/10.1152/ajpendo.90226.2008.
Повний текст джерелаFareed, Moin U., Amy R. Evenson, Wei Wei, Michael Menconi, Vitaliy Poylin, Victoria Petkova, Bernadette Pignol, and Per-Olof Hasselgren. "Treatment of rats with calpain inhibitors prevents sepsis-induced muscle proteolysis independent of atrogin-1/MAFbx and MuRF1 expression." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 290, no. 6 (June 2006): R1589—R1597. http://dx.doi.org/10.1152/ajpregu.00668.2005.
Повний текст джерелаAnagli, J., J. Hagmann, and E. Shaw. "Investigation of the role of calpain as a stimulus-response mediator in human platelets using new synthetic inhibitors." Biochemical Journal 274, no. 2 (March 1, 1991): 497–502. http://dx.doi.org/10.1042/bj2740497.
Повний текст джерелаMa, Xiufeng, Hui Chang, Zhe Wang, Shenhui Xu, Xin Peng, Jie Zhang, Xia Yan, Tingyun Lei, Huiping Wang, and Yunfang Gao. "Differential activation of the calpain system involved in individualized adaptation of different fast-twitch muscles in hibernating Daurian ground squirrels." Journal of Applied Physiology 127, no. 2 (August 1, 2019): 328–41. http://dx.doi.org/10.1152/japplphysiol.00124.2019.
Повний текст джерелаWeber, Jonasz Jeremiasz, Priscila Pereira Sena, Elisabeth Singer, and Huu Phuc Nguyen. "Killing Two Angry Birds with One Stone: Autophagy Activation by Inhibiting Calpains in Neurodegenerative Diseases and Beyond." BioMed Research International 2019 (February 14, 2019): 1–13. http://dx.doi.org/10.1155/2019/4741252.
Повний текст джерелаCoria, María Sumampa, Pablo Sebastián Reineri, Dario Pighin, Maria Guadalupe Barrionuevo, Pedro Gabriel Carranza, Gabriela Grigioni, and Gustavo Adolfo Palma. "Feeding strategies alter gene expression of the calpain system and meat quality in the longissimus muscle of Braford steers." Asian-Australasian Journal of Animal Sciences 33, no. 5 (May 1, 2020): 753–62. http://dx.doi.org/10.5713/ajas.19.0163.
Повний текст джерелаTalbert, Erin E., Ashley J. Smuder, Kisuk Min, Oh Sung Kwon, and Scott K. Powers. "Calpain and caspase-3 play required roles in immobilization-induced limb muscle atrophy." Journal of Applied Physiology 114, no. 10 (May 15, 2013): 1482–89. http://dx.doi.org/10.1152/japplphysiol.00925.2012.
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