Artykuły w czasopismach na temat „Calpain 2”
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Upla, Paula, Varpu Marjomäki, Liisa Nissinen, Camilla Nylund, Matti Waris, Timo Hyypiä i Jyrki Heino. "Calpain 1 and 2 Are Required for RNA Replication of Echovirus 1". Journal of Virology 82, nr 3 (21.11.2007): 1581–90. http://dx.doi.org/10.1128/jvi.01375-07.
Pełny tekst źródłaWang, Yubin, Yan Liu, Xiaoning Bi i Michel Baudry. "Calpain-1 and Calpain-2 in the Brain: New Evidence for a Critical Role of Calpain-2 in Neuronal Death". Cells 9, nr 12 (16.12.2020): 2698. http://dx.doi.org/10.3390/cells9122698.
Pełny tekst źródłaBen-Aharon, Irit, Paula R. Brown, Nir Etkovitz, Edward M. Eddy i Ruth Shalgi. "The expression of calpain 1 and calpain 2 in spermatogenic cells and spermatozoa of the mouse". Reproduction 129, nr 4 (kwiecień 2005): 435–42. http://dx.doi.org/10.1530/rep.1.00255.
Pełny tekst źródłaBaudry, Michel. "Calpain-1 and Calpain-2 in the Brain: Dr. Jekill and Mr Hyde?" Current Neuropharmacology 17, nr 9 (22.08.2019): 823–29. http://dx.doi.org/10.2174/1570159x17666190228112451.
Pełny tekst źródłaMcCartney, Christian-Scott E., Qilu Ye, Robert L. Campbell i Peter L. Davies. "Insertion sequence 1 from calpain-3 is functional in calpain-2 as an internal propeptide". Journal of Biological Chemistry 293, nr 46 (25.09.2018): 17716–30. http://dx.doi.org/10.1074/jbc.ra118.004803.
Pełny tekst źródłaCovington, Marisa D., David D. Arrington i Rick G. Schnellmann. "Calpain 10 is required for cell viability and is decreased in the aging kidney". American Journal of Physiology-Renal Physiology 296, nr 3 (marzec 2009): F478—F486. http://dx.doi.org/10.1152/ajprenal.90477.2008.
Pełny tekst źródłaMuniappan, Latha, Michihiro Okuyama, Aida Javidan, Devi Thiagarajan, Weihua Jiang, Jessica J. Moorleghen, Lihua Yang i in. "Inducible Depletion of Calpain-2 Mitigates Abdominal Aortic Aneurysm in Mice". Arteriosclerosis, Thrombosis, and Vascular Biology 41, nr 5 (5.05.2021): 1694–709. http://dx.doi.org/10.1161/atvbaha.120.315546.
Pełny tekst źródłaMurphy, Robyn M., Rodney J. Snow i Graham D. Lamb. "μ-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans". American Journal of Physiology-Cell Physiology 290, nr 1 (styczeń 2006): C116—C122. http://dx.doi.org/10.1152/ajpcell.00291.2005.
Pełny tekst źródłaPiper, Ann-Katrin, Reece A. Sophocleous, Samuel E. Ross, Frances J. Evesson, Omar Saleh, Adam Bournazos, Joe Yasa i in. "Loss of calpains-1 and -2 prevents repair of plasma membrane scrape injuries, but not small pores, and induces a severe muscular dystrophy". American Journal of Physiology-Cell Physiology 318, nr 6 (1.06.2020): C1226—C1237. http://dx.doi.org/10.1152/ajpcell.00408.2019.
Pełny tekst źródłaTheopold, U., M. Pintér, S. Daffre, Y. Tryselius, P. Friedrich, D. R. Nässel i D. Hultmark. "CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells." Molecular and Cellular Biology 15, nr 2 (luty 1995): 824–34. http://dx.doi.org/10.1128/mcb.15.2.824.
Pełny tekst źródłaArora, A. S., P. de Groen, Y. Emori i G. J. Gores. "A cascade of degradative hydrolase activity contributes to hepatocyte necrosis during anoxia". American Journal of Physiology-Gastrointestinal and Liver Physiology 270, nr 2 (1.02.1996): G238—G245. http://dx.doi.org/10.1152/ajpgi.1996.270.2.g238.
Pełny tekst źródłaIlian, M. A., i N. E. Forsberg. "Gene expression of calpains and their specific endogenous inhibitor, calpastatin, in skeletal muscle of fed and fasted rabbits". Biochemical Journal 287, nr 1 (1.10.1992): 163–71. http://dx.doi.org/10.1042/bj2870163.
Pełny tekst źródłaMontgomery, Darrice S., Ling Yu, Zinah M. Ghazi, Tiffany L. Thai, Otor Al-Khalili, He-Ping Ma, Douglas C. Eaton i Abdel A. Alli. "ENaC activity is regulated by calpain-2 proteolysis of MARCKS proteins". American Journal of Physiology-Cell Physiology 313, nr 1 (1.07.2017): C42—C53. http://dx.doi.org/10.1152/ajpcell.00244.2016.
Pełny tekst źródłaPánico, Pablo, Marcia Hiriart, Patricia Ostrosky-Wegman i Ana María Salazar. "TUG is a calpain-10 substrate involved in the translocation of GLUT4 in adipocytes". Journal of Molecular Endocrinology 65, nr 3 (październik 2020): 45–57. http://dx.doi.org/10.1530/jme-19-0253.
Pełny tekst źródłaVermaelen, Marianne, Pascal Sirvent, Fabrice Raynaud, Catherine Astier, Jacques Mercier, Alain Lacampagne i Olivier Cazorla. "Differential localization of autolyzed calpains 1 and 2 in slow and fast skeletal muscles in the early phase of atrophy". American Journal of Physiology-Cell Physiology 292, nr 5 (maj 2007): C1723—C1731. http://dx.doi.org/10.1152/ajpcell.00398.2006.
Pełny tekst źródłaMoshal, Karni S., Mahavir Singh, Utpal Sen, Dorothea Susanne E. Rosenberger, Brooke Henderson, Neetu Tyagi, Hong Zhang i Suresh C. Tyagi. "Homocysteine-mediated activation and mitochondrial translocation of calpain regulates MMP-9 in MVEC". American Journal of Physiology-Heart and Circulatory Physiology 291, nr 6 (grudzień 2006): H2825—H2835. http://dx.doi.org/10.1152/ajpheart.00377.2006.
Pełny tekst źródłaLiu, Xiuli, Juanita J. Rainey, Jay F. Harriman i Rick G. Schnellmann. "Calpains mediate acute renal cell death: role of autolysis and translocation". American Journal of Physiology-Renal Physiology 281, nr 4 (1.10.2001): F728—F738. http://dx.doi.org/10.1152/ajprenal.2001.281.4.f728.
Pełny tekst źródłaSeremwe, Mutsa, Rick G. Schnellmann i Wendy B. Bollag. "Calpain-10 Activity Underlies Angiotensin II-Induced Aldosterone Production in an Adrenal Glomerulosa Cell Model". Endocrinology 156, nr 6 (1.06.2015): 2138–49. http://dx.doi.org/10.1210/en.2014-1866.
Pełny tekst źródłaHata, Shoji, Naoko Doi, Fujiko Kitamura i 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, nr 38 (23.07.2007): 27847–56. http://dx.doi.org/10.1074/jbc.m703168200.
Pełny tekst źródłaOu, B. R., i N. E. Forsberg. "Determination of skeletal muscle calpain and calpastatin activities during maturation". American Journal of Physiology-Endocrinology and Metabolism 261, nr 6 (1.12.1991): E677—E683. http://dx.doi.org/10.1152/ajpendo.1991.261.6.e677.
Pełny tekst źródłaLee, Wing-Kee, Blazej Torchalski i Frank Thévenod. "Cadmium-induced ceramide formation triggers calpain-dependent apoptosis in cultured kidney proximal tubule cells". American Journal of Physiology-Cell Physiology 293, nr 3 (wrzesień 2007): C839—C847. http://dx.doi.org/10.1152/ajpcell.00197.2007.
Pełny tekst źródłaLaajala, Mira, Minna M. Hankaniemi, Juha A. E. Määttä, Vesa P. Hytönen, Olli H. Laitinen i Varpu Marjomäki. "Host Cell Calpains Can Cleave Structural Proteins from the Enterovirus Polyprotein". Viruses 11, nr 12 (28.11.2019): 1106. http://dx.doi.org/10.3390/v11121106.
Pełny tekst źródłaDouillard, Aymeric, Olivier Galbes, Bernadette Rossano, Barbara Vernus, Anne Bonnieu, Robin Candau i Guillaume Py. "Time course in calpain activity and autolysis in slow and fast skeletal muscle during clenbuterol treatment". Canadian Journal of Physiology and Pharmacology 89, nr 2 (luty 2011): 117–25. http://dx.doi.org/10.1139/y10-114.
Pełny tekst źródłaGOLL, DARREL E., VALERY F. THOMPSON, HONGQI LI, WEI WEI i JINYANG CONG. "The Calpain System". Physiological Reviews 83, nr 3 (lipiec 2003): 731–801. http://dx.doi.org/10.1152/physrev.00029.2002.
Pełny tekst źródłaWang, Lijing, Ligong Duan, Xukun Li i Guoping Li. "Acute-Exercise-Induced Alterations in Calpain and Calpastatin Expression in Rat Muscle". Journal of Sport Rehabilitation 18, nr 2 (maj 2009): 213–28. http://dx.doi.org/10.1123/jsr.18.2.213.
Pełny tekst źródłaPAUL, David S., Anne W. HARMON, Courtney P. WINSTON i Yashomati M. PATEL. "Calpain facilitates GLUT4 vesicle translocation during insulin-stimulated glucose uptake in adipocytes". Biochemical Journal 376, nr 3 (15.12.2003): 625–32. http://dx.doi.org/10.1042/bj20030681.
Pełny tekst źródłaSuzuki, K., K. Shimizu, T. Hamamoto, Y. Nakagawa, T. Murachi i T. Yamamuro. "Characterization of proteoglycan degradation by calpain". Biochemical Journal 285, nr 3 (1.08.1992): 857–62. http://dx.doi.org/10.1042/bj2850857.
Pełny tekst źródłaElagib, Kamaleldin E., Lorrie L. Delehanty, Ivailo Mihaylov i Adam Goldfarb. "Calpain Regulation of Megakaryopoiesis through a Positive Regulatory Loop Involving P-TEFb, GATA-1, and RUNX1." Blood 114, nr 22 (20.11.2009): 566. http://dx.doi.org/10.1182/blood.v114.22.566.566.
Pełny tekst źródłaMacqueen, Daniel J., i Alexander H. Wilcox. "Characterization of the definitive classical calpain family of vertebrates using phylogenetic, evolutionary and expression analyses". Open Biology 4, nr 4 (kwiecień 2014): 130219. http://dx.doi.org/10.1098/rsob.130219.
Pełny tekst źródłaLehti, Maarit, Riikka Kivelä, Paavo Komi, Jyrki Komulainen, Heikki Kainulainen i Heikki Kyröläinen. "Effects of fatiguing jumping exercise on mRNA expression of titin-complex proteins and calpains". Journal of Applied Physiology 106, nr 4 (kwiecień 2009): 1419–24. http://dx.doi.org/10.1152/japplphysiol.90660.2008.
Pełny tekst źródłaBartus, Raymond T. "The Calpain Hypothesis of Neurodegeneration: Evidence for a Common Cytotoxic Pathway". Neuroscientist 3, nr 5 (wrzesień 1997): 314–27. http://dx.doi.org/10.1177/107385849700300513.
Pełny tekst źródłaNuzzi, Paul A., Melissa A. Senetar i Anna Huttenlocher. "Asymmetric Localization of Calpain 2 during Neutrophil Chemotaxis". Molecular Biology of the Cell 18, nr 3 (marzec 2007): 795–805. http://dx.doi.org/10.1091/mbc.e06-09-0876.
Pełny tekst źródłaGoll, Darrel E., Valery F. Thompson, Richard G. Taylor i Ahmed Ouali. "The calpain system and skeletal muscle growth". Canadian Journal of Animal Science 78, nr 4 (1.12.1998): 503–12. http://dx.doi.org/10.4141/a98-081.
Pełny tekst źródłaLarsen, Anna K., René Lametsch, John S. Elce, Jørgen K. Larsen, Bo Thomsen, Martin R. Larsen, Moira A. Lawson, Peter A. Greer i Per Ertbjerg. "Genetic disruption of calpain correlates with loss of membrane blebbing and differential expression of RhoGDI-1, cofilin and tropomyosin". Biochemical Journal 411, nr 3 (14.04.2008): 657–66. http://dx.doi.org/10.1042/bj20070522.
Pełny tekst źródłaRandriamboavonjy, Voahanginirina, Johann Isaak, Amro Elgheznawy, Frank Pistrosch, Timo Frömel, Xiaoke Yin, Klaus Badenhoop, Heinrich Heide, Manuel Mayr i Ingrid Fleming. "Calpain inhibition stabilizes the platelet proteome and reactivity in diabetes". Blood 120, nr 2 (12.07.2012): 415–23. http://dx.doi.org/10.1182/blood-2011-12-399980.
Pełny tekst źródłaMeier, Markus, Harald H. Klein, Jan Kramer, Maren Drenckhan i Morten Schütt. "Calpain inhibition impairs glycogen syntheses in HepG2 hepatoma cells without altering insulin signaling". Journal of Endocrinology 193, nr 1 (kwiecień 2007): 45–51. http://dx.doi.org/10.1677/joe.1.07087.
Pełny tekst źródłaNATH, Rathna, Kadee J. RASER, Daniel STAFFORD, Iradj HAJIMOHAMMADREZA, Avigail POSNER, Hamish ALLEN, Robert V. TALANIAN, Po-wai YUEN, Richard B. GILBERTSEN i Kevin K. W. WANG. "Non-erythroid α-spectrin breakdown by calpain and interleukin 1 β-converting-enzyme-like protease(s) in apoptotic cells: contributory roles of both protease families in neuronal apoptosis". Biochemical Journal 319, nr 3 (1.11.1996): 683–90. http://dx.doi.org/10.1042/bj3190683.
Pełny tekst źródłaPerrin, B. J., i A. Huttenlocher. "Calpain". International Journal of Biochemistry & Cell Biology 34, nr 7 (lipiec 2002): 722–25. http://dx.doi.org/10.1016/s1357-2725(02)00009-2.
Pełny tekst źródłaGoette, Andreas, Marco Arndt, Christoph Röcken, Thorsten Staack, Roland Bechtloff, Dirk Reinhold, Christof Huth, Siegfried Ansorge, Helmut U. Klein i Uwe Lendeckel. "Calpains and cytokines in fibrillating human atria". American Journal of Physiology-Heart and Circulatory Physiology 283, nr 1 (1.07.2002): H264—H272. http://dx.doi.org/10.1152/ajpheart.00505.2001.
Pełny tekst źródłaPestereva, N. S., A. Z. Marshak i M. N. Karpenko. "CALPAIN ACTIVITY UNDER EXPERIMENTAL INCREASING OF DOPAMINE LEVEL". Medical academic journal 19, nr 1S (15.12.2019): 221–22. http://dx.doi.org/10.17816/maj191s1221-222.
Pełny tekst źródłaLiu, Ming Cheng, Veronica Akle, Wenrong Zheng, Jitendra R. Dave, Frank C. Tortella, Ronald L. Hayes i Kevin K. W. Wang. "Comparing calpain- and caspase-3-mediated degradation patterns in traumatic brain injury by differential proteome analysis". Biochemical Journal 394, nr 3 (24.02.2006): 715–25. http://dx.doi.org/10.1042/bj20050905.
Pełny tekst źródłaWang, Yubin, Yan Liu, Amy Nham, Arash Sherbaf, Diana Quach, Emad Yahya, Davis Ranburger, Xiaoning Bi i Michel Baudry. "Calpain-2 as a therapeutic target in repeated concussion–induced neuropathy and behavioral impairment". Science Advances 6, nr 27 (lipiec 2020): eaba5547. http://dx.doi.org/10.1126/sciadv.aba5547.
Pełny tekst źródłaSaatman, Kathryn E., Babak Abai, Ashley Grosvenor, Christian K. Vorwerk, Douglas H. Smith i David F. Meaney. "Traumatic Axonal Injury Results in Biphasic Calpain Activation and Retrograde Transport Impairment in Mice". Journal of Cerebral Blood Flow & Metabolism 23, nr 1 (styczeń 2003): 34–42. http://dx.doi.org/10.1097/01.wcb.0000035040.10031.b0.
Pełny tekst źródłaSupinski, Gerald S., Alexander P. Alimov, Lin Wang, Xiao-Hong Song i Leigh A. Callahan. "Neutral sphingomyelinase 2 is required for cytokine-induced skeletal muscle calpain activation". American Journal of Physiology-Lung Cellular and Molecular Physiology 309, nr 6 (15.09.2015): L614—L624. http://dx.doi.org/10.1152/ajplung.00141.2015.
Pełny tekst źródłaStruglics, André, i Maria Hansson. "Calpain is involved in C-terminal truncation of human aggrecan". Biochemical Journal 430, nr 3 (27.08.2010): 531–38. http://dx.doi.org/10.1042/bj20100591.
Pełny tekst źródłaRAVULAPALLI, Ravikiran, Beatriz GARCIA DIAZ, Robert L. CAMPBELL i Peter L. DAVIES. "Homodimerization of calpain 3 penta-EF-hand domain". Biochemical Journal 388, nr 2 (24.05.2005): 585–91. http://dx.doi.org/10.1042/bj20041821.
Pełny tekst źródłaParnaud, Géraldine, Eva Hammar, Dominique G. Rouiller i Domenico Bosco. "Inhibition of calpain blocks pancreatic β-cell spreading and insulin secretion". American Journal of Physiology-Endocrinology and Metabolism 289, nr 2 (sierpień 2005): E313—E321. http://dx.doi.org/10.1152/ajpendo.00006.2005.
Pełny tekst źródłaAlvarez-Arce, Alejandro, Irene Lee-Rivera, Edith López, Arturo Hernández-Cruz i Ana María López-Colomé. "Thrombin-Induced Calpain Activation Promotes Protease-Activated Receptor 1 Internalization". International Journal of Cell Biology 2017 (2017): 1–14. http://dx.doi.org/10.1155/2017/1908310.
Pełny tekst źródłaAbeyrathna, Prasanna, Laszlo Kovacs, Weihong Han i Yunchao Su. "Calpain-2 activates Akt via TGF-β1-mTORC2 pathway in pulmonary artery smooth muscle cells". American Journal of Physiology-Cell Physiology 311, nr 1 (1.07.2016): C24—C34. http://dx.doi.org/10.1152/ajpcell.00295.2015.
Pełny tekst źródłaYeh, J.-Y., B.-R. Ou i 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, nr 2 (maj 1994): 209–17. http://dx.doi.org/10.1677/joe.0.1410209.
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