Journal articles on the topic 'Calpain'
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Chhabra, A., H. Fernando, R. E. Mansel, and W. G. Jiang. "Pattern of expression of calpain subunits (large and small) in human breast cancer and the prognostic significance." Journal of Clinical Oncology 25, no. 18_suppl (June 20, 2007): 21078. http://dx.doi.org/10.1200/jco.2007.25.18_suppl.21078.
Full textUpla, Paula, Varpu Marjomäki, Liisa Nissinen, Camilla Nylund, Matti Waris, Timo Hyypiä, and Jyrki Heino. "Calpain 1 and 2 Are Required for RNA Replication of Echovirus 1." Journal of Virology 82, no. 3 (November 21, 2007): 1581–90. http://dx.doi.org/10.1128/jvi.01375-07.
Full textFontenele, Marcio, Bomyi Lim, Danielle Oliveira, Márcio Buffolo, David H. Perlman, Trudi Schupbach, and Helena Araujo. "Calpain A modulates Toll responses by limited Cactus/IκB proteolysis." Molecular Biology of the Cell 24, no. 18 (September 15, 2013): 2966–80. http://dx.doi.org/10.1091/mbc.e13-02-0113.
Full textSORIMACHI, Hiroyuki, Shoichi ISHIURA, and Koichi SUZUKI. "Structure and physiological function of calpains." Biochemical Journal 328, no. 3 (December 15, 1997): 721–32. http://dx.doi.org/10.1042/bj3280721.
Full textMurphy, Robyn M., Rodney J. Snow, and Graham D. Lamb. "μ-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans." American Journal of Physiology-Cell Physiology 290, no. 1 (January 2006): C116—C122. http://dx.doi.org/10.1152/ajpcell.00291.2005.
Full textTheopold, 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.
Full textCovington, Marisa D., David D. Arrington, and Rick G. Schnellmann. "Calpain 10 is required for cell viability and is decreased in the aging kidney." American Journal of Physiology-Renal Physiology 296, no. 3 (March 2009): F478—F486. http://dx.doi.org/10.1152/ajprenal.90477.2008.
Full textArora, A. S., P. de Groen, Y. Emori, and G. J. Gores. "A cascade of degradative hydrolase activity contributes to hepatocyte necrosis during anoxia." American Journal of Physiology-Gastrointestinal and Liver Physiology 270, no. 2 (February 1, 1996): G238—G245. http://dx.doi.org/10.1152/ajpgi.1996.270.2.g238.
Full textSultan, Karim R., Bernd T. Dittrich, and Dirk Pette. "Calpain activity in fast, slow, transforming, and regenerating skeletal muscles of rat." American Journal of Physiology-Cell Physiology 279, no. 3 (September 1, 2000): C639—C647. http://dx.doi.org/10.1152/ajpcell.2000.279.3.c639.
Full textMiyazaki, Takuro. "Calpain and Cardiometabolic Diseases." International Journal of Molecular Sciences 24, no. 23 (November 26, 2023): 16782. http://dx.doi.org/10.3390/ijms242316782.
Full textPánico, 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.
Full textMellgren, 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.
Full textWeber, 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.
Full textAzam, Mohammad, Shaida S. Andrabi, Kenneth E. Sahr, Lakshmi Kamath, Athan Kuliopulos, and Athar H. Chishti. "Disruption of the Mouse μ-Calpain Gene Reveals an Essential Role in Platelet Function." Molecular and Cellular Biology 21, no. 6 (March 15, 2001): 2213–20. http://dx.doi.org/10.1128/mcb.21.6.2213-2220.2001.
Full textSchultz, Bruna, Jéssica Taday, Leonardo Menezes, Anderson Cigerce, Marina C. Leite, and Carlos-Alberto Gonçalves. "Calpain-Mediated Alterations in Astrocytes Before and During Amyloid Chaos in Alzheimer’s Disease." Journal of Alzheimer's Disease 84, no. 4 (December 7, 2021): 1415–30. http://dx.doi.org/10.3233/jad-215182.
Full textLiu, Xiuli, Juanita J. Rainey, Jay F. Harriman, and Rick G. Schnellmann. "Calpains mediate acute renal cell death: role of autolysis and translocation." American Journal of Physiology-Renal Physiology 281, no. 4 (October 1, 2001): F728—F738. http://dx.doi.org/10.1152/ajprenal.2001.281.4.f728.
Full textKhoutorsky, Arkady, and Micha E. Spira. "Calpain Inhibitors Alter the Excitable Membrane Properties of Cultured Aplysia Neurons." Journal of Neurophysiology 100, no. 5 (November 2008): 2784–93. http://dx.doi.org/10.1152/jn.90487.2008.
Full textIlian, 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.
Full textBen-Aharon, Irit, Paula R. Brown, Nir Etkovitz, Edward M. Eddy, and Ruth Shalgi. "The expression of calpain 1 and calpain 2 in spermatogenic cells and spermatozoa of the mouse." Reproduction 129, no. 4 (April 2005): 435–42. http://dx.doi.org/10.1530/rep.1.00255.
Full textNina S. Pestereva, Irina S. Ivleva, Irina M. Kotova, Dmitriy S. Traktirov, and Marina N. Karpenko. "Region-specific changes in expression and activity of calpains in the CNS of native rats." Biomedicine 42, no. 4 (September 12, 2022): 771–74. http://dx.doi.org/10.51248/.v42i4.1653.
Full textSeremwe, Mutsa, Rick G. Schnellmann, and Wendy B. Bollag. "Calpain-10 Activity Underlies Angiotensin II-Induced Aldosterone Production in an Adrenal Glomerulosa Cell Model." Endocrinology 156, no. 6 (June 1, 2015): 2138–49. http://dx.doi.org/10.1210/en.2014-1866.
Full textZhang, Mengxiao, Grace Wang, and Tianqing Peng. "Calpain-Mediated Mitochondrial Damage: An Emerging Mechanism Contributing to Cardiac Disease." Cells 10, no. 8 (August 8, 2021): 2024. http://dx.doi.org/10.3390/cells10082024.
Full textELCE, John S., Peter L. DAVIES, Carol HEGADORN, Donald H. MAURICE, and J. Simon C. ARTHUR. "The effects of truncations of the small subunit on m-calpain activity and heterodimer formation." Biochemical Journal 326, no. 1 (August 15, 1997): 31–38. http://dx.doi.org/10.1042/bj3260031.
Full textPiper, Ann-Katrin, Reece A. Sophocleous, Samuel E. Ross, Frances J. Evesson, Omar Saleh, Adam Bournazos, Joe Yasa, et al. "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, no. 6 (June 1, 2020): C1226—C1237. http://dx.doi.org/10.1152/ajpcell.00408.2019.
Full textBlanc, Fany, Laetitia Furio, Dorothée Moisy, Hui-Ling Yen, Michel Chignard, Emmanuel Letavernier, Nadia Naffakh, Chris Ka Pun Mok, and Mustapha Si-Tahar. "Targeting host calpain proteases decreases influenza A virus infection." American Journal of Physiology-Lung Cellular and Molecular Physiology 310, no. 7 (April 1, 2016): L689—L699. http://dx.doi.org/10.1152/ajplung.00314.2015.
Full textKuchay, 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.
Full textSorimachi, Hiroyuki, Hiroshi Mamitsuka, and Yasuko Ono. "Understanding the substrate specificity of conventional calpains." Biological Chemistry 393, no. 9 (September 1, 2012): 853–71. http://dx.doi.org/10.1515/hsz-2012-0143.
Full textOu, B. R., and N. E. Forsberg. "Determination of skeletal muscle calpain and calpastatin activities during maturation." American Journal of Physiology-Endocrinology and Metabolism 261, no. 6 (December 1, 1991): E677—E683. http://dx.doi.org/10.1152/ajpendo.1991.261.6.e677.
Full textBevers, 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.
Full textMcCartney, Christian-Scott E., Qilu Ye, Robert L. Campbell, and Peter L. Davies. "Insertion sequence 1 from calpain-3 is functional in calpain-2 as an internal propeptide." Journal of Biological Chemistry 293, no. 46 (September 25, 2018): 17716–30. http://dx.doi.org/10.1074/jbc.ra118.004803.
Full textBaudry, 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.
Full textMoraczewski, J., E. Piekarska, M. Zimowska, and M. Sobolewska. "Activity of mu- and m-calpain in regenerating fast and slow twitch skeletal muscles." Acta Biochimica Polonica 43, no. 4 (December 31, 1996): 693–700. http://dx.doi.org/10.18388/abp.1996_4466.
Full textKashiwagi, Aki, Ernestina Schipani, Mikaela J. Fein, Peter A. Greer, and Masako Shimada. "Targeted Deletion of Capn4 in Cells of the Chondrocyte Lineage Impairs Chondrocyte Proliferation and Differentiation." Molecular and Cellular Biology 30, no. 11 (April 5, 2010): 2799–810. http://dx.doi.org/10.1128/mcb.00157-10.
Full textMoshal, Karni S., Mahavir Singh, Utpal Sen, Dorothea Susanne E. Rosenberger, Brooke Henderson, Neetu Tyagi, Hong Zhang, and 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, no. 6 (December 2006): H2825—H2835. http://dx.doi.org/10.1152/ajpheart.00377.2006.
Full textBen-Aharon, Irit, Karin Haim, Ruth Shalgi, and Dalit Ben-Yosef. "Expression and possible involvement of calpain isoforms in mammalian egg activation." Reproduction 130, no. 2 (August 2005): 165–75. http://dx.doi.org/10.1530/rep.1.00602.
Full textGafni, Juliette, Evan Hermel, Jessica E. Young, Cheryl L. Wellington, Michael R. Hayden, and Lisa M. Ellerby. "Inhibition of Calpain Cleavage of Huntingtin Reduces Toxicity." Journal of Biological Chemistry 279, no. 19 (February 23, 2004): 20211–20. http://dx.doi.org/10.1074/jbc.m401267200.
Full textWang, Yubin, Yan Liu, Xiaoning Bi, and Michel Baudry. "Calpain-1 and Calpain-2 in the Brain: New Evidence for a Critical Role of Calpain-2 in Neuronal Death." Cells 9, no. 12 (December 16, 2020): 2698. http://dx.doi.org/10.3390/cells9122698.
Full textGOLL, 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.
Full textEnnes-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.
Full textRose, Aaron, Huang Zhi, Fukun Hoffmann, Robert Norton, and Peter Hoffamann. "Selenoprotein K is a novel target of m-calpain, and cleavage is regulated by toll-like receptor-induced calpastatin in macrophages (54.22)." Journal of Immunology 188, no. 1_Supplement (May 1, 2012): 54.22. http://dx.doi.org/10.4049/jimmunol.188.supp.54.22.
Full textArrington, David D., Terry R. Van Vleet, and Rick G. Schnellmann. "Calpain 10: a mitochondrial calpain and its role in calcium-induced mitochondrial dysfunction." American Journal of Physiology-Cell Physiology 291, no. 6 (December 2006): C1159—C1171. http://dx.doi.org/10.1152/ajpcell.00207.2006.
Full textPotter, David A., Jennifer S. Tirnauer, Richard Janssen, Dorothy E. Croall, Christina N. Hughes, Kerry A. Fiacco, James W. Mier, Masatoshi Maki, and Ira M. Herman. "Calpain Regulates Actin Remodeling during Cell Spreading." Journal of Cell Biology 141, no. 3 (May 4, 1998): 647–62. http://dx.doi.org/10.1083/jcb.141.3.647.
Full textKalbe, 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.
Full textNakagawa, Toshiyuki, and Junying Yuan. "Cross-Talk between Two Cysteine Protease Families." Journal of Cell Biology 150, no. 4 (August 21, 2000): 887–94. http://dx.doi.org/10.1083/jcb.150.4.887.
Full textBelhadj, Soumaya, Nina Sofia Hermann, Yu Zhu, Gustav Christensen, Torsten Strasser, and François Paquet-Durand. "Visualizing Cell Death in Live Retina: Using Calpain Activity Detection as a Biomarker for Retinal Degeneration." International Journal of Molecular Sciences 23, no. 7 (March 31, 2022): 3892. http://dx.doi.org/10.3390/ijms23073892.
Full textWang, Lijing, Ligong Duan, Xukun Li, and Guoping Li. "Acute-Exercise-Induced Alterations in Calpain and Calpastatin Expression in Rat Muscle." Journal of Sport Rehabilitation 18, no. 2 (May 2009): 213–28. http://dx.doi.org/10.1123/jsr.18.2.213.
Full textLee, Wing-Kee, Blazej Torchalski, and Frank Thévenod. "Cadmium-induced ceramide formation triggers calpain-dependent apoptosis in cultured kidney proximal tubule cells." American Journal of Physiology-Cell Physiology 293, no. 3 (September 2007): C839—C847. http://dx.doi.org/10.1152/ajpcell.00197.2007.
Full textMacqueen, 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.
Full textMuniappan, Latha, Michihiro Okuyama, Aida Javidan, Devi Thiagarajan, Weihua Jiang, Jessica J. Moorleghen, Lihua Yang, et al. "Inducible Depletion of Calpain-2 Mitigates Abdominal Aortic Aneurysm in Mice." Arteriosclerosis, Thrombosis, and Vascular Biology 41, no. 5 (May 5, 2021): 1694–709. http://dx.doi.org/10.1161/atvbaha.120.315546.
Full textKuchay, Shafi M., William P. Fay, and Athar H. Chishti. "Double Knockouts Reveal That Protein Tyrosine Phosphatase 1B Is a Physiological Substrate of Calpain-1 in Platelets." Blood 108, no. 11 (November 16, 2006): 396. http://dx.doi.org/10.1182/blood.v108.11.396.396.
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