Artykuły w czasopismach na temat „Calpain 1”
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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 źródłaWeber, Jonasz J., Eva Haas, Yacine Maringer, Stefan Hauser, Nicolas L. P. Casadei, Athar H. Chishti, Olaf Riess i Jeannette Hübener-Schmid. "Calpain-1 ablation partially rescues disease-associated hallmarks in models of Machado-Joseph disease". Human Molecular Genetics 29, nr 6 (21.01.2020): 892–906. http://dx.doi.org/10.1093/hmg/ddaa010.
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 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 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 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 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 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 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 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 źródłaKuchay, Shafi M., William P. Fay i Athar H. Chishti. "Double Knockouts Reveal That Protein Tyrosine Phosphatase 1B Is a Physiological Substrate of Calpain-1 in Platelets." Blood 108, nr 11 (16.11.2006): 396. http://dx.doi.org/10.1182/blood.v108.11.396.396.
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 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 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 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 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 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 źródłaWieschhaus, Adam, Anwar Khan, Asma Zaidi, Henry Rogalin, Toshihiko Hanada, Fei Liu, Lucia De Franceschi, Carlo Brugnara, Alicia Rivera i Athar H. Chishti. "Calpain-1 knockout reveals broad effects on erythrocyte deformability and physiology". Biochemical Journal 448, nr 1 (18.10.2012): 141–52. http://dx.doi.org/10.1042/bj20121008.
Pełny tekst źródłaGafni, Juliette, Evan Hermel, Jessica E. Young, Cheryl L. Wellington, Michael R. Hayden i Lisa M. Ellerby. "Inhibition of Calpain Cleavage of Huntingtin Reduces Toxicity". Journal of Biological Chemistry 279, nr 19 (23.02.2004): 20211–20. http://dx.doi.org/10.1074/jbc.m401267200.
Pełny tekst źródłaKuchay, Shafi M., Nayoung Kim, Elizabeth A. Grunz, William P. Fay i Athar H. Chishti. "Double Knockouts Reveal that Protein Tyrosine Phosphatase 1B Is a Physiological Target of Calpain-1 in Platelets". Molecular and Cellular Biology 27, nr 17 (18.06.2007): 6038–52. http://dx.doi.org/10.1128/mcb.00522-07.
Pełny tekst źródłaZhao, Ming, Yang Yang, Xueyuan Bi, Xiaojiang Yu, Hanghuan Jia, Huanle Fang i Weijin Zang. "Acetylcholine Attenuated TNF-α-Induced Apoptosis in H9c2 Cells: Role of Calpain and the p38-MAPK Pathway". Cellular Physiology and Biochemistry 36, nr 5 (2015): 1877–89. http://dx.doi.org/10.1159/000430157.
Pełny tekst źródłaMcClung, J. M., A. R. Judge, E. E. Talbert i S. K. Powers. "Calpain-1 is required for hydrogen peroxide-induced myotube atrophy". American Journal of Physiology-Cell Physiology 296, nr 2 (luty 2009): C363—C371. http://dx.doi.org/10.1152/ajpcell.00497.2008.
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 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 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 źródłaArnandis, Teresa, Ivan Ferrer-Vicens, Luis Torres, Concha García, Elena R. Garcia-Trevijano, Rosa Zaragoza i Juan R. Viña. "Differential functions of calpain 1 during epithelial cell death and adipocyte differentiation in mammary gland involution". Biochemical Journal 459, nr 2 (28.03.2014): 355–68. http://dx.doi.org/10.1042/bj20130847.
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 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 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 źródłaRintanen, Nina, Mikko Karjalainen, Jonna Alanko, Lassi Paavolainen, Anita Mäki, Liisa Nissinen, Moona Lehkonen i in. "Calpains promote α2β1 integrin turnover in nonrecycling integrin pathway". Molecular Biology of the Cell 23, nr 3 (luty 2012): 448–63. http://dx.doi.org/10.1091/mbc.e11-06-0548.
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 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 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 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 źródłaNwankwo, Jennifer O., Sha Huang, Jongyoon Han i Athar H. Chishti. "Genetic Deletion of Calpain-1 Improves Reticulocyte Deformability in a Mouse Model of Severe Sickle Cell Disease". Blood 124, nr 21 (6.12.2014): 2698. http://dx.doi.org/10.1182/blood.v124.21.2698.2698.
Pełny tekst źródłaWatson, P. H., S. T. Mortimer, K. K. W. Wang, D. E. Croall i D. A. Hanley. "Calcium-activated proteases in the bovine parathyroid gland: potential role in degradation of parathyroid hormone to peptide fragments". Journal of Molecular Endocrinology 15, nr 1 (sierpień 1995): 61–71. http://dx.doi.org/10.1677/jme.0.0150061.
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 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.
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 źródłaVerheijden, Kim A. T., Ramon Sonneveld, Marinka Bakker-van Bebber, Jack F. M. Wetzels, Johan van der Vlag i Tom Nijenhuis. "The Calcium-Dependent Protease Calpain-1 Links TRPC6 Activity to Podocyte Injury". Journal of the American Society of Nephrology 29, nr 8 (28.06.2018): 2099–109. http://dx.doi.org/10.1681/asn.2016111248.
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 źródłaBerkholz, Janine, Andreas Zakrzewicz i Barbara Munz. "skNAC depletion stimulates myoblast migration and perturbs sarcomerogenesis by enhancing calpain 1 and 3 activity". Biochemical Journal 453, nr 2 (28.06.2013): 303–10. http://dx.doi.org/10.1042/bj20130195.
Pełny tekst źródłaBriz, Victor, i Michel Baudry. "Calpains: Master Regulators of Synaptic Plasticity". Neuroscientist 23, nr 3 (17.05.2016): 221–31. http://dx.doi.org/10.1177/1073858416649178.
Pełny tekst źródłaYoshikawa, Yoshiro, Hiroji Hagihara, Yoshimi Ohga, Chikako Nakajima-Takenaka, Ken-ya Murata, Shigeki Taniguchi i Miyako Takaki. "Calpain inhibitor-1 protects the rat heart from ischemia-reperfusion injury: analysis by mechanical work and energetics". American Journal of Physiology-Heart and Circulatory Physiology 288, nr 4 (kwiecień 2005): H1690—H1698. http://dx.doi.org/10.1152/ajpheart.00666.2004.
Pełny tekst źródłaFareed, Moin U., Amy R. Evenson, Wei Wei, Michael Menconi, Vitaliy Poylin, Victoria Petkova, Bernadette Pignol i 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, nr 6 (czerwiec 2006): R1589—R1597. http://dx.doi.org/10.1152/ajpregu.00668.2005.
Pełny tekst źródłaSAVART, M., V. PALLET, P. LETRAD, C. BOSSUET i A. DUCASTAING. "Calpain 1-protein kinase C complex: effect of calpain inhibitors after dissociation". Biochimie 73, nr 11 (listopad 1991): 1409–16. http://dx.doi.org/10.1016/0300-9084(91)90172-w.
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