Artículos de revistas sobre el tema "Ceramidase"
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Yuan, Changqing, Raghavendra Pralhada Rao, Nahid Jesmin, Takeshi Bamba, Kunio Nagashima, Alberto Pascual, Thomas Preat, Eiichiro Fukusaki, Usha Acharya y Jairaj K. Acharya. "CDase is a pan-ceramidase in Drosophila". Molecular Biology of the Cell 22, n.º 1 (enero de 2011): 33–43. http://dx.doi.org/10.1091/mbc.e10-05-0453.
Texto completoDuarte, Carolina, Juliet Akkaoui, Chiaki Yamada, Anny Ho, Cungui Mao y Alexandru Movila. "Elusive Roles of the Different Ceramidases in Human Health, Pathophysiology, and Tissue Regeneration". Cells 9, n.º 6 (2 de junio de 2020): 1379. http://dx.doi.org/10.3390/cells9061379.
Texto completoParveen, Farzana, Daniel Bender, Shi-Hui Law, Vineet Kumar Mishra, Chih-Chieh Chen y Liang-Yin Ke. "Role of Ceramidases in Sphingolipid Metabolism and Human Diseases". Cells 8, n.º 12 (4 de diciembre de 2019): 1573. http://dx.doi.org/10.3390/cells8121573.
Texto completoJin, K., Y. Higaki, Y. Takagi, K. Higuchi, Y. Yada, M. Kawashima y G. Imokawa. "Analysis of beta-glucocerebrosidase and ceramidase activities in atopic and aged dry skin." Acta Dermato-Venereologica 74, n.º 5 (1 de septiembre de 1994): 337–40. http://dx.doi.org/10.2340/0001555574341343.
Texto completoRamachandra, Nagaraju y Andreas Conzelmann. "Membrane topology of yeast alkaline ceramidase YPC1". Biochemical Journal 452, n.º 3 (31 de mayo de 2013): 585–94. http://dx.doi.org/10.1042/bj20130085.
Texto completoZaibaq, Faris, Tyrone Dowdy y Mioara Larion. "TMET-36. ACID CERAMIDASE INHIBITION EXPLOITS SPHINGOLIPID VULNERABILITIES IN IDH MUTANT GLIOMAS". Neuro-Oncology 24, Supplement_7 (1 de noviembre de 2022): vii269—vii270. http://dx.doi.org/10.1093/neuonc/noac209.1041.
Texto completoProksch, Denny, Jan Jasper Klein y Christoph Arenz. "Potent Inhibition of Acid Ceramidase by Novel B-13 Analogues". Journal of Lipids 2011 (2011): 1–8. http://dx.doi.org/10.1155/2011/971618.
Texto completoYi, Jae Kyo, Ruijuan Xu, Lina M. Obeid, Yusuf A. Hannun, Michael V. Airola y Cungui Mao. "Alkaline ceramidase catalyzes the hydrolysis of ceramides via a catalytic mechanism shared by Zn2+-dependent amidases". PLOS ONE 17, n.º 9 (1 de septiembre de 2022): e0271540. http://dx.doi.org/10.1371/journal.pone.0271540.
Texto completoOlsson, Maria, Rui-Dong Duan, Lena Ohlsson y Åke Nilsson. "Rat intestinal ceramidase: purification, properties, and physiological relevance". American Journal of Physiology-Gastrointestinal and Liver Physiology 287, n.º 4 (octubre de 2004): G929—G937. http://dx.doi.org/10.1152/ajpgi.00155.2004.
Texto completoBIONDA, Clara, Jacques PORTOUKALIAN, Daniel SCHMITT, Claire RODRIGUEZ-LAFRASSE y Dominique ARDAIL. "Subcellular compartmentalization of ceramide metabolism: MAM (mitochondria-associated membrane) and/or mitochondria?" Biochemical Journal 382, n.º 2 (24 de agosto de 2004): 527–33. http://dx.doi.org/10.1042/bj20031819.
Texto completoBeckmann, Nadine, Katrin Anne Becker, Stephanie Kadow, Fabian Schumacher, Melanie Kramer, Claudine Kühn, Walter J. Schulz-Schaeffer et al. "Acid Sphingomyelinase Deficiency Ameliorates Farber Disease". International Journal of Molecular Sciences 20, n.º 24 (11 de diciembre de 2019): 6253. http://dx.doi.org/10.3390/ijms20246253.
Texto completoLi, Wen-hong. "Targeting Ceramides and Adiponectin Receptors in the Islet of Langerhans for Treating Diabetes". Molecules 27, n.º 18 (19 de septiembre de 2022): 6117. http://dx.doi.org/10.3390/molecules27186117.
Texto completoZager, R. A., D. S. Conrad y K. Burkhart. "Ceramide accumulation during oxidant renal tubular injury: mechanisms and potential consequences." Journal of the American Society of Nephrology 9, n.º 9 (septiembre de 1998): 1670–80. http://dx.doi.org/10.1681/asn.v991670.
Texto completoVijayan, Yadu, Manendra Babu Lankadasari y Kuzhuvelil B. Harikumar. "Acid Ceramidase: A Novel Therapeutic Target in Cancer". Current Topics in Medicinal Chemistry 19, n.º 17 (19 de septiembre de 2019): 1512–20. http://dx.doi.org/10.2174/1568026619666190227222930.
Texto completoGeiger, Nina, Louise Kersting, Jan Schlegel, Linda Stelz, Sofie Fähr, Viktoria Diesendorf, Valeria Roll et al. "The Acid Ceramidase Is a SARS-CoV-2 Host Factor". Cells 11, n.º 16 (15 de agosto de 2022): 2532. http://dx.doi.org/10.3390/cells11162532.
Texto completoBeckmann, Nadine, Stephanie Kadow, Fabian Schumacher, Joachim R. Göthert, Stefanie Kesper, Annette Draeger, Walter J. Schulz-Schaeffer et al. "Pathological manifestations of Farber disease in a new mouse model". Biological Chemistry 399, n.º 10 (25 de septiembre de 2018): 1183–202. http://dx.doi.org/10.1515/hsz-2018-0170.
Texto completoHawkins, Cyntanna C., Amber B. Jones, Emily R. Gordon, Sarah E. Williford, Yuvika Harsh, Julia K. Ziebro, Catherine J. Landis et al. "Targeting Acid Ceramidase Inhibits Glioblastoma Cell Migration through Decreased AKT Signaling". Cells 11, n.º 12 (9 de junio de 2022): 1873. http://dx.doi.org/10.3390/cells11121873.
Texto completoOuairy, Cécile M. J., Maria J. Ferraz, Rolf G. Boot, Marc P. Baggelaar, Mario van der Stelt, Monique Appelman, Gijsbert A. van der Marel, Bogdan I. Florea, Johannes M. F. G. Aerts y Herman S. Overkleeft. "Development of an acid ceramidase activity-based probe". Chemical Communications 51, n.º 28 (2015): 6161–63. http://dx.doi.org/10.1039/c5cc00356c.
Texto completoStrelow, Astrid, Katussevani Bernardo, Sabine Adam-Klages, Thomas Linke, Konrad Sandhoff, Martin Krönke y Dieter Adam. "Overexpression of Acid Ceramidase Protects from Tumor Necrosis Factor–Induced Cell Death". Journal of Experimental Medicine 192, n.º 5 (28 de agosto de 2000): 601–12. http://dx.doi.org/10.1084/jem.192.5.601.
Texto completoKato, H., K. Nemoto, M. Shimizu, A. Abe, S. Asai, N. Ishihama, S. Matsuoka et al. "Recognition of pathogen-derived sphingolipids in Arabidopsis". Science 376, n.º 6595 (20 de mayo de 2022): 857–60. http://dx.doi.org/10.1126/science.abn0650.
Texto completoHe, Xingxuan y Edward H. Schuchman. "Ceramide and Ischemia/Reperfusion Injury". Journal of Lipids 2018 (2018): 1–11. http://dx.doi.org/10.1155/2018/3646725.
Texto completoCorrenti, Jason, Chelsea Lin, Jascha Brettschneider, Amy Kuriakose, Sookyoung Jeon, Eleonora Scorletti, Amanke Oranu et al. "Liver-specific ceramide reduction alleviates steatosis and insulin resistance in alcohol-fed mice". Journal of Lipid Research 61, n.º 7 (12 de mayo de 2020): 983–94. http://dx.doi.org/10.1194/jlr.ra119000446.
Texto completoLaurier-Laurin, Marie-Elaine, Audrée De Montigny, Suzanne Attiori Essis, Michel Cyr y Guy Massicotte. "Blockade of Lysosomal Acid Ceramidase Induces GluN2B-Dependent Tau Phosphorylation in Rat Hippocampal Slices". Neural Plasticity 2014 (2014): 1–11. http://dx.doi.org/10.1155/2014/196812.
Texto completoKITA, Katsuhiro, Noriyuki SUEYOSHI, Nozomu OKINO, Masanori INAGAKI, Hideharu ISHIDA, Makoto KISO, Shuhei IMAYAMA, Takashi NAKAMURA y Makoto ITO. "Activation of bacterial ceramidase by anionic glycerophospholipids: possible involvement in ceramide hydrolysis on atopic skin by Pseudomonas ceramidase". Biochemical Journal 362, n.º 3 (8 de marzo de 2002): 619–26. http://dx.doi.org/10.1042/bj3620619.
Texto completoChoi, Moonsuk S., Mary A. Anderson, Zhongjian Zhang, Drazen B. Zimonjic, Nicolae Popescu y Anil B. Mukherjee. "Neutral ceramidase gene: role in regulating ceramide-induced apoptosis". Gene 315 (octubre de 2003): 113–22. http://dx.doi.org/10.1016/s0378-1119(03)00721-2.
Texto completoBhabak, Krishna P., Denny Proksch, Susanne Redmer y Christoph Arenz. "Novel fluorescent ceramide derivatives for probing ceramidase substrate specificity". Bioorganic & Medicinal Chemistry 20, n.º 20 (octubre de 2012): 6154–61. http://dx.doi.org/10.1016/j.bmc.2012.08.035.
Texto completoKITA, Katsuhiro, Noriyuki SUEYOSHI, Nozomu OKINO, Masanori INAGAKI, Hideharu ISHIDA, Makoto KISO, Shuhei IMAYAMA, Takashi NAKAMURA y Makoto ITO. "Activation of bacterial ceramidase by anionic glycerophospholipids: possible involvement in ceramide hydrolysis on atopic skin by Pseudomonas ceramidase". Biochemical Journal 362, n.º 3 (15 de marzo de 2002): 619. http://dx.doi.org/10.1042/0264-6021:3620619.
Texto completoHawkins, Cyntanna, Amber Jones, Julia Ziebro, Emily Gordon, Catherine Libby, Sarah Williford, Jeremy Allegood et al. "DDRE-06. TARGETING THE SPHINGOLIPID BALANCE VIA ACID CERAMIDASE INHIBITION TO DECREASE GROWTH OF TMZ-RESISTANT GLIOBLASTOMA AND BLOCK MIGRATION". Neuro-Oncology 23, Supplement_6 (2 de noviembre de 2021): vi75. http://dx.doi.org/10.1093/neuonc/noab196.290.
Texto completoFrohbergh, Michael, Xingxuan He y Edward H. Schuchman. "The molecular medicine of acid ceramidase". Biological Chemistry 396, n.º 6-7 (1 de junio de 2015): 759–65. http://dx.doi.org/10.1515/hsz-2014-0290.
Texto completoFerlinz, Klaus, Guido Kopal, Katussevani Bernardo, Thomas Linke, Julia Bär, Bernadette Breiden, Ulrich Neumann, Florian Lang, Edward H. Schuchman y Konrad Sandhoff. "Human Acid Ceramidase". Journal of Biological Chemistry 276, n.º 38 (12 de julio de 2001): 35352–60. http://dx.doi.org/10.1074/jbc.m103066200.
Texto completoLu, Ping, Shai White-Gilbertson, Gyda Beeson, Craig Beeson, Besim Ogretmen, James Norris y Christina Voelkel-Johnson. "Ceramide Synthase 6 Maximizes p53 Function to Prevent Progeny Formation from Polyploid Giant Cancer Cells". Cancers 13, n.º 9 (5 de mayo de 2021): 2212. http://dx.doi.org/10.3390/cancers13092212.
Texto completoKlemetti, Miira M., Sruthi Alahari, Martin Post y Isabella Caniggia. "Distinct Changes in Placental Ceramide Metabolism Characterize Type 1 and 2 Diabetic Pregnancies with Fetal Macrosomia or Preeclampsia". Biomedicines 11, n.º 3 (17 de marzo de 2023): 932. http://dx.doi.org/10.3390/biomedicines11030932.
Texto completoOhnishi, Yoshinori, Nozomu Okino, Makoto Ito y Shuhei Imayama. "Ceramidase Activity in Bacterial Skin Flora as a Possible Cause of Ceramide Deficiency in Atopic Dermatitis". Clinical Diagnostic Laboratory Immunology 6, n.º 1 (1 de enero de 1999): 101–4. http://dx.doi.org/10.1128/cdli.6.1.101-104.1999.
Texto completoZAGER, RICHARD A., KRISTIN M. BURKHART y ALI JOHNSON. "Sphingomyelinase and Membrane Sphingomyelin Content". Journal of the American Society of Nephrology 11, n.º 5 (mayo de 2000): 894–902. http://dx.doi.org/10.1681/asn.v115894.
Texto completoIkarashi, Nobutomo, Wataru Sato, Takahiro Toda, Makoto Ishii, Wataru Ochiai y Kiyoshi Sugiyama. "Inhibitory Effect of Polyphenol-Rich Fraction from the Bark ofAcacia mearnsiion Itching Associated with Allergic Dermatitis". Evidence-Based Complementary and Alternative Medicine 2012 (2012): 1–9. http://dx.doi.org/10.1155/2012/120389.
Texto completoHadas, Yoav, Adam S. Vincek, Elias Youssef, Magdalena M. Żak, Elena Chepurko, Nishat Sultana, Mohammad Tofael Kabir Sharkar et al. "Altering Sphingolipid Metabolism Attenuates Cell Death and Inflammatory Response After Myocardial Infarction". Circulation 141, n.º 11 (17 de marzo de 2020): 916–30. http://dx.doi.org/10.1161/circulationaha.119.041882.
Texto completoKeitsch, Simone, Joachim Riethmüller, Matthias Soddemann, Carolin Sehl, Barbara Wilker, Michael J. Edwards, Charles C. Caldwell, Martin Fraunholz, Erich Gulbins y Katrin Anne Becker. "Pulmonary infection of cystic fibrosis mice with Staphylococcus aureus requires expression of α-toxin". Biological Chemistry 399, n.º 10 (25 de septiembre de 2018): 1203–13. http://dx.doi.org/10.1515/hsz-2018-0161.
Texto completoWang, Chunyan, Juan Pablo Palavicini y Xianlin Han. "A Lipidomics Atlas of Selected Sphingolipids in Multiple Mouse Nervous System Regions". International Journal of Molecular Sciences 22, n.º 21 (21 de octubre de 2021): 11358. http://dx.doi.org/10.3390/ijms222111358.
Texto completoZHANG, XIAOJING, XINYAN KONG, CUI YANG, WENQI LIU, ZHIWEN ZOU, BIN XIA y TIANRONG XIN. "Ceramidase is involved in the development and reproduction of Panonychus citri". Zoosymposia 22 (30 de noviembre de 2022): 254. http://dx.doi.org/10.11646/zoosymposia.22.1.155.
Texto completoCasasampere, Mireia, Núria Bielsa, Daniel Riba, Laura Bassas, Ruijuan Xu, Cungui Mao, Gemma Fabriàs, José-Luis Abad, Antonio Delgado y Josefina Casas. "New fluorogenic probes for neutral and alkaline ceramidases". Journal of Lipid Research 60, n.º 6 (29 de marzo de 2019): 1174–81. http://dx.doi.org/10.1194/jlr.d092759.
Texto completoUsta, Julnar, Samer El Bawab, Patrick Roddy, Zdzislaw M. Szulc, Yusuf, A. Hannun y Alicja Bielawska. "Structural Requirements of Ceramide and Sphingosine Based Inhibitors of Mitochondrial Ceramidase†". Biochemistry 40, n.º 32 (agosto de 2001): 9657–68. http://dx.doi.org/10.1021/bi010535k.
Texto completoAirola, Michael V., William J. Allen, Michael J. Pulkoski-Gross, Lina M. Obeid, Robert C. Rizzo y Yusuf A. Hannun. "Structural Basis for Ceramide Recognition and Hydrolysis by Human Neutral Ceramidase". Structure 23, n.º 8 (agosto de 2015): 1482–91. http://dx.doi.org/10.1016/j.str.2015.06.013.
Texto completoRealini, Natalia, Francesca Palese, Daniela Pizzirani, Silvia Pontis, Abdul Basit, Anders Bach, Anand Ganesan y Daniele Piomelli. "Acid Ceramidase in Melanoma". Journal of Biological Chemistry 291, n.º 5 (9 de noviembre de 2015): 2422–34. http://dx.doi.org/10.1074/jbc.m115.666909.
Texto completoAlsamman, Sarah, Stephanie A. Christenson, Amy Yu, Nadia M. E. Ayad, Meghan S. Mooring, Joe M. Segal, Jimmy Kuang-Hsien Hu et al. "Targeting acid ceramidase inhibits YAP/TAZ signaling to reduce fibrosis in mice". Science Translational Medicine 12, n.º 557 (19 de agosto de 2020): eaay8798. http://dx.doi.org/10.1126/scitranslmed.aay8798.
Texto completoLai, Michele, Veronica La Rocca, Rachele Amato, Giulia Freer, Mario Costa, Pietro Giorgio Spezia, Paola Quaranta, Giuseppe Lombardo, Daniele Piomelli y Mauro Pistello. "Ablation of Acid Ceramidase Impairs Autophagy and Mitochondria Activity in Melanoma Cells". International Journal of Molecular Sciences 22, n.º 6 (23 de marzo de 2021): 3247. http://dx.doi.org/10.3390/ijms22063247.
Texto completoHajj, Carla, Katrin Anne Becker-Flegler y Adriana Haimovitz-Friedman. "Novel mechanisms of action of classical chemotherapeutic agents on sphingolipid pathways". Biological Chemistry 396, n.º 6-7 (1 de junio de 2015): 669–79. http://dx.doi.org/10.1515/hsz-2014-0302.
Texto completoJan, Jia-Tsrong, Subroto Chatterjee y Diane E. Griffin. "Sindbis Virus Entry into Cells Triggers Apoptosis by Activating Sphingomyelinase, Leading to the Release of Ceramide". Journal of Virology 74, n.º 14 (15 de julio de 2000): 6425–32. http://dx.doi.org/10.1128/jvi.74.14.6425-6432.2000.
Texto completoInoue, Tsuyoshi, Nozomu Okino, Yoshimitsu Kakuta, Atsushi Hijikata, Hiroyuki Okano, Hatsumi M. Goda, Motohiro Tani et al. "Mechanistic Insights into the Hydrolysis and Synthesis of Ceramide by Neutral Ceramidase". Journal of Biological Chemistry 284, n.º 14 (16 de diciembre de 2008): 9566–77. http://dx.doi.org/10.1074/jbc.m808232200.
Texto completoPark, Jae-Ho y Suk Hoo Yoon. "Ceramide, a crucial functional lipid, and its metabolic regulation by acid ceramidase". Food Science and Biotechnology 19, n.º 4 (agosto de 2010): 859–64. http://dx.doi.org/10.1007/s10068-010-0122-y.
Texto completoRajah.R, Nirmal y Rufus Auxillia. "Phylogenetic Analysis of Neutral Ceramidase". International Journal of Computer Applications 108, n.º 7 (18 de diciembre de 2014): 18–23. http://dx.doi.org/10.5120/18923-0271.
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