Artículos de revistas sobre el tema "FBXO24"
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Chen, Wei, Sheng Xiong, Jin Li, Xiuying Li, Yuan Liu, Chunbin Zou y Rama K. Mallampalli. "The Ubiquitin E3 Ligase SCF-FBXO24 Recognizes Deacetylated Nucleoside Diphosphate Kinase A To Enhance Its Degradation". Molecular and Cellular Biology 35, n.º 6 (12 de enero de 2015): 1001–13. http://dx.doi.org/10.1128/mcb.01185-14.
Texto completoYuan, Lamei, Zhi Song, Xiong Deng, Zhijian Yang, Yan Yang, Yi Guo, Hongwei Lu y Hao Deng. "Genetic Analysis of FBXO2, FBXO6, FBXO12, and FBXO41 Variants in Han Chinese Patients with Sporadic Parkinson’s Disease". Neuroscience Bulletin 33, n.º 5 (24 de marzo de 2017): 510–14. http://dx.doi.org/10.1007/s12264-017-0122-5.
Texto completoChen, Wei, Denghui Gao, Long Xie, Anling Wang, Hui Zhao, Chaowan Guo, Yunqi Sun, Yanfeng Nie, An Hong y Sheng Xiong. "SCF-FBXO24 regulates cell proliferation by mediating ubiquitination and degradation of PRMT6". Biochemical and Biophysical Research Communications 530, n.º 1 (septiembre de 2020): 75–81. http://dx.doi.org/10.1016/j.bbrc.2020.06.007.
Texto completoZhang, Yuan-Meng, Ling-Bing Meng, Si-Jun Yu y Dong-Xing Ma. "Identification of potential crucial genes in monocytes for atherosclerosis using bioinformatics analysis". Journal of International Medical Research 48, n.º 4 (abril de 2020): 030006052090927. http://dx.doi.org/10.1177/0300060520909277.
Texto completoAngeli, Franca, Russell Wyborski, Bill Chen, Rama Mallampalli y Michael Lark. "P157 FBXO3-FBXL2 AXIS MODULATORS AS A NOVEL CLASS OF ORAL SMALL MOLECULE COMPOUNDS FOR THE TREATMENT OF CROHN’S DISEASE". Inflammatory Bowel Diseases 26, Supplement_1 (enero de 2020): S6. http://dx.doi.org/10.1093/ibd/zaa010.014.
Texto completoMasle-Farquhar, Etienne, Amanda Russell, Yangguang Li, Fen Zhu, Lixin Rui, Robert Brink y Christopher C. Goodnow. "Loss-of-function of Fbxo10, encoding a post-translational regulator of BCL2 in lymphomas, has no discernible effect on BCL2 or B lymphocyte accumulation in mice". PLOS ONE 16, n.º 4 (29 de abril de 2021): e0237830. http://dx.doi.org/10.1371/journal.pone.0237830.
Texto completoManfiolli, Adriana O., Ana Leticia G. C. Maragno, Munira M. A. Baqui, Sami Yokoo, Felipe R. Teixeira, Eduardo B. Oliveira y Marcelo D. Gomes. "FBXO25-associated Nuclear Domains: A Novel Subnuclear Structure". Molecular Biology of the Cell 19, n.º 5 (mayo de 2008): 1848–61. http://dx.doi.org/10.1091/mbc.e07-08-0815.
Texto completoGuo, Fengjie, Xiaoyu Jiang, Domenico Roberti, Lixin Rui y Izidore S. Lossos. "FBXO10 Targets HGAL for Degradation". Blood 126, n.º 23 (3 de diciembre de 2015): 3904. http://dx.doi.org/10.1182/blood.v126.23.3904.3904.
Texto completoQie, Shuo. "The E3 Ubiquitin Ligase Fbxo4 Functions as a Tumor Suppressor: Its Biological Importance and Therapeutic Perspectives". Cancers 14, n.º 9 (25 de abril de 2022): 2133. http://dx.doi.org/10.3390/cancers14092133.
Texto completoQie, Shuo. "The E3 Ubiquitin Ligase Fbxo4 Functions as a Tumor Suppressor: Its Biological Importance and Therapeutic Perspectives". Cancers 14, n.º 9 (25 de abril de 2022): 2133. http://dx.doi.org/10.3390/cancers14092133.
Texto completoWong, Siau Yen, Peiran Lu, Lei Wu, Mckale Montgomery, Winyoo Chowanadisai, Edralin Lucas, Brenda Smith, Stephen Clarke y Dingbo Lin. "Hepatic F-box Only Protein 2 (FBXO2) Might Not Mediate Glucose Homeostasis in Obese Diabetic Mice". Current Developments in Nutrition 4, Supplement_2 (29 de mayo de 2020): 1281. http://dx.doi.org/10.1093/cdn/nzaa058_039.
Texto completoChang, Shu-Chun, Chin-Sheng Hung, Bo-Xiang Zhang, Tsung-Han Hsieh, Wayne Hsu y Jeak Ling Ding. "A Novel Signature of CCNF-Associated E3 Ligases Collaborate and Counter Each Other in Breast Cancer". Cancers 13, n.º 12 (8 de junio de 2021): 2873. http://dx.doi.org/10.3390/cancers13122873.
Texto completoLee, Eric K., Zhaorui Lian, Kurt D'Andrea, Richard Letrero, WeiQi Sheng, Shujing Liu, J. Nathaniel Diehl et al. "The FBXO4 Tumor Suppressor Functions as a Barrier to BrafV600E-Dependent Metastatic Melanoma". Molecular and Cellular Biology 33, n.º 22 (9 de septiembre de 2013): 4422–33. http://dx.doi.org/10.1128/mcb.00706-13.
Texto completoDhar, Ruby, Goura Kishor Rath y Subhradip Karmakar. "FBXO4 as a novel ubiquitin ligase that targets Cyclin D in the pathogenesis of breast cancer." Journal of Clinical Oncology 37, n.º 15_suppl (20 de mayo de 2019): e14722-e14722. http://dx.doi.org/10.1200/jco.2019.37.15_suppl.e14722.
Texto completoLin, T. B., M. C. Hsieh, C. Y. Lai, J. K. Cheng, Y. P. Chau, T. Ruan, G. D. Chen y H. Y. Peng. "Fbxo3-Dependent Fbxl2 Ubiquitination Mediates Neuropathic Allodynia through the TRAF2/TNIK/GluR1 Cascade". Journal of Neuroscience 35, n.º 50 (16 de diciembre de 2015): 16545–60. http://dx.doi.org/10.1523/jneurosci.2301-15.2015.
Texto completoAkiyama, Mari. "Roles of Two F-Box Proteins: FBXL14 in the Periosteum and FBXW2 at Elastic Fibers". Osteology 3, n.º 1 (5 de enero de 2023): 1–10. http://dx.doi.org/10.3390/osteology3010001.
Texto completoSelander, Erik, Jan Heuschele y Ann I. Larsson. "Hydrodynamic properties and distribution of bait downstream of a zooplankton trap". Journal of Plankton Research 39, n.º 6 (2 de mayo de 2017): 1020–27. http://dx.doi.org/10.1093/plankt/fbx024.
Texto completoYoshida, Yukiko, Sayaka Yasuda, Toshiharu Fujita, Maho Hamasaki, Arisa Murakami, Junko Kawawaki, Kazuhiro Iwai et al. "Ubiquitination of exposed glycoproteins by SCFFBXO27 directs damaged lysosomes for autophagy". Proceedings of the National Academy of Sciences 114, n.º 32 (25 de julio de 2017): 8574–79. http://dx.doi.org/10.1073/pnas.1702615114.
Texto completoZhou, Huijun, Chong Zeng, Jie Liu, Haijun Luo y Wei Huang. "F-Box Protein 43, Stabilized by N6-Methyladenosine Methylation, Enhances Hepatocellular Carcinoma Cell Growth and Invasion via Promoting p53 Degradation in a Ubiquitin Conjugating Enzyme E2 C -Dependent Manner". Cancers 15, n.º 3 (2 de febrero de 2023): 957. http://dx.doi.org/10.3390/cancers15030957.
Texto completoDeng, Chao, Hongzhi Li y Qingmin Li. "F-box protein 17 promotes glioma progression by regulating glycolysis pathway". Bioscience, Biotechnology, and Biochemistry 86, n.º 4 (19 de enero de 2022): 455–63. http://dx.doi.org/10.1093/bbb/zbac008.
Texto completoMo, Angela, Linda Ya-Ting Chang, Gerben Duns, Xuan Wang, Gregg Morin, Tammy Lau, Rod Docking et al. "Elucidating the Mechanisms of Leukemogenesis Driven By FBXO11 Depletion". Blood 138, Supplement 1 (5 de noviembre de 2021): 3328. http://dx.doi.org/10.1182/blood-2021-145384.
Texto completoHabel, Nadia, Najla El-Hachem, Frédéric Soysouvanh, Hanene Hadhiri-Bzioueche, Serena Giuliano, Sophie Nguyen, Pavel Horák et al. "FBXO32 links ubiquitination to epigenetic reprograming of melanoma cells". Cell Death & Differentiation 28, n.º 6 (18 de enero de 2021): 1837–48. http://dx.doi.org/10.1038/s41418-020-00710-x.
Texto completoSaiga, Toru, Takaichi Fukuda, Masaki Matsumoto, Hirobumi Tada, Hirotaka James Okano, Hideyuki Okano y Keiichi I. Nakayama. "Fbxo45 Forms a Novel Ubiquitin Ligase Complex and Is Required for Neuronal Development". Molecular and Cellular Biology 29, n.º 13 (27 de abril de 2009): 3529–43. http://dx.doi.org/10.1128/mcb.00364-09.
Texto completoLai, C. Y., Y. C. Ho, M. C. Hsieh, H. H. Wang, J. K. Cheng, Y. P. Chau y H. Y. Peng. "Spinal Fbxo3-Dependent Fbxl2 Ubiquitination of Active Zone Protein RIM1 Mediates Neuropathic Allodynia through CaV2.2 Activation". Journal of Neuroscience 36, n.º 37 (14 de septiembre de 2016): 9722–38. http://dx.doi.org/10.1523/jneurosci.1732-16.2016.
Texto completoWang, Ning, Qian Song, Hai Yu y Gang Bao. "Overexpression of FBXO17 Promotes the Proliferation, Migration and Invasion of Glioma Cells Through the Akt/GSK-3β/Snail Pathway". Cell Transplantation 30 (1 de enero de 2021): 096368972110073. http://dx.doi.org/10.1177/09636897211007395.
Texto completoChoppara, Srinadh, Sunil K. Malonia, Ganga Sankaran, Michael R. Green y Manas Kumar Santra. "Degradation of FBXO31 by APC/C is regulated by AKT- and ATM-mediated phosphorylation". Proceedings of the National Academy of Sciences 115, n.º 5 (17 de enero de 2018): 998–1003. http://dx.doi.org/10.1073/pnas.1705954115.
Texto completoSahasrabuddhe, Anagh Anant, Xiaofei Chen, Kaiyu Ma, Rui Wu, Richa Kapoor, Rishi Raj Chhipa, Xiao Zhang et al. "A Novel FBXO45-Gef-H1 Axis Controls Oncogenic Signaling in B-Cell Lymphoma". Blood 138, Supplement 1 (5 de noviembre de 2021): 711. http://dx.doi.org/10.1182/blood-2021-151245.
Texto completoBrewer, Kelly, Isabel Nip, Justin Bellizzi, Jessica Costa-Guda y Andrew Arnold. "Molecular analysis of cyclin D1 modulators PRKN and FBX4 as candidate tumor suppressors in sporadic parathyroid adenomas". Endocrine Connections 10, n.º 3 (marzo de 2021): 302–8. http://dx.doi.org/10.1530/ec-21-0055.
Texto completoPighi, Chiara, Mara Compagno, Qi Wang, Taek-Chin Cheong, Teresa Poggio, Fernanda Langellotto, Paola Francia di Celle, Alberto Zamò y Roberto Chiarle. "FBXO11, a Regulator of BCL6 Stability, Is Recurrently Mutated in Burkitt Lymphoma". Blood 126, n.º 23 (3 de diciembre de 2015): 3673. http://dx.doi.org/10.1182/blood.v126.23.3673.3673.
Texto completoLi, Yunfeng, Kai Jin, Eric Bunker, Xiaojuan Zhang, Xuemei Luo, Xuedong Liu y Bing Hao. "Structural basis of the phosphorylation-independent recognition of cyclin D1 by the SCFFBXO31 ubiquitin ligase". Proceedings of the National Academy of Sciences 115, n.º 2 (26 de diciembre de 2017): 319–24. http://dx.doi.org/10.1073/pnas.1708677115.
Texto completoPighi, Chiara, Taek-Chin Cheong, Mara Compagno, Enrico Patrucco, Maddalena Arigoni, Martina Olivero, Qi Wang et al. "Frequent mutations of FBXO11 highlight BCL6 as a therapeutic target in Burkitt lymphoma". Blood Advances 5, n.º 23 (8 de diciembre de 2021): 5239–57. http://dx.doi.org/10.1182/bloodadvances.2021005682.
Texto completoMatsushima, Norio, Shintaro Takatsuka, Hiroki Miyashita y Robert H. Kretsinger. "Leucine Rich Repeat Proteins: Sequences, Mutations, Structures and Diseases". Protein & Peptide Letters 26, n.º 2 (20 de febrero de 2019): 108–31. http://dx.doi.org/10.2174/0929866526666181208170027.
Texto completoXu, Peng, Daniel C. Scott, Xing Tang, Yu Yao, Yong-Dong Wang, Wenjian Bi, Lance E. Palmer et al. "FBXO11 Activates Erythroid Gene Transcription By Degrading Heterochromatin-Associated Protein BAHD1". Blood 132, Supplement 1 (29 de noviembre de 2018): 529. http://dx.doi.org/10.1182/blood-2018-99-117362.
Texto completoHughes, David C., Leslie M. Baehr, Julia R. Driscoll, Sarah A. Lynch, David S. Waddell y Sue C. Bodine. "Identification and characterization of Fbxl22, a novel skeletal muscle atrophy-promoting E3 ubiquitin ligase". American Journal of Physiology-Cell Physiology 319, n.º 4 (1 de octubre de 2020): C700—C719. http://dx.doi.org/10.1152/ajpcell.00253.2020.
Texto completoMalonia, Sunil K., Parul Dutta, Manas Kumar Santra y Michael R. Green. "F-box protein FBXO31 directs degradation of MDM2 to facilitate p53-mediated growth arrest following genotoxic stress". Proceedings of the National Academy of Sciences 112, n.º 28 (29 de junio de 2015): 8632–37. http://dx.doi.org/10.1073/pnas.1510929112.
Texto completoLim, Ji Ye, Eunju Kim, Collin M. Douglas, Marvin Wirianto, Chorong Han, Kaori Ono, Sun Young Kim et al. "The circadian E3 ligase FBXL21 regulates myoblast differentiation and sarcomere architecture via MYOZ1 ubiquitination and NFAT signaling". PLOS Genetics 18, n.º 12 (27 de diciembre de 2022): e1010574. http://dx.doi.org/10.1371/journal.pgen.1010574.
Texto completoCleveland, Beth M. y Gregory M. Weber. "Effects of insulin-like growth factor-I, insulin, and leucine on protein turnover and ubiquitin ligase expression in rainbow trout primary myocytes". American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 298, n.º 2 (febrero de 2010): R341—R350. http://dx.doi.org/10.1152/ajpregu.00516.2009.
Texto completoZhang, Liping, Zihong Chen, Ying Wang, David J. Tweardy y William E. Mitch. "Stat3 activation induces insulin resistance via a muscle-specific E3 ubiquitin ligase Fbxo40". American Journal of Physiology-Endocrinology and Metabolism 318, n.º 5 (1 de mayo de 2020): E625—E635. http://dx.doi.org/10.1152/ajpendo.00480.2019.
Texto completoAkiyama, Mari. "Characterization of the F-box Proteins FBXW2 and FBXL14 in the Initiation of Bone Regeneration in Transplants given to Nude Mice". Open Biomedical Engineering Journal 12, n.º 1 (18 de octubre de 2018): 75–89. http://dx.doi.org/10.2174/1874120701812010075.
Texto completoSchieber, Michael y John D. Crispino. "FBXO11 Is a Candidate Tumor Suppressor in the Transformation of MDS to Secondary AML". Blood 134, Supplement_1 (13 de noviembre de 2019): 4217. http://dx.doi.org/10.1182/blood-2019-124007.
Texto completoSchneider, Christof, Ning Kon, Letizia Amadori, Qiong Shen, Friederike H. Schwartz, Benjamin Tischler, Marion Bossennec et al. "FBXO11 inactivation leads to abnormal germinal-center formation and lymphoproliferative disease". Blood 128, n.º 5 (4 de agosto de 2016): 660–66. http://dx.doi.org/10.1182/blood-2015-11-684357.
Texto completoCleveland, Beth M. y Jason P. Evenhuis. "Molecular characterization of atrogin-1/F-box protein-32 (FBXO32) and F-box protein-25 (FBXO25) in rainbow trout (Oncorhynchus mykiss): Expression across tissues in response to feed deprivation". Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 157, n.º 3 (noviembre de 2010): 248–57. http://dx.doi.org/10.1016/j.cbpb.2010.06.010.
Texto completoAngeli, Franca, Russell Wyborski, Bill Chen, Rama Mallampalli y Michael Lark. "P157 FBXO3-FBXL2 AXIS MODULATORS AS A NOVEL CLASS OF ORAL SMALL MOLECULE COMPOUNDS FOR THE TREATMENT OF CROHN’S DISEASE". Gastroenterology 158, n.º 3 (febrero de 2020): S9—S10. http://dx.doi.org/10.1053/j.gastro.2019.11.061.
Texto completoFang, Xiaoguang, Wenchao Zhou, Qiulian Wu, Zhi Huang, Yu Shi, Kailin Yang, Cong Chen et al. "Deubiquitinase USP13 maintains glioblastoma stem cells by antagonizing FBXL14-mediated Myc ubiquitination". Journal of Experimental Medicine 214, n.º 1 (6 de diciembre de 2016): 245–67. http://dx.doi.org/10.1084/jem.20151673.
Texto completoGao, Yu, Xinyu Xiao, Jing Luo, Jianwei Wang, Qiling Peng, Jing Zhao, Ning Jiang y Yong Zhao. "E3 Ubiquitin Ligase FBXO3 Drives Neuroinflammation to Aggravate Cerebral Ischemia/Reperfusion Injury". International Journal of Molecular Sciences 23, n.º 21 (7 de noviembre de 2022): 13648. http://dx.doi.org/10.3390/ijms232113648.
Texto completoWatanabe, Koki, Kanae Yumimoto y Keiichi I. Nakayama. "FBXO21 mediates the ubiquitylation and proteasomal degradation of EID1". Genes to Cells 20, n.º 8 (18 de junio de 2015): 667–74. http://dx.doi.org/10.1111/gtc.12260.
Texto completoCai, Lili, Liang Liu, Lihui Li y Lijun Jia. "SCFFBXO28-mediated self-ubiquitination of FBXO28 promotes its degradation". Cellular Signalling 65 (enero de 2020): 109440. http://dx.doi.org/10.1016/j.cellsig.2019.109440.
Texto completoJiang, Gui-Yang, Xiu-Peng Zhang, Liang Wang, Xu-Yong Lin, Juan-Han Yu, En-Hua Wang y Yong Zhang. "FBXO25 promotes cell proliferation, invasion, and migration of NSCLC". Tumor Biology 37, n.º 10 (5 de septiembre de 2016): 14311–19. http://dx.doi.org/10.1007/s13277-016-5298-1.
Texto completoRen, Jun, Mingming Sun, Hao Zhou, Amir Ajoolabady, Yuan Zhou, Jun Tao, James R. Sowers y Yingmei Zhang. "FUNDC1 interacts with FBXL2 to govern mitochondrial integrity and cardiac function through an IP3R3-dependent manner in obesity". Science Advances 6, n.º 38 (septiembre de 2020): eabc8561. http://dx.doi.org/10.1126/sciadv.abc8561.
Texto completoLiu, Lin, Kun Liu, Yanzhe Yan, Zhuangzhuang Chu, Yi Tang y Chunbo Tang. "Two Transcripts of FBXO5 Promote Migration and Osteogenic Differentiation of Human Periodontal Ligament Mesenchymal Stem Cells". BioMed Research International 2018 (2018): 1–12. http://dx.doi.org/10.1155/2018/7849294.
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