Статті в журналах з теми "E3 LIGASE ACTIVITY"
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Pao, Kuan-Chuan, Nicola T. Wood, Axel Knebel, Karim Rafie, Mathew Stanley, Peter D. Mabbitt, Ramasubramanian Sundaramoorthy, Kay Hofmann, Daan M. F. van Aalten, and Satpal Virdee. "Activity-based E3 ligase profiling uncovers an E3 ligase with esterification activity." Nature 556, no. 7701 (April 2018): 381–85. http://dx.doi.org/10.1038/s41586-018-0026-1.
Повний текст джерелаMarblestone, Jeffrey G., K. G. Suresh Kumar, Michael J. Eddins, Craig A. Leach, David E. Sterner, Michael R. Mattern, and Benjamin Nicholson. "Novel Approach for Characterizing Ubiquitin E3 Ligase Function." Journal of Biomolecular Screening 15, no. 10 (September 23, 2010): 1220–28. http://dx.doi.org/10.1177/1087057110380456.
Повний текст джерелаLi, Qianyan, Arshdeep Kaur, Kyoko Okada, Richard J. McKenney, and JoAnne Engebrecht. "Differential requirement for BRCA1-BARD1 E3 ubiquitin ligase activity in DNA damage repair and meiosis in the Caenorhabditis elegans germ line." PLOS Genetics 19, no. 1 (January 30, 2023): e1010457. http://dx.doi.org/10.1371/journal.pgen.1010457.
Повний текст джерелаKim, Jong Hum, Seok Keun Cho, Tae Rin Oh, Moon Young Ryu, Seong Wook Yang, and Woo Taek Kim. "MPSR1 is a cytoplasmic PQC E3 ligase for eliminating emergent misfolded proteins in Arabidopsis thaliana." Proceedings of the National Academy of Sciences 114, no. 46 (October 30, 2017): E10009—E10017. http://dx.doi.org/10.1073/pnas.1713574114.
Повний текст джерелаBustos, Francisco, Sunil Mathur, Carmen Espejo-Serrano, Rachel Toth, C. James Hastie, Satpal Virdee, and Greg M. Findlay. "Activity-based probe profiling of RNF12 E3 ubiquitin ligase function in Tonne-Kalscheuer syndrome." Life Science Alliance 5, no. 11 (June 28, 2022): e202101248. http://dx.doi.org/10.26508/lsa.202101248.
Повний текст джерелаChinnam, Meenalakshmi, Chao Xu, Rati Lama, Xiaojing Zhang, Carlos D. Cedeno, Yanqing Wang, Aimee B. Stablewski, David W. Goodrich, and Xinjiang Wang. "MDM2 E3 ligase activity is essential for p53 regulation and cell cycle integrity." PLOS Genetics 18, no. 5 (May 19, 2022): e1010171. http://dx.doi.org/10.1371/journal.pgen.1010171.
Повний текст джерелаGong, Yao, and Yue Chen. "UbE3-APA: a bioinformatic strategy to elucidate ubiquitin E3 ligase activities in quantitative proteomics study." Bioinformatics 38, no. 8 (February 9, 2022): 2211–18. http://dx.doi.org/10.1093/bioinformatics/btac069.
Повний текст джерелаHorn-Ghetko, Daniel, David T. Krist, J. Rajan Prabu, Kheewoong Baek, Monique P. C. Mulder, Maren Klügel, Daniel C. Scott, Huib Ovaa, Gary Kleiger, and Brenda A. Schulman. "Ubiquitin ligation to F-box protein targets by SCF–RBR E3–E3 super-assembly." Nature 590, no. 7847 (February 3, 2021): 671–76. http://dx.doi.org/10.1038/s41586-021-03197-9.
Повний текст джерелаKelsall, Ian R., Jiazhen Zhang, Axel Knebel, J. Simon C. Arthur, and Philip Cohen. "The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells." Proceedings of the National Academy of Sciences 116, no. 27 (June 17, 2019): 13293–98. http://dx.doi.org/10.1073/pnas.1905873116.
Повний текст джерелаLi, Haoyan, Yanjia Fang, Chunyi Niu, Hengyi Cao, Ting Mi, Hong Zhu, Junying Yuan, and Jidong Zhu. "Inhibition of cIAP1 as a strategy for targeting c-MYC–driven oncogenic activity." Proceedings of the National Academy of Sciences 115, no. 40 (September 4, 2018): E9317—E9324. http://dx.doi.org/10.1073/pnas.1807711115.
Повний текст джерелаZhang, Gui, Yunfang Zhang, Luxuan Chen, Langxia Liu, and Xuejuan Gao. "E3 ubiquitin ligase-dependent regulatory mechanism of TRIM family in carcinogenesis." Cancer Insight 2, no. 1 (June 28, 2023): 102–30. http://dx.doi.org/10.58567/ci02010007.
Повний текст джерелаCerqueira, Sofia A., Min Tan, Shijun Li, Franceline Juillard, Colin E. McVey, Kenneth M. Kaye, and J. Pedro Simas. "Latency-Associated Nuclear Antigen E3 Ubiquitin Ligase Activity Impacts Gammaherpesvirus-Driven Germinal Center B Cell Proliferation." Journal of Virology 90, no. 17 (June 15, 2016): 7667–83. http://dx.doi.org/10.1128/jvi.00813-16.
Повний текст джерелаBehera, Adaitya Prasad, Pritam Naskar, Shubhangi Agarwal, Prerana Agarwal Banka, Asim Poddar, and Ajit B. Datta. "Structural insights into the nanomolar affinity of RING E3 ligase ZNRF1 for Ube2N and its functional implications." Biochemical Journal 475, no. 9 (May 9, 2018): 1569–82. http://dx.doi.org/10.1042/bcj20170909.
Повний текст джерелаLama, Rati, Samuel L. Galster, Chao Xu, Luke W. Davison, Sherry R. Chemler, and Xinjiang Wang. "Dual Targeting of MDM4 and FTH1 by MMRi71 for Induced Protein Degradation and p53-Independent Apoptosis in Leukemia Cells." Molecules 27, no. 22 (November 8, 2022): 7665. http://dx.doi.org/10.3390/molecules27227665.
Повний текст джерелаChu, Y., and X. Yang. "SUMO E3 ligase activity of TRIM proteins." Oncogene 30, no. 9 (October 25, 2010): 1108–16. http://dx.doi.org/10.1038/onc.2010.462.
Повний текст джерелаWalden, Helen, and R. Julio Martinez-Torres. "Regulation of Parkin E3 ubiquitin ligase activity." Cellular and Molecular Life Sciences 69, no. 18 (April 19, 2012): 3053–67. http://dx.doi.org/10.1007/s00018-012-0978-5.
Повний текст джерелаChinnam, Meenalakshmi, Rati Lama, Chao Xu, Xiaojing Zhang, Carlos Cedeno, Yanqing Wang, Aimee B. Stablewski, David W. Goodrich, and Xinjiang Wang. "Abstract 2606: Requirement of MDM2 E3 ligase activity for regulating p53 during normal development, cell cycle regulation and genome integrity." Cancer Research 83, no. 7_Supplement (April 4, 2023): 2606. http://dx.doi.org/10.1158/1538-7445.am2023-2606.
Повний текст джерелаNurieva, Roza, Junmei Wang, and Andrei Alekseev. "Essential role of E3 ubiquitin ligase activity of GRAIL in T cell functions (P1111)." Journal of Immunology 190, no. 1_Supplement (May 1, 2013): 122.7. http://dx.doi.org/10.4049/jimmunol.190.supp.122.7.
Повний текст джерелаLin, You-Sheng, Yung-Chi Chang, Ting-Yu Lai, Chih-Yuan Lee, Tsung-Hsien Chuang, and Li-Chung Hsu. "The role of novel E3 ubiquitin ligase in the regulation of TLR3 signaling pathway." Journal of Immunology 204, no. 1_Supplement (May 1, 2020): 226.26. http://dx.doi.org/10.4049/jimmunol.204.supp.226.26.
Повний текст джерелаSicari, Daria, Janine Weber, Elena Maspero, and Simona Polo. "The NEDD4 ubiquitin E3 ligase: a snapshot view of its functional activity and regulation." Biochemical Society Transactions 50, no. 1 (February 7, 2022): 473–85. http://dx.doi.org/10.1042/bst20210731.
Повний текст джерелаBalaji, Vishnu, and Thorsten Hoppe. "Regulation of E3 ubiquitin ligases by homotypic and heterotypic assembly." F1000Research 9 (February 6, 2020): 88. http://dx.doi.org/10.12688/f1000research.21253.1.
Повний текст джерелаSantini, S., V. Stagni, R. Giambruno, G. Fianco, A. Di Benedetto, M. Mottolese, M. Pellegrini, and D. Barilà. "ATM kinase activity modulates ITCH E3-ubiquitin ligase activity." Oncogene 33, no. 9 (February 25, 2013): 1113–23. http://dx.doi.org/10.1038/onc.2013.52.
Повний текст джерелаEldin, Patrick, Laura Papon, Alexandra Oteiza, Emiliana Brocchi, T. Glen Lawson, and Nadir Mechti. "TRIM22 E3 ubiquitin ligase activity is required to mediate antiviral activity against encephalomyocarditis virus." Journal of General Virology 90, no. 3 (March 1, 2009): 536–45. http://dx.doi.org/10.1099/vir.0.006288-0.
Повний текст джерелаSpratt, Donald E., Helen Walden, and Gary S. Shaw. "RBR E3 ubiquitin ligases: new structures, new insights, new questions." Biochemical Journal 458, no. 3 (February 28, 2014): 421–37. http://dx.doi.org/10.1042/bj20140006.
Повний текст джерелаLazzari, Elisa, Medhat El-Halawany, Matteo De March, Floriana Valentino, Francesco Cantatore, Chiara Migliore, Silvia Onesti, and Germana Meroni. "Analysis of the Zn-Binding Domains of TRIM32, the E3 Ubiquitin Ligase Mutated in Limb Girdle Muscular Dystrophy 2H." Cells 8, no. 3 (March 16, 2019): 254. http://dx.doi.org/10.3390/cells8030254.
Повний текст джерелаRiling, Christopher, Hari Kamadurai, Suresh Kumar, Claire E. O'Leary, Kuen-Phon Wu, Erica E. Manion, Mingjie Ying, Brenda A. Schulman, and Paula M. Oliver. "Itch WW Domains Inhibit Its E3 Ubiquitin Ligase Activity by Blocking E2-E3 Ligase Trans-thiolation." Journal of Biological Chemistry 290, no. 39 (August 5, 2015): 23875–87. http://dx.doi.org/10.1074/jbc.m115.649269.
Повний текст джерелаGorelik, Maryna, and Sachdev S. Sidhu. "Regulation of SCF E3 ligase activity by Cand1." Biotarget 2 (June 2018): 10. http://dx.doi.org/10.21037/biotarget.2018.05.03.
Повний текст джерелаEggleston, Angela K. "E3 ligase activity and suppression of breast cancer." Nature Structural & Molecular Biology 11, no. 1 (January 2004): 8. http://dx.doi.org/10.1038/nsmb0104-8.
Повний текст джерелаPichler, Andrea, Andreas Gast, Jacob S. Seeler, Anne Dejean, and Frauke Melchior. "The Nucleoporin RanBP2 Has SUMO1 E3 Ligase Activity." Cell 108, no. 1 (January 2002): 109–20. http://dx.doi.org/10.1016/s0092-8674(01)00633-x.
Повний текст джерелаKane, Lesley A., Michael Lazarou, Adam I. Fogel, Yan Li, Koji Yamano, Shireen A. Sarraf, Soojay Banerjee, and Richard J. Youle. "PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity." Journal of Cell Biology 205, no. 2 (April 21, 2014): 143–53. http://dx.doi.org/10.1083/jcb.201402104.
Повний текст джерелаStevens, Rebecca V., Diego Esposito, and Katrin Rittinger. "Characterisation of class VI TRIM RING domains: linking RING activity to C-terminal domain identity." Life Science Alliance 2, no. 3 (April 26, 2019): e201900295. http://dx.doi.org/10.26508/lsa.201900295.
Повний текст джерелаLÖSCHER, Marlies, Klaus FORTSCHEGGER, Gustav RITTER, Martina WOSTRY, Regina VOGLAUER, Johannes A. SCHMID, Steven WATTERS та ін. "Interaction of U-box E3 ligase SNEV with PSMB4, the β7 subunit of the 20 S proteasome". Biochemical Journal 388, № 2 (24 травня 2005): 593–603. http://dx.doi.org/10.1042/bj20041517.
Повний текст джерелаGoldenberg, Seth J., Jeffrey G. Marblestone, Michael R. Mattern, and Benjamin Nicholson. "Strategies for the identification of ubiquitin ligase inhibitors." Biochemical Society Transactions 38, no. 1 (January 19, 2010): 132–36. http://dx.doi.org/10.1042/bst0380132.
Повний текст джерелаMedina-Medina, Ixaura, Paola García-Beltrán, Ignacio de la Mora-de la Mora, Jesús Oria-Hernández, Guy Millot, Robin Fahraeus, Horacio Reyes-Vivas, José G. Sampedro, and Vanesa Olivares-Illana. "Allosteric Interactions byp53mRNA Govern HDM2 E3 Ubiquitin Ligase Specificity under Different Conditions." Molecular and Cellular Biology 36, no. 16 (May 23, 2016): 2195–205. http://dx.doi.org/10.1128/mcb.00113-16.
Повний текст джерелаYin, Chenlei, Ru Zhang, Yongyu Xu, Qiuyan Chen та Xin Xie. "Intact MDM2 E3 ligase activity is required for the cytosolic localization and function of β-arrestin2". Molecular Biology of the Cell 22, № 9 (травень 2011): 1608–16. http://dx.doi.org/10.1091/mbc.e10-09-0779.
Повний текст джерелаCombs, Lauren R., Jacob Combs, Robert McKenna, and Zsolt Toth. "Protein Degradation by Gammaherpesvirus RTAs: More Than Just Viral Transactivators." Viruses 15, no. 3 (March 11, 2023): 730. http://dx.doi.org/10.3390/v15030730.
Повний текст джерелаWei, Wei, Jian-ye Chen, Ze-xiang Zeng, Jian-fei Kuang, Wang-jin Lu, and Wei Shan. "The Ubiquitin E3 Ligase MaLUL2 Is Involved in High Temperature-Induced Green Ripening in Banana Fruit." International Journal of Molecular Sciences 21, no. 24 (December 9, 2020): 9386. http://dx.doi.org/10.3390/ijms21249386.
Повний текст джерелаOkada, Maiko, Fumiaki Ohtake, Hiroyuki Nishikawa, Wenwen Wu, Yasushi Saeki, Keiji Takana та Tomohiko Ohta. "Liganded ERα Stimulates the E3 Ubiquitin Ligase Activity of UBE3C to Facilitate Cell Proliferation". Molecular Endocrinology 29, № 11 (1 листопада 2015): 1646–57. http://dx.doi.org/10.1210/me.2015-1125.
Повний текст джерелаKawai, Hidehiko, Dmitri Wiederschain, and Zhi-Min Yuan. "Critical Contribution of the MDM2 Acidic Domain to p53 Ubiquitination." Molecular and Cellular Biology 23, no. 14 (July 15, 2003): 4939–47. http://dx.doi.org/10.1128/mcb.23.14.4939-4947.2003.
Повний текст джерелаYang, Cheng-Wei, Yue-Zhi Lee, Hsing-Yu Hsu, Guan-Hao Zhao, and Shiow-Ju Lee. "Tyrphostin AG1024 Suppresses Coronaviral Replication by Downregulating JAK1 via an IR/IGF-1R Independent Proteolysis Mediated by Ndfip1/2_NEDD4-like E3 Ligase Itch." Pharmaceuticals 15, no. 2 (February 17, 2022): 241. http://dx.doi.org/10.3390/ph15020241.
Повний текст джерелаMalonis, Ryan J., Wenxiang Fu, Mark J. Jelcic, Marae Thompson, Brian S. Canter, Mary Tsikitis, Francisco J. Esteva та Irma Sánchez. "RNF11 sequestration of the E3 ligase SMURF2 on membranes antagonizes SMAD7 down-regulation of transforming growth factor β signaling". Journal of Biological Chemistry 292, № 18 (14 березня 2017): 7435–51. http://dx.doi.org/10.1074/jbc.m117.783662.
Повний текст джерелаBossuyt, Stijn N. V., A. Mattijs Punt, Ilona J. de Graaf, Janny van den Burg, Mark G. Williams, Helen Heussler, Ype Elgersma, and Ben Distel. "Loss of nuclear UBE3A activity is the predominant cause of Angelman syndrome in individuals carrying UBE3A missense mutations." Human Molecular Genetics 30, no. 6 (February 19, 2021): 430–42. http://dx.doi.org/10.1093/hmg/ddab050.
Повний текст джерелаElliott, Joanne, Oonagh T. Lynch, Yvonne Suessmuth, Ping Qian, Caroline R. Boyd, James F. Burrows, Richard Buick, et al. "Respiratory Syncytial Virus NS1 Protein Degrades STAT2 by Using the Elongin-Cullin E3 Ligase." Journal of Virology 81, no. 7 (January 24, 2007): 3428–36. http://dx.doi.org/10.1128/jvi.02303-06.
Повний текст джерелаMoses, Niko, Mu Zhang, Jheng-Yu Wu, Chen Hu, Shengyan Xiang, Xinran Geng, Yue Chen, et al. "HDAC6 Regulates Radiosensitivity of Non-Small Cell Lung Cancer by Promoting Degradation of Chk1." Cells 9, no. 10 (October 4, 2020): 2237. http://dx.doi.org/10.3390/cells9102237.
Повний текст джерелаLin, Yachun, Qinli Hu, Jia Zhou, Weixiao Yin, Deqiang Yao, Yuanyuan Shao, Yao Zhao, et al. "Phytophthora sojae effector Avr1d functions as an E2 competitor and inhibits ubiquitination activity of GmPUB13 to facilitate infection." Proceedings of the National Academy of Sciences 118, no. 10 (March 3, 2021): e2018312118. http://dx.doi.org/10.1073/pnas.2018312118.
Повний текст джерелаMintis, Dimitris G., Anastasia Chasapi, Konstantinos Poulas, George Lagoumintzis, and Christos T. Chasapis. "Assessing the Direct Binding of Ark-Like E3 RING Ligases to Ubiquitin and Its Implication on Their Protein Interaction Network." Molecules 25, no. 20 (October 19, 2020): 4787. http://dx.doi.org/10.3390/molecules25204787.
Повний текст джерелаHong, Jeongkwan, Minho Won, and Hyunju Ro. "The Molecular and Pathophysiological Functions of Members of the LNX/PDZRN E3 Ubiquitin Ligase Family." Molecules 25, no. 24 (December 15, 2020): 5938. http://dx.doi.org/10.3390/molecules25245938.
Повний текст джерелаTracz, Michał, Ireneusz Górniak, Andrzej Szczepaniak, and Wojciech Białek. "E3 Ubiquitin Ligase SPL2 Is a Lanthanide-Binding Protein." International Journal of Molecular Sciences 22, no. 11 (May 27, 2021): 5712. http://dx.doi.org/10.3390/ijms22115712.
Повний текст джерелаUchida, Daisuke, Shigetsugu Hatakeyama, Akemi Matsushima, Hongwei Han, Satoshi Ishido, Hak Hotta, Jun Kudoh, et al. "AIRE Functions As an E3 Ubiquitin Ligase." Journal of Experimental Medicine 199, no. 2 (January 19, 2004): 167–72. http://dx.doi.org/10.1084/jem.20031291.
Повний текст джерелаLazarou, Michael, Derek P. Narendra, Seok Min Jin, Ephrem Tekle, Soojay Banerjee, and Richard J. Youle. "PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding." Journal of Cell Biology 200, no. 2 (January 14, 2013): 163–72. http://dx.doi.org/10.1083/jcb.201210111.
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