Добірка наукової літератури з теми "E3 LIGASE ACTIVITY"
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Статті в журналах з теми "E3 LIGASE ACTIVITY"
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 джерелаДисертації з теми "E3 LIGASE ACTIVITY"
Dickens, Michael. "Small molecule inhibitors of Mdm2 E3 ubiquitin ligase activity." Thesis, University of Nottingham, 2011. http://eprints.nottingham.ac.uk/11960/.
Повний текст джерелаZANCHETTA, MELANIA EVA. "BRAF35 as target of MID1/TRIM18 E3 ligase activity." Doctoral thesis, Università degli Studi di Trieste, 2016. http://hdl.handle.net/11368/2908069.
Повний текст джерелаFu, Wei. "Regulation of FOXO stability and activity by MDM2 E3 ligase." [Tampa, Fla] : University of South Florida, 2007. http://purl.fcla.edu/usf/dc/et/SFE0002222.
Повний текст джерелаPao, Kuan-Chuan. "Design and synthesis of an E3 ligase activity-based probe and its application for the discovery of a new class of E3 ligase." Thesis, University of Dundee, 2018. https://discovery.dundee.ac.uk/en/studentTheses/6239e172-60b3-47c3-81e1-f4b0a577f1a4.
Повний текст джерелаKoliopoulos, Marios Grigorios. "Structural and functional basis for TRIM25 E3 ligase catalytic activity and NS1-mediated suppression." Thesis, University College London (University of London), 2017. http://discovery.ucl.ac.uk/10038260/.
Повний текст джерелаValentini, E. "UNDERSTANDING THE CATALYTIC MECHANISMS OF UBIQUITIN-E3 LIGASES." Doctoral thesis, Università degli Studi di Milano, 2016. http://hdl.handle.net/2434/354478.
Повний текст джерелаFurlan, Giulia [Verfasser]. "Phosphorylation of the E3 ubiquitin ligase PUB22 controls its ubiquitination activity to dampen the immune response / Giulia Furlan." Halle, 2017. http://d-nb.info/1141177102/34.
Повний текст джерелаFoster, Benjamin. "An in vitro biochemical investigation into the conformation, binding and E3-ubiquitin ligase activity of mammalian UHRF1 with reconstituted chromatin." Thesis, Imperial College London, 2017. http://hdl.handle.net/10044/1/55875.
Повний текст джерелаGao, Chengzhuo. "Mechanisms Underlying the Regulation and Functions of HDAC7." Case Western Reserve University School of Graduate Studies / OhioLINK, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=case1213890889.
Повний текст джерелаCourivaud, Thomas. "Caractérisation d'un nouveau mécanisme d'action de la E3 ubiquitine ligase WWP1 et régulation de son activité dans la cancérogenèse." Thesis, Paris 6, 2015. http://www.theses.fr/2015PA066300/document.
Повний текст джерелаThe TGF-β pathway plays a biphasic role during cancerogenesis. My laboratory identified a new protein, WWP1, as a negative regulator of TGF-β signaling. WWP1 is an E3 ubiquitin ligase that triggers polyubiquitination and degradation of TGF-β type I receptor. A genomic amplification of WWP1 is found in a large portion of mammary and prostatic tumors, suggesting a key role for WWP1 during carcinogenesis related to TGF-β. My thesis project was to determine the regulation of the catalytic activity of WWP1 and a new molecular mechanism of action of WWP1 whose deregulation can be implicated in cancerogenesis. My results indicate that at steady states, WWP1 is monoubiquitinated, its polyubiquitination activity being silenced due to the inhibitory effects of C2 or/and WW domains on its Hect domain. In presence of substrates, WWP1 is « opened » and induces polyubiquitination and degradation of its substrates. Moreover, a WWP1 mutation found in prostate cancer disrupts this regulatory mechanism. It possesses an increased ligase activity towards itself and its substrates, which leads to the attenuation of TGF-β cytostatic signaling, a consequence that could conceivably confer tumorigenic properties to WWP1. We also identified STARD13 as a novel WWP1 interacting partner. STARD13 has a RhoGAP activity, and is considered as a tumor suppressor. We have shown that STARD13 mediates the association of WWP1 with the GTPase RhoA, ultimately leading to RhoA polyubiquitination and degradation. Interestingly, the WWP1/STARD13 complex is involved in the actin cytoskeleton rearrangement by preferentially targeting the active form of RhoA for degradation. These results reveal a previously unrecognized role for WWP1, which could play a key role in the migration of cancer cells during metastasis. Characterization of new regulation and action mechanisms for WWP1 should allow identifying whether WWP1 is a diagnosis biomarker in cancer and/or a new therapeutic target for the development of anticancer drugs
Книги з теми "E3 LIGASE ACTIVITY"
Barañano, Kristin W. Angelman Syndrome. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199937837.003.0055.
Повний текст джерелаЧастини книг з теми "E3 LIGASE ACTIVITY"
Ren, Hong Yu, Cam Patterson, Douglas M. Cyr, and Meredith F. N. Rosser. "Reconstitution of CHIP E3 Ubiquitin Ligase Activity." In Methods in Molecular Biology, 93–103. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-295-3_8.
Повний текст джерелаOhtake, Fumiaki, and Shigeaki Kato. "The E3 Ubiquitin Ligase Activity of Transcription Factor AHR Permits Nongenomic Regulation of Biological Pathways." In The AH Receptor in Biology and Toxicology, 143–56. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118140574.ch10.
Повний текст джерелаTieroyaare Dongdem, Julius, and Cletus Adiyaga Wezena. "Functional Significance of the E3 Ubiquitin Ligases in Disease and Therapeutics." In Hydrolases [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.100534.
Повний текст джерелаSong, Jie, and Maréne Landström. "Lys63-Linked Polyubiquitination of Transforming Growth Factor β Type I Receptor (TβRI) Specifies Oncogenic Signaling." In Ubiquitin - Proteasome Pathway. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.93065.
Повний текст джерела"Molecular Investigation of Protein–Protein Interaction Candidates Related to the Mammalian Brain." In Cheminformatics and Bioinformatics at the Interface with Systems Biology, 81–107. Royal Society of Chemistry, 2023. http://dx.doi.org/10.1039/9781839166037-00081.
Повний текст джерелаSandmann, Alexander, and Nico Dissmeyer. "In vitro autoubiquitination activity of E3 ubiquitin ligases of the N-degron pathway." In Methods in Enzymology. Elsevier, 2023. http://dx.doi.org/10.1016/bs.mie.2023.02.014.
Повний текст джерелаТези доповідей конференцій з теми "E3 LIGASE ACTIVITY"
Lin, Huan-Yu, Shiu-Ting Lin, Mei-June Wang, and Jeou-Yuan Chen. "Abstract 1699: Suppressor of cytokine signaling 6 (SOCS6) promotes mitochondrial fission through E3 ubiquitin ligase complex activity." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-1699.
Повний текст джерелаShin, Jun-Wan, and Young-Joon Surh. "Abstract B67: Curcumin induces stabilization of Nrf2 protein by decreasing the activity of Cullin3-Rbx1 E3 ubiquitin ligase." In Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Oct 22-25, 2011; Boston, MA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1940-6207.prev-11-b67.
Повний текст джерелаShukla, Shirish, Felicia Gray, Weijiang Ying, Hyoje Cho, Qingjie Zhao, Hongzhi Miao, Hongzhi Miao, et al. "Abstract 50: Small molecule Ring1B-Bmi1 inhibitor attenuates PRC1 E3 ligase activity and targets leukemia stem cells self-renewal." In Abstracts: Second AACR Conference on Hematologic Malignancies: Translating Discoveries to Novel Therapies; May 6-9, 2017; Boston, MA. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1557-3265.hemmal17-50.
Повний текст джерелаQian, Tingting, Jeong-Yeon Lee, Hyun-Jun Kim, and Gu Kong. "Abstract LB-96: Id1 enhances RING1b E3 ubiquitin ligase activity through the Mel-18/Bmi-1 polycomb group complex." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-lb-96.
Повний текст джерелаQi, Jianfei, Manisha Tripathi, Natasha Sahgal, Ladan Fazil, Susan Ettinger, William J. Placzek, Giuseppina Claps, et al. "Abstract 5456: The E3 ubiquitin ligase Siah2 regulates the androgen receptor activity and contributes to castration-resistant prostate cancer." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-5456.
Повний текст джерелаYu, Yonghui, Jinyi Liu, Dongyun Zhang, Wenjing Luo, Jianxiu Yu, Jingxia Li, Xinhai Zhang, Jingyuan Chen, and Chuanshu Huang. "Abstract 4312: E3 ligase activity of XIAP RING domain is required for XIAP-mediated cancer cell migration but not for its RhoGDI binding activity." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4312.
Повний текст джерелаShukla, Shirish, Qingjie Zhao, Weijang Ying, Felicia Gray, Kelly Vandenberg, George Lund, Bohdan Boytsov, Shihan He, Jolanta Grembecka, and Tomasz Cierpicki. "Abstract 3520: Small molecule inhibitors of ring1B-Bmi1 E3 ligase target polycomb repressive complex 1 activity and regulate cell proliferation." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-3520.
Повний текст джерелаBanh, Robert S., Caterina Iorio, Richard Marcotte, Yang Xu, Dan Cojocari, Anas Abdel Rahman, Judy Pawling, et al. "Abstract LB-302: PTP1B regulates the Moyamoya disease-associated E3 ligase, RNF213 and cellular dioxygenase activity to allow breast tumor survival in hypoxia." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-lb-302.
Повний текст джерелаSosin, Angela M., Angelika M. Burger, Dajun Yang, Ramzi M. Mohammad, and Ayad Al-Katib. "Abstract 4516: A new class of MDM2 inhibitors cause growth inhibition and stabilize wt p53 in lymphoma cells but do not interfere with MDM2 E3 ligase activity." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-4516.
Повний текст джерелаZhao, Hongling, Vineeth Sukrithan, Niloy Iqbal, Cari Nicholas, Yingjiao Xue, Joseph Locker, Juntao Zou, Liang Zhu, and Edward L. Schwartz. "Abstract 1060: Genetic and pharmacologic inhibition of Skp2, an E3 ubiquitin ligase and RB1-target, has antitumor activity in RB1-deficient human and mouse small cell lung cancer (SCLC)." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-1060.
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