Статті в журналах з теми "Ligase I Inhibitors"
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Alomari, Arqam, Robert Gowland, Callum Southwood, Jak Barrow, Zoe Bentley, Jashel Calvin-Nelson, Alice Kaminski, et al. "Identification of Novel Inhibitors of Escherichia coli DNA Ligase (LigA)." Molecules 26, no. 9 (April 25, 2021): 2508. http://dx.doi.org/10.3390/molecules26092508.
Повний текст джерелаCiarrocchi, Giovanni, Donald G. MacPhee, Les W. Deady, and Leann Tilley. "Specific Inhibition of the Eubacterial DNA Ligase by Arylamino Compounds." Antimicrobial Agents and Chemotherapy 43, no. 11 (November 1, 1999): 2766–72. http://dx.doi.org/10.1128/aac.43.11.2766.
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 джерелаShapiro, Adam B., Ann E. Eakin, Grant K. Walkup, and Olga Rivin. "A High-Throughput Fluorescence Resonance Energy Transfer-Based Assay for DNA Ligase." Journal of Biomolecular Screening 16, no. 5 (March 11, 2011): 486–93. http://dx.doi.org/10.1177/1087057111398295.
Повний текст джерелаGorelik, Maryna, Stephen Orlicky, Maria A. Sartori, Xiaojing Tang, Edyta Marcon, Igor Kurinov, Jack F. Greenblatt, et al. "Inhibition of SCF ubiquitin ligases by engineered ubiquitin variants that target the Cul1 binding site on the Skp1–F-box interface." Proceedings of the National Academy of Sciences 113, no. 13 (March 14, 2016): 3527–32. http://dx.doi.org/10.1073/pnas.1519389113.
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 джерелаTobin, Lisa A., Aaron P. Rapoport, Ivana Gojo, Maria R. Baer, Alan E. Tomkinson, and Feyruz V. Rassool. "DNA Ligase III Alpha and (Poly-ADP) Ribose Polymerase (PARP1) Are Therapeutic Targets in Imatinib-Resistant (IR) Chronic Myeloid Leukemia (CML)." Blood 114, no. 22 (November 20, 2009): 853. http://dx.doi.org/10.1182/blood.v114.22.853.853.
Повний текст джерелаTAN, Ghee T., Sangkook LEE, Ik-Soo LEE, Jingwen CHEN, Pete LEITNER, Jeffrey M. BESTERMAN, Douglas A. KINGHORN, and John M. PEZZUTO. "Natural-product inhibitors of human DNA ligase I." Biochemical Journal 314, no. 3 (March 15, 1996): 993–1000. http://dx.doi.org/10.1042/bj3140993.
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 джерелаMills, Scott D., Ann E. Eakin, Ed T. Buurman, Joseph V. Newman, Ning Gao, Hoan Huynh, Kenneth D. Johnson, et al. "Novel Bacterial NAD+-Dependent DNA Ligase Inhibitors with Broad-Spectrum Activity and Antibacterial EfficacyIn Vivo." Antimicrobial Agents and Chemotherapy 55, no. 3 (December 28, 2010): 1088–96. http://dx.doi.org/10.1128/aac.01181-10.
Повний текст джерелаHowes, Timothy R. L., Annahita Sallmyr, Rhys Brooks, George E. Greco, Darin E. Jones, Yoshihiro Matsumoto, and Alan E. Tomkinson. "Structure-activity relationships among DNA ligase inhibitors: Characterization of a selective uncompetitive DNA ligase I inhibitor." DNA Repair 60 (December 2017): 29–39. http://dx.doi.org/10.1016/j.dnarep.2017.10.002.
Повний текст джерелаTomkinson, Alan E., Tasmin Naila, and Seema Khattri Bhandari. "Altered DNA ligase activity in human disease." Mutagenesis 35, no. 1 (October 20, 2019): 51–60. http://dx.doi.org/10.1093/mutage/gez026.
Повний текст джерелаGiardina, Sarah F., Elena Valdambrini, Michael Peel, Manny D. Bacolod, Mace L. Rothenberg, Richard B. Lanman, J. David Warren, and Francis Barany. "Cure-PROs: Next-generation targeted protein degraders." Journal of Clinical Oncology 41, no. 16_suppl (June 1, 2023): e15101-e15101. http://dx.doi.org/10.1200/jco.2023.41.16_suppl.e15101.
Повний текст джерелаWatanabe, Bunta, Hiroaki Kirikae, Takao Koeduka, Yoshinori Takeuchi, Tomoki Asai, Yoshiyuki Naito, Hideya Tokuoka, et al. "Synthesis and inhibitory activity of mechanism-based 4-coumaroyl-CoA ligase inhibitors." Bioorganic & Medicinal Chemistry 26, no. 9 (May 2018): 2466–74. http://dx.doi.org/10.1016/j.bmc.2018.04.006.
Повний текст джерелаBaum, Ellen Z., Steven M. Crespo-Carbone, Darren Abbanat, Barbara Foleno, Amy Maden, Raul Goldschmidt, and Karen Bush. "Utility of Muropeptide Ligase for Identification of Inhibitors of the Cell Wall Biosynthesis Enzyme MurF." Antimicrobial Agents and Chemotherapy 50, no. 1 (January 2006): 230–36. http://dx.doi.org/10.1128/aac.50.1.230-236.2006.
Повний текст джерелаKristan, Katja, Miha Kotnik, Marko Oblak, and Uroš Urleb. "New High-Throughput Fluorimetric Assay for Discovering Inhibitors of UDP-N-Acetylmuramyl-l-Alanine: d-Glutamate (MurD) Ligase." Journal of Biomolecular Screening 14, no. 4 (April 2009): 412–18. http://dx.doi.org/10.1177/1087057109332597.
Повний текст джерелаPavlides, Savvas C., Kuang-Tzu Huang, Dylan A. Reid, Lily Wu, Stephanie V. Blank, Khushbakhat Mittal, Lankai Guo, et al. "Inhibitors of SCF-Skp2/Cks1 E3 Ligase Block Estrogen-Induced Growth Stimulation and Degradation of Nuclear p27kip1: Therapeutic Potential for Endometrial Cancer." Endocrinology 154, no. 11 (November 1, 2013): 4030–45. http://dx.doi.org/10.1210/en.2013-1757.
Повний текст джерелаPowell, Jason A., Melissa R. Pitman, Julia R. Zebol, Paul A. B. Moretti, Heidi A. Neubauer, Lorena T. Davies, Alexander C. Lewis, et al. "Kelch-like protein 5-mediated ubiquitination of lysine 183 promotes proteasomal degradation of sphingosine kinase 1." Biochemical Journal 476, no. 21 (November 11, 2019): 3211–26. http://dx.doi.org/10.1042/bcj20190245.
Повний текст джерелаWan, Yichao, Chunxing Yan, Han Gao, and Tingting Liu. "Small-molecule PROTACs: novel agents for cancer therapy." Future Medicinal Chemistry 12, no. 10 (May 2020): 915–38. http://dx.doi.org/10.4155/fmc-2019-0340.
Повний текст джерелаPandey, Monica, Sujeet Kumar, Gunaseelan Goldsmith, Mrinal Srivastava, Santhini Elango, Mohammad Shameem, Dibyendu Bannerjee, Bibha Choudhary, Subhas S. Karki, and Sathees C. Raghavan. "Identification and characterization of novel ligase I inhibitors." Molecular Carcinogenesis 56, no. 2 (June 27, 2016): 550–66. http://dx.doi.org/10.1002/mc.22516.
Повний текст джерелаWatt, Jessica E., Gregory R. Hughes, Samuel Walpole, Serena Monaco, G. Richard Stephenson, Philip C. Bulman Page, Andrew M. Hemmings, Jesus Angulo, and Andrew Chantry. "Discovery of Small Molecule WWP2 Ubiquitin Ligase Inhibitors." Chemistry - A European Journal 24, no. 67 (November 6, 2018): 17677–80. http://dx.doi.org/10.1002/chem.201804169.
Повний текст джерелаKuai, Jun, Yingzhi Bi, Yilin Qi, Deborah Conrady, Rajiv Govindaraj, Graham Hone, R. Aldrin Denny, Ken Carson, Geraldine Harriman, and Fang Wang. "864 Identification of a novel allosteric oral Cbl-b inhibitor that augmented T cell response and enhanced NK cell killing in vitro and in vivo." Journal for ImmunoTherapy of Cancer 9, Suppl 2 (November 2021): A905. http://dx.doi.org/10.1136/jitc-2021-sitc2021.864.
Повний текст джерелаNicholson, B., Suresh Kumar, S. Agarwal, M. J. Eddins, J. G. Marblestone, J. Wu, M. P. Kodrasov, J. P. LaRocque, D. E. Sterner, and M. R. Mattern. "Discovery of Therapeutic Deubiquitylase Effector Molecules." Journal of Biomolecular Screening 19, no. 7 (March 14, 2014): 989–99. http://dx.doi.org/10.1177/1087057114527312.
Повний текст джерелаBjij, Imane, Pritika Ramharack, Shama Khan, Driss Cherqaoui, and Mahmoud Soliman. "Tracing Potential Covalent Inhibitors of an E3 Ubiquitin Ligase Through Target-Focused Modelling." Proceedings 22, no. 1 (November 14, 2019): 103. http://dx.doi.org/10.3390/proceedings2019022103.
Повний текст джерелаGutierrez-Lugo, Maria-Teresa, Heather Baker, Joseph Shiloach, Helena Boshoff, and Carole A. Bewley. "Dequalinium, a New Inhibitor of Mycobacterium tuberculosis Mycothiol Ligase Identified by High-Throughput Screening." Journal of Biomolecular Screening 14, no. 6 (June 12, 2009): 643–52. http://dx.doi.org/10.1177/1087057109335743.
Повний текст джерелаChu, Yu-Yi, Mei-Kuang Chen, Yongkun Wei, Heng-Huan Lee, Weiya Xia, Ying-Nai Wang, Clinton Yam, et al. "Targeting the ALK–CDK9-Tyr19 kinase cascade sensitizes ovarian and breast tumors to PARP inhibition via destabilization of the P-TEFb complex." Nature Cancer 3, no. 10 (October 17, 2022): 1211–27. http://dx.doi.org/10.1038/s43018-022-00438-2.
Повний текст джерелаLu, Jing, Yimin Qian, Kanak Raina, Martha Altieri, Hanqing Dong, Jing Wang, Xin Chen, et al. "BRD4 Degradation By Protacs Represents a More Effective Therapeutic Strategy Than BRD4 Inhibitors in DLBCL." Blood 126, no. 23 (December 3, 2015): 2050. http://dx.doi.org/10.1182/blood.v126.23.2050.2050.
Повний текст джерелаMartinez-Iglesias, Olaia, Alba Casas-Pais, Raquel Castosa, Andrea Díaz-Díaz, Daniel Roca-Lema, Ángel Concha, Álvaro Cortés, Federico Gago, and Angélica Figueroa. "Hakin-1, a New Specific Small-Molecule Inhibitor for the E3 Ubiquitin-Ligase Hakai, Inhibits Carcinoma Growth and Progression." Cancers 12, no. 5 (May 23, 2020): 1340. http://dx.doi.org/10.3390/cancers12051340.
Повний текст джерелаChen, Qing, Weilin Xie, Deborah J. Kuhn, Peter M. Voorhees, Antonia Lopez-Girona, Derek Mendy, Laura G. Corral, et al. "Targeting the p27 E3 ligase SCFSkp2 results in p27- and Skp2-mediated cell-cycle arrest and activation of autophagy." Blood 111, no. 9 (May 1, 2008): 4690–99. http://dx.doi.org/10.1182/blood-2007-09-112904.
Повний текст джерелаBjij, Imane, Pritika Ramharack, Shama Khan, Driss Cherqaoui, and Mahmoud E. S. Soliman. "Tracing Potential Covalent Inhibitors of an E3 Ubiquitin Ligase through Target-Focused Modelling." Molecules 24, no. 17 (August 28, 2019): 3125. http://dx.doi.org/10.3390/molecules24173125.
Повний текст джерелаSallmyr, Annahita, Lisa Tobin, Alan E. Tomkinson, and Feyruz V. Rassool. "Inhibiting Alternative Non Homologus Endjoining (NHEJ) Pathways: Therapeutic Targets in Chronic Myeloid Leukemia (CML)." Blood 112, no. 11 (November 16, 2008): 1088. http://dx.doi.org/10.1182/blood.v112.11.1088.1088.
Повний текст джерелаLandré, Vivien, Barak Rotblat, Sonia Melino, Francesca Bernassola, and Gerry Melino. "Screening for E3-Ubiquitin ligase inhibitors: challenges and opportunities." Oncotarget 5, no. 18 (September 3, 2014): 7988–8013. http://dx.doi.org/10.18632/oncotarget.2431.
Повний текст джерелаParsons, William H., Arthur A. Patchett, Herbert G. Bull, William R. Schoen, David Taub, Jacqueline Davidson, Patricia L. Combs, James P. Springer, and Hans Gadebusch. "Phosphinic acid inhibitors of D-alanyl-D-alanine ligase." Journal of Medicinal Chemistry 31, no. 9 (September 1988): 1772–78. http://dx.doi.org/10.1021/jm00117a017.
Повний текст джерелаvan der Meer, Laurens T., Jurgen A. F. Marteijn, Theo M. de Witte, Joop H. Jansen, and Bert A. van der Reijden. "Gfi1 Protein Turnover Is Regulated by the Ubiquitin Ligase Triad1." Blood 108, no. 11 (November 16, 2006): 1173. http://dx.doi.org/10.1182/blood.v108.11.1173.1173.
Повний текст джерелаTsukahara, Fujiko, and Yoshiro Maru. "Bag1 directly routes immature BCR-ABL for proteasomal degradation." Blood 116, no. 18 (November 4, 2010): 3582–92. http://dx.doi.org/10.1182/blood-2009-10-249623.
Повний текст джерелаWilson, Brice A. P., Donna Voeller, Emily A. Smith, Antony Wamiru, Ekaterina I. Goncharova, Gang Liu, Stanley Lipkowitz, and Barry R. O’Keefe. "In Vitro Ubiquitination Platform Identifies Methyl Ellipticiniums as Ubiquitin Ligase Inhibitors." SLAS DISCOVERY: Advancing the Science of Drug Discovery 26, no. 7 (April 21, 2021): 870–84. http://dx.doi.org/10.1177/24725552211000675.
Повний текст джерелаRana, Sandeep, Jayapal Reddy Mallareddy, Sarbjit Singh, Lidia Boghean, and Amarnath Natarajan. "Inhibitors, PROTACs and Molecular Glues as Diverse Therapeutic Modalities to Target Cyclin-Dependent Kinase." Cancers 13, no. 21 (November 2, 2021): 5506. http://dx.doi.org/10.3390/cancers13215506.
Повний текст джерелаCasaletto, Jessica B., Leta K. Nutt, Qiju Wu, Jonathan D. Moore, Laurence D. Etkin, Peter K. Jackson, Tim Hunt, and Sally Kornbluth. "Inhibition of the anaphase-promoting complex by the Xnf7 ubiquitin ligase." Journal of Cell Biology 169, no. 1 (April 11, 2005): 61–71. http://dx.doi.org/10.1083/jcb.200411056.
Повний текст джерелаMontecucco, A., M. Lestingi, G. Pedrali-Noy, S. Spadari та G. Ciarrocchi. "Use of ATP, dATP and their α-thio derivatives to study DNA ligase adenylation". Biochemical Journal 271, № 1 (1 жовтня 1990): 265–68. http://dx.doi.org/10.1042/bj2710265.
Повний текст джерелаChen, Wei-Yi, Jui-Hsia Weng, Chen-Che Huang, and Bon-chu Chung. "Histone Deacetylase Inhibitors Reduce Steroidogenesis through SCF-Mediated Ubiquitination and Degradation of Steroidogenic Factor 1 (NR5A1)." Molecular and Cellular Biology 27, no. 20 (August 20, 2007): 7284–90. http://dx.doi.org/10.1128/mcb.00476-07.
Повний текст джерелаTriola, Gemma, Stefan Wetzel, Bernhard Ellinger, Marcus A. Koch, Katja Hübel, Daniel Rauh, and Herbert Waldmann. "ATP competitive inhibitors of d-alanine–d-alanine ligase based on protein kinase inhibitor scaffolds." Bioorganic & Medicinal Chemistry 17, no. 3 (February 2009): 1079–87. http://dx.doi.org/10.1016/j.bmc.2008.02.046.
Повний текст джерелаShrivastava, Nidhi, Jeetendra K. Nag, Jyoti Pandey, Rama Pati Tripathi, Priyanka Shah, Mohammad Imran Siddiqi, and Shailja Misra-Bhattacharya. "Homology Modeling of NAD+-Dependent DNA Ligase of the Wolbachia Endosymbiont of Brugia malayi and Its Drug Target Potential Using Dispiro-Cycloalkanones." Antimicrobial Agents and Chemotherapy 59, no. 7 (April 6, 2015): 3736–47. http://dx.doi.org/10.1128/aac.03449-14.
Повний текст джерелаAshraf, Zaman, Aamer Saeed, and Humaira Nadeem. "Design, synthesis and docking studies of some novel isocoumarin analogues as antimicrobial agents." RSC Adv. 4, no. 96 (2014): 53842–53. http://dx.doi.org/10.1039/c4ra07223e.
Повний текст джерелаKovač, Andreja, Vita Majce, Roman Lenaršič, Sergeja Bombek, Julieanne M. Bostock, Ian Chopra, Slovenko Polanc, and Stanislav Gobec. "Diazenedicarboxamides as inhibitors of d-alanine-d-alanine ligase (Ddl)." Bioorganic & Medicinal Chemistry Letters 17, no. 7 (April 2007): 2047–54. http://dx.doi.org/10.1016/j.bmcl.2007.01.015.
Повний текст джерелаDuckworth, Benjamin P., Todd W. Geders, Divya Tiwari, Helena I. Boshoff, Paul A. Sibbald, Clifton E. Barry, Dirk Schnappinger, Barry C. Finzel, and Courtney C. Aldrich. "Bisubstrate Adenylation Inhibitors of Biotin Protein Ligase from Mycobacterium tuberculosis." Chemistry & Biology 18, no. 11 (November 2011): 1432–41. http://dx.doi.org/10.1016/j.chembiol.2011.08.013.
Повний текст джерелаLee, Junglim, Deanne W. Sammond, Zeno Fiorini, Jonel P. Saludes, Michael G. Resch, Bing Hao, Wei Wang, Hang Yin, and Xuedong Liu. "Computationally Designed Peptide Inhibitors of the Ubiquitin E3 Ligase SCFFbx4." ChemBioChem 14, no. 4 (February 11, 2013): 445–51. http://dx.doi.org/10.1002/cbic.201200777.
Повний текст джерелаBruning, John B., Ana C. Murillo, Ofelia Chacon, Raúl G. Barletta, and James C. Sacchettini. "Structure of theMycobacterium tuberculosisd-Alanine:d-Alanine Ligase, a Target of the Antituberculosis Drug d-Cycloserine." Antimicrobial Agents and Chemotherapy 55, no. 1 (October 18, 2010): 291–301. http://dx.doi.org/10.1128/aac.00558-10.
Повний текст джерелаAndo, Kiyohiro, Yusuke Suenaga, and Takehiko Kamijo. "DNA Ligase 4 Contributes to Cell Proliferation against DNA-PK Inhibition in MYCN-Amplified Neuroblastoma IMR32 Cells." International Journal of Molecular Sciences 24, no. 10 (May 19, 2023): 9012. http://dx.doi.org/10.3390/ijms24109012.
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 джерелаRajalingam, Krishnaraj, and Ivan Dikic. "Inhibitors of apoptosis catch ubiquitin." Biochemical Journal 417, no. 1 (December 12, 2008): e1-e3. http://dx.doi.org/10.1042/bj20082215.
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