Artigos de revistas sobre o tema "3CLpro"
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Ziebuhr, John, Sonja Bayer, Jeff A. Cowley e Alexander E. Gorbalenya. "The 3C-Like Proteinase of an Invertebrate Nidovirus Links Coronavirus and Potyvirus Homologs". Journal of Virology 77, n.º 2 (15 de janeiro de 2003): 1415–26. http://dx.doi.org/10.1128/jvi.77.2.1415-1426.2003.
Texto completo da fonteTsu, Brian V., Rimjhim Agarwal, Nandan S. Gokhale, Jessie Kulsuptrakul, Andrew P. Ryan, Elizabeth J. Fay, Lennice K. Castro et al. "Host-specific sensing of coronaviruses and picornaviruses by the CARD8 inflammasome". PLOS Biology 21, n.º 6 (8 de junho de 2023): e3002144. http://dx.doi.org/10.1371/journal.pbio.3002144.
Texto completo da fonteRawson, Jonathan M. O., Alice Duchon, Olga A. Nikolaitchik, Vinay K. Pathak e Wei-Shau Hu. "Development of a Cell-Based Luciferase Complementation Assay for Identification of SARS-CoV-2 3CLpro Inhibitors". Viruses 13, n.º 2 (24 de janeiro de 2021): 173. http://dx.doi.org/10.3390/v13020173.
Texto completo da fonteZhang, Jingjing, Yingpei Jiang, Chunxiu Wu, Dan Zhou, Jufang Gong, Tiejun Zhao e Zhigang Jin. "Development of FRET and Stress Granule Dual-Based System to Screen for Viral 3C Protease Inhibitors". Molecules 28, n.º 7 (28 de março de 2023): 3020. http://dx.doi.org/10.3390/molecules28073020.
Texto completo da fonteSanachai, Kamonpan, Tuanjai Somboon, Patcharin Wilasluck, Peerapon Deetanya, Peter Wolschann, Thierry Langer, Vannajan Sanghiran Lee, Kittikhun Wangkanont, Thanyada Rungrotmongkol e Supot Hannongbua. "Identification of repurposing therapeutics toward SARS-CoV-2 main protease by virtual screening". PLOS ONE 17, n.º 6 (30 de junho de 2022): e0269563. http://dx.doi.org/10.1371/journal.pone.0269563.
Texto completo da fonteGlab-ampai, Kittirat, Kanasap Kaewchim, Thanatsaran Saenlom, Watayagorn Thepsawat, Kodchakorn Mahasongkram, Nitat Sookrung, Wanpen Chaicumpa e Monrat Chulanetra. "Human Superantibodies to 3CLpro Inhibit Replication of SARS-CoV-2 across Variants". International Journal of Molecular Sciences 23, n.º 12 (13 de junho de 2022): 6587. http://dx.doi.org/10.3390/ijms23126587.
Texto completo da fonteYe, Gang, Xiaowei Wang, Xiaohan Tong, Yuejun Shi, Zhen F. Fu e Guiqing Peng. "Structural Basis for Inhibiting Porcine Epidemic Diarrhea Virus Replication with the 3C-Like Protease Inhibitor GC376". Viruses 12, n.º 2 (21 de fevereiro de 2020): 240. http://dx.doi.org/10.3390/v12020240.
Texto completo da fonteChen, Chia-Nan, Coney P. C. Lin, Kuo-Kuei Huang, Wei-Cheng Chen, Hsin-Pang Hsieh, Po-Huang Liang e John T. A. Hsu. "Inhibition of SARS-CoV 3C-like Protease Activity by Theaflavin-3,3'-digallate (TF3)". Evidence-Based Complementary and Alternative Medicine 2, n.º 2 (2005): 209–15. http://dx.doi.org/10.1093/ecam/neh081.
Texto completo da fonteRana, Shiwani, Prateek Kumar, Anchal Sharma, Sanjay Sharma, Rajanish Giri e Kalyan S. Ghosh. "Identification of Naturally Occurring Antiviral Molecules for SARS-CoV-2 Mitigation". Open COVID Journal 1, n.º 1 (10 de junho de 2021): 38–46. http://dx.doi.org/10.2174/2666958702101010038.
Texto completo da fonteWu, Jing, Bo Feng, Li-Xin Gao, Chun Zhang, Jia Li, Da-Jun Xiang, Yi Zang e Wen-Long Wang. "Synthesis and Biochemical Evaluation of 8H-Indeno[1,2-d]thiazole Derivatives as Novel SARS-CoV-2 3CL Protease Inhibitors". Molecules 27, n.º 10 (23 de maio de 2022): 3359. http://dx.doi.org/10.3390/molecules27103359.
Texto completo da fonteKim, Yunjeong, Vinay Shivanna, Sanjeev Narayanan, Allan M. Prior, Sahani Weerasekara, Duy H. Hua, Anushka C. Galasiti Kankanamalage, William C. Groutas e Kyeong-Ok Chang. "Broad-Spectrum Inhibitors against 3C-Like Proteases of Feline Coronaviruses and Feline Caliciviruses". Journal of Virology 89, n.º 9 (18 de fevereiro de 2015): 4942–50. http://dx.doi.org/10.1128/jvi.03688-14.
Texto completo da fonteNaumovich, Vladislav, Maria Grishina e Vladimir Potemkin. "Establishment of models for reliability evaluation of 3CLpro ligand-receptor complexes with different binding sites". Future Medicinal Chemistry 14, n.º 7 (abril de 2022): 501–10. http://dx.doi.org/10.4155/fmc-2021-0271.
Texto completo da fonteZhang, Yue, Huijie Chen, Mengmeng Zou, Rick Oerlemans, Changhao Shao, Yudong Ren, Ruili Zhang, Xiaodan Huang, Guangxing Li e Yingying Cong. "Hypericin Inhibit Alpha-Coronavirus Replication by Targeting 3CL Protease". Viruses 13, n.º 9 (14 de setembro de 2021): 1825. http://dx.doi.org/10.3390/v13091825.
Texto completo da fonteAhmad, Bilal, Maria Batool, Qurat ul Ain, Moon Suk Kim e Sangdun Choi. "Exploring the Binding Mechanism of PF-07321332 SARS-CoV-2 Protease Inhibitor through Molecular Dynamics and Binding Free Energy Simulations". International Journal of Molecular Sciences 22, n.º 17 (24 de agosto de 2021): 9124. http://dx.doi.org/10.3390/ijms22179124.
Texto completo da fonteLu, Xiao Tao, Amy C. Sims e Mark R. Denison. "Mouse Hepatitis Virus 3C-Like Protease Cleaves a 22-Kilodalton Protein from the Open Reading Frame 1a Polyprotein in Virus-Infected Cells and In Vitro". Journal of Virology 72, n.º 3 (1 de março de 1998): 2265–71. http://dx.doi.org/10.1128/jvi.72.3.2265-2271.1998.
Texto completo da fonteIbrahim, Mahmoud A. A., Alaa H. M. Abdelrahman, Dina E. M. Mohamed, Khlood A. A. Abdeljawaad, Mohamed Ahmed Naeem, Gamal A. Gabr, Ahmed M. Shawky et al. "Chetomin, a SARS-CoV-2 3C-like Protease (3CLpro) Inhibitor: In Silico Screening, Enzyme Docking, Molecular Dynamics and Pharmacokinetics Analysis". Viruses 15, n.º 1 (15 de janeiro de 2023): 250. http://dx.doi.org/10.3390/v15010250.
Texto completo da fonteFakih, Taufik Muhammad, e Dwi Syah Fitra Ramadhan. "Prediction of SARS-CoV-2 3C-like protease (3CLpro) crystal structure to provide COVID-19 inhibitor design through computational studies". Biogenesis: Jurnal Ilmiah Biologi 9, n.º 2 (30 de dezembro de 2021): 213–19. http://dx.doi.org/10.24252/bio.v9i2.24520.
Texto completo da fonteMa, Ling, Yongli Xie, Mei Zhu, Dongrong Yi, Jianyuan Zhao, Saisai Guo, Yongxin Zhang et al. "Identification of Darunavir Derivatives for Inhibition of SARS-CoV-2 3CLpro". International Journal of Molecular Sciences 23, n.º 24 (16 de dezembro de 2022): 16011. http://dx.doi.org/10.3390/ijms232416011.
Texto completo da fonteValipour, Mehdi, Silvia Di Giacomo, Antonella Di Sotto e Hamid Irannejad. "Discovery of Chalcone-Based Hybrid Structures as High Affinity and Site-Specific Inhibitors against SARS-CoV-2: A Comprehensive Structural Analysis Based on Various Host-Based and Viral Targets". International Journal of Molecular Sciences 24, n.º 10 (15 de maio de 2023): 8789. http://dx.doi.org/10.3390/ijms24108789.
Texto completo da fonteGuijarro-Real, Carla, Mariola Plazas, Adrián Rodríguez-Burruezo, Jaime Prohens e Ana Fita. "Potential In Vitro Inhibition of Selected Plant Extracts against SARS-CoV-2 Chymotripsin-Like Protease (3CLPro) Activity". Foods 10, n.º 7 (29 de junho de 2021): 1503. http://dx.doi.org/10.3390/foods10071503.
Texto completo da fonteJukič, Marko, Blaž Škrlj, Gašper Tomšič, Sebastian Pleško, Črtomir Podlipnik e Urban Bren. "Prioritisation of Compounds for 3CLpro Inhibitor Development on SARS-CoV-2 Variants". Molecules 26, n.º 10 (18 de maio de 2021): 3003. http://dx.doi.org/10.3390/molecules26103003.
Texto completo da fonteHuynh, Thi Ngoc Thanh, Thi Thanh Thu Tran, Thi My Hanh Pham e Kha Quang Quach. "Study on the interaction mechanism of penciclovir drug on 3CLpro of SAR-COV-2 by simulation methods". Dong Thap University Journal of Science 12, n.º 5 (23 de junho de 2023): 42–47. http://dx.doi.org/10.52714/dthu.12.5.2023.1070.
Texto completo da fonteChen, Lili, Shuai Chen, Chunshan Gui, Jianhua Shen, Xu Shen e Hualiang Jiang. "Discovering Severe Acute Respiratory Syndrome Coronavirus 3CL Protease Inhibitors: Virtual Screening, Surface Plasmon Resonance, and Fluorescence Resonance Energy Transfer Assays". Journal of Biomolecular Screening 11, n.º 8 (dezembro de 2006): 915–21. http://dx.doi.org/10.1177/1087057106293295.
Texto completo da fonteHamill, Pamela, Derek Hudson, Richard Y. Kao, Polly Chow, Meera Raj, Hongyan Xu, Martin J. Richer e François Jean. "Development of a red-shifted fluorescence-based assay for SARS-coronavirus 3CL protease: identification of a novel class of anti-SARS agents from the tropical marine sponge Axinella corrugata". Biological Chemistry 387, n.º 8 (1 de agosto de 2006): 1063–74. http://dx.doi.org/10.1515/bc.2006.131.
Texto completo da fonteJo, Seri, Hwa Young Kim, Dong Hae Shin e Mi-Sun Kim. "Dimerization Tendency of 3CLpros of Human Coronaviruses Based on the X-ray Crystal Structure of the Catalytic Domain of SARS-CoV-2 3CLpro". International Journal of Molecular Sciences 23, n.º 9 (9 de maio de 2022): 5268. http://dx.doi.org/10.3390/ijms23095268.
Texto completo da fonteGarland, Gavin D., Robert F. Harvey, Thomas E. Mulroney, Mie Monti, Stewart Fuller, Richard Haigh, Pehuén Pereyra Gerber, Michael R. Barer, Nicholas J. Matheson e Anne E. Willis. "Development of a colorimetric assay for the detection of SARS-CoV-2 3CLpro activity". Biochemical Journal 479, n.º 8 (21 de abril de 2022): 901–20. http://dx.doi.org/10.1042/bcj20220105.
Texto completo da fonteLi, Zhonghua, Hua Cao, Yufang Cheng, Xiaoqian Zhang, Wei Zeng, Yumei Sun, Shuhua Chen, Qigai He e Heyou Han. "Inhibition of Porcine Epidemic Diarrhea Virus Replication and Viral 3C-Like Protease by Quercetin". International Journal of Molecular Sciences 21, n.º 21 (30 de outubro de 2020): 8095. http://dx.doi.org/10.3390/ijms21218095.
Texto completo da fonteFitriana, Adita Silvia, e Sri Royani. "Molecular Docking Study of Chalcone Derivatives as Potential Inhibitors of SARS-CoV-2 Main Protease". Indo. J. Chem. Res. 9, n.º 3 (29 de janeiro de 2022): 150–62. http://dx.doi.org/10.30598//ijcr.2022.9-fit.
Texto completo da fonteHegyi, Annette, Agnes Friebe, Alexander E. Gorbalenya e John Ziebuhr. "Mutational analysis of the active centre of coronavirus 3C-like proteases". Journal of General Virology 83, n.º 3 (1 de março de 2002): 581–93. http://dx.doi.org/10.1099/0022-1317-83-3-581.
Texto completo da fonteSaquib, Quaiser, Ahmed H. Bakheit, Sarfaraz Ahmed, Sabiha M. Ansari, Abdullah M. Al-Salem e Abdulaziz A. Al-Khedhairy. "Identification of Phytochemicals from Arabian Peninsula Medicinal Plants as Strong Binders to SARS-CoV-2 Proteases (3CLPro and PLPro) by Molecular Docking and Dynamic Simulation Studies". Molecules 29, n.º 5 (25 de fevereiro de 2024): 998. http://dx.doi.org/10.3390/molecules29050998.
Texto completo da fonteKomissarov, Alexey, Maria Karaseva, Marina Roschina, Sergey Kostrov e Ilya Demidyuk. "The SARS-CoV-2 main protease doesn’t induce cell death in human cells in vitro". PLOS ONE 17, n.º 5 (24 de maio de 2022): e0266015. http://dx.doi.org/10.1371/journal.pone.0266015.
Texto completo da fonteZhang, Shilei, Jingfeng Wang e Genhong Cheng. "Protease cleavage of RNF20 facilitates coronavirus replication via stabilization of SREBP1". Proceedings of the National Academy of Sciences 118, n.º 37 (27 de agosto de 2021): e2107108118. http://dx.doi.org/10.1073/pnas.2107108118.
Texto completo da fonteDuarte Filho, Luiz Antonio Miranda de Souza, Cintia Emi Yanaguibashi Leal, Pierre-Edouard Bodet, Edilson Beserra de Alencar Filho, Jackson Roberto Guedes da Silva Almeida, Manon Porta Zapata, Oussama Achour et al. "The Identification of Peptide Inhibitors of the Coronavirus 3CL Protease from a Fucus ceranoides L. Hydroalcoholic Extract Using a Ligand-Fishing Strategy". Marine Drugs 22, n.º 6 (27 de maio de 2024): 244. http://dx.doi.org/10.3390/md22060244.
Texto completo da fonteRajeswari, Kalepu, W. Jun Chen, A. Aashika, T. Xian Ying, C. Choon Hoong, S. Kuha e Diya Rajasekhar Chinta. "Binding Interaction Analysis of Phytoconstituents of Commiphora mukul with 3CLPro and PlPro Enzymes of SARS-CoV-2 Virus". ECS Transactions 107, n.º 1 (24 de abril de 2022): 7509–30. http://dx.doi.org/10.1149/10701.7509ecst.
Texto completo da fonteWang, Yaxin, Binghong Xu, Sen Ma, Hao Wang, Luqing Shang, Cheng Zhu e Sheng Ye. "Discovery of SARS-CoV-2 3CLPro Peptidomimetic Inhibitors through the Catalytic Dyad Histidine-Specific Protein–Ligand Interactions". International Journal of Molecular Sciences 23, n.º 4 (21 de fevereiro de 2022): 2392. http://dx.doi.org/10.3390/ijms23042392.
Texto completo da fonteOlubiyi, Olujide O., Maryam Olagunju, Monika Keutmann, Jennifer Loschwitz e Birgit Strodel. "High Throughput Virtual Screening to Discover Inhibitors of the Main Protease of the Coronavirus SARS-CoV-2". Molecules 25, n.º 14 (13 de julho de 2020): 3193. http://dx.doi.org/10.3390/molecules25143193.
Texto completo da fonteYang, Cheng-Wei, Yung-Ning Yang, Po-Huang Liang, Chi-Min Chen, Wei-Liang Chen, Hwan-You Chang, Yu-Sheng Chao e Shiow-Ju Lee. "Novel Small-Molecule Inhibitors of Transmissible Gastroenteritis Virus". Antimicrobial Agents and Chemotherapy 51, n.º 11 (20 de agosto de 2007): 3924–31. http://dx.doi.org/10.1128/aac.00408-07.
Texto completo da fonteSobhy, Remah, Asad Nawaz, Mohammad Fikry, Rokayya Sami, Eman Algarni, Nada Benajiba, Sameer H. Qari, Alaa T. Qumsani e Ibrahim Khalifa. "In-Silico Evaluation of 10 Structurally Different Glucosinolates on the Key Enzyme of SARS-CoV-2". Science of Advanced Materials 14, n.º 1 (1 de janeiro de 2022): 162–74. http://dx.doi.org/10.1166/sam.2022.4190.
Texto completo da fonteDu, Weian, Liang Zhao, Rong Wu, Boning Huang, Si Liu, Yufeng Liu, Huaiqiu Huang e Ge Shi. "Predicting drug–Protein interaction with deep learning framework for molecular graphs and sequences: Potential candidates against SAR-CoV-2". PLOS ONE 19, n.º 5 (10 de maio de 2024): e0299696. http://dx.doi.org/10.1371/journal.pone.0299696.
Texto completo da fonteHaniyya, M. Ulfah, A. Riswoko, L. Mulyawati, T. Ernawati e I. Helianti. "Production of recombinant SARS-CoV-2 3CL-protease: The key for the development of protease inhibitors screening kit in search of potential herb cure for COVID-19". IOP Conference Series: Earth and Environmental Science 976, n.º 1 (1 de fevereiro de 2022): 012051. http://dx.doi.org/10.1088/1755-1315/976/1/012051.
Texto completo da fonteZiebuhr, John, e Stuart G. Siddell. "Processing of the Human Coronavirus 229E Replicase Polyproteins by the Virus-Encoded 3C-Like Proteinase: Identification of Proteolytic Products and Cleavage Sites Common to pp1a and pp1ab". Journal of Virology 73, n.º 1 (1 de janeiro de 1999): 177–85. http://dx.doi.org/10.1128/jvi.73.1.177-185.1999.
Texto completo da fonteCheng, Jin, Yixuan Hao, Qin Shi, Guanyu Hou, Yanan Wang, Yong Wang, Wen Xiao et al. "Discovery of Novel Chinese Medicine Compounds Targeting 3CL Protease by Virtual Screening and Molecular Dynamics Simulation". Molecules 28, n.º 3 (17 de janeiro de 2023): 937. http://dx.doi.org/10.3390/molecules28030937.
Texto completo da fonteRazali, Rafida, Vijay Kumar Subbiah e Cahyo Budiman. "Technical Data of Heterologous Expression and Purification of SARS-CoV-2 Proteases Using Escherichia coli System". Data 6, n.º 9 (16 de setembro de 2021): 99. http://dx.doi.org/10.3390/data6090099.
Texto completo da fonteRizzuti, Bruno, Laura Ceballos-Laita, David Ortega-Alarcon, Ana Jimenez-Alesanco, Sonia Vega, Fedora Grande, Filomena Conforti, Olga Abian e Adrian Velazquez-Campoy. "Sub-Micromolar Inhibition of SARS-CoV-2 3CLpro by Natural Compounds". Pharmaceuticals 14, n.º 9 (1 de setembro de 2021): 892. http://dx.doi.org/10.3390/ph14090892.
Texto completo da fonteMorita, Takeshi, Kei Miyakawa, Sundararaj Stanleyraj Jeremiah, Yutaro Yamaoka, Mitsuru Sada, Tomoko Kuniyoshi, Jinwei Yang, Hirokazu Kimura e Akihide Ryo. "All-Trans Retinoic Acid Exhibits Antiviral Effect against SARS-CoV-2 by Inhibiting 3CLpro Activity". Viruses 13, n.º 8 (23 de agosto de 2021): 1669. http://dx.doi.org/10.3390/v13081669.
Texto completo da fonteAHMED, N. ZAHEER, DICKY JOHN DAVIS, NOMAN ANWAR, ASIM ALI KHAN, RAM PRATAP MEENA, ZEBA AFNAAN e MEERA DEVI. "In-Silico Evaluation of Tiryaq-E-Wabai, an Unani Formulation for its Potency against SARS-CoV-2 Spike Glycoprotein and Main Protease". Journal of Drug Delivery and Therapeutics 11, n.º 4-S (15 de agosto de 2021): 86–100. http://dx.doi.org/10.22270/jddt.v11i4-s.4993.
Texto completo da fonteRizma, Baiq Ressa Puspita, Yek Zen Mubarok, Dian Fathita Dwi Lestari e Agus Dwi Ananto. "Molecular Study of Antiviral Compound of Indonesian Herbal Medicine as 3CLpro and PLpro Inhibitor in SARS-COV-2". Acta Chimica Asiana 4, n.º 2 (29 de outubro de 2021): 127–34. http://dx.doi.org/10.29303/aca.v4i2.74.
Texto completo da fonteHerlah, Barbara, Andrej Hoivik, Luka Jamšek, Katja Valjavec, Norio Yamamoto, Tyuji Hoshino, Krištof Kranjc e Andrej Perdih. "Design, Synthesis and Evaluation of Fused Bicyclo[2.2.2]octene as a Potential Core Scaffold for the Non-Covalent Inhibitors of SARS-CoV-2 3CLpro Main Protease". Pharmaceuticals 15, n.º 5 (27 de abril de 2022): 539. http://dx.doi.org/10.3390/ph15050539.
Texto completo da fonteFagnani, Lorenza, Lisaurora Nazzicone, Pierangelo Bellio, Nicola Franceschini, Donatella Tondi, Andrea Verri, Sabrina Petricca et al. "Protocetraric and Salazinic Acids as Potential Inhibitors of SARS-CoV-2 3CL Protease: Biochemical, Cytotoxic, and Computational Characterization of Depsidones as Slow-Binding Inactivators". Pharmaceuticals 15, n.º 6 (4 de junho de 2022): 714. http://dx.doi.org/10.3390/ph15060714.
Texto completo da fonteMohammad, Firdous Sayeed, Mohsina F. Patwekar e Faheem I. Patwekar. "Are Plant-derived Flavonoids the Emerging Anti-coronavirus Agents?" INNOSC Theranostics and Pharmacological Sciences 4, n.º 2 (29 de abril de 2022): 11–16. http://dx.doi.org/10.36922/itps.v4i2.42.
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