Artigos de revistas sobre o tema "Inhibition covalente"
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Aljoundi, Aimen, Ahmed El Rashedy, Patrick Appiah-Kubi e Mahmoud E. S. Soliman. "Coupling of HSP72 α-Helix Subdomains by the Unexpected Irreversible Targeting of Lysine-56 over Cysteine-17; Coevolution of Covalent Bonding". Molecules 25, n.º 18 (16 de setembro de 2020): 4239. http://dx.doi.org/10.3390/molecules25184239.
Texto completo da fonteLiu, S. Q., e P. A. Knauf. "Lys-430, site of irreversible inhibition of band 3 Cl- flux by eosin-5-maleimide, is not at the transport site". American Journal of Physiology-Cell Physiology 264, n.º 5 (1 de maio de 1993): C1155—C1164. http://dx.doi.org/10.1152/ajpcell.1993.264.5.c1155.
Texto completo da fonteYang, Jianhong, Yong Li, Wei Yan, Weimin Li, Qiang Qiu, Haoyu Ye e Lijuan Chen. "Covalent modification of Cys-239 in β-tubulin by small molecules as a strategy to promote tubulin heterodimer degradation". Journal of Biological Chemistry 294, n.º 20 (2 de abril de 2019): 8161–70. http://dx.doi.org/10.1074/jbc.ra118.006325.
Texto completo da fonteMaksimenko, A. V., e R. Sh Beabealashvili. "Theoretical Grounding and Formation of Experimental Approaches to Hyaluronidase Structure Consolidation due to Its Computational Interactions with Shortchain Glycosaminoglycan Ligands". Биоорганическая химия 49, n.º 4 (1 de julho de 2023): 369–83. http://dx.doi.org/10.31857/s0132342323020161.
Texto completo da fonteBhatia, Sumeena, Steven C. Almo, Stanley G. Nathenson e Richard J. Hodes. "Dynamic equilibrium of B7-1 dimers and monomers is important for regulation of TCR/CD28 – mediated T cell activation (33.28)". Journal of Immunology 182, n.º 1_Supplement (1 de abril de 2009): 33.28. http://dx.doi.org/10.4049/jimmunol.182.supp.33.28.
Texto completo da fonteKuznetsova, Anastasiya, Philipp Klein e Till Opatz. "Halogenated 2,1,3-benzoxadiazoles as Potential Fluorescent Warheads for Covalent Protease Inhibitors". Proceedings 9, n.º 1 (14 de novembro de 2018): 54. http://dx.doi.org/10.3390/ecsoc-22-05670.
Texto completo da fonteHognon, Cécilia, Marco Marazzi e Cristina García-Iriepa. "Atomistic-Level Description of the Covalent Inhibition of SARS-CoV-2 Papain-like Protease". International Journal of Molecular Sciences 23, n.º 10 (23 de maio de 2022): 5855. http://dx.doi.org/10.3390/ijms23105855.
Texto completo da fonteBisconte, Angelina, Ronald Hill, Michael Bradshaw, Erik Verner, David Finkle, Ken Brameld, Jens Funk, David Goldstein e Phil Nunn. "Efficacy in collagen induced arthritis models with a selective, reversible covalent Bruton’s tyrosine kinase inhibitor PRN473 is driven by durable target occupancy rather than extended plasma exposure (THER5P.904)". Journal of Immunology 194, n.º 1_Supplement (1 de maio de 2015): 139.6. http://dx.doi.org/10.4049/jimmunol.194.supp.139.6.
Texto completo da fonteBeck, Philipp, Christian Dubiella e Michael Groll. "Covalent and non-covalent reversible proteasome inhibition". Biological Chemistry 393, n.º 10 (1 de outubro de 2012): 1101–20. http://dx.doi.org/10.1515/hsz-2012-0212.
Texto completo da fontePiestrzeniewicz, Mariola K., Dorota Wilmańska, Janusz Szemraj, Kazimierz Studzian e Marek Gniazdowski. "Interactions of Novel Morpholine and Hexamethylene Derivatives of Anthracycline Antibiotics with DNA". Zeitschrift für Naturforschung C 59, n.º 9-10 (1 de outubro de 2004): 739–48. http://dx.doi.org/10.1515/znc-2004-9-1020.
Texto completo da fonteMüller, Patrick, Mergim Meta, Jan Laurenz Meidner, Marvin Schwickert, Jessica Meyr, Kevin Schwickert, Christian Kersten et al. "Investigation of the Compatibility between Warheads and Peptidomimetic Sequences of Protease Inhibitors—A Comprehensive Reactivity and Selectivity Study". International Journal of Molecular Sciences 24, n.º 8 (13 de abril de 2023): 7226. http://dx.doi.org/10.3390/ijms24087226.
Texto completo da fonteGerling, Katharina, Sabrina Ölschläger, Meltem Avci-Adali, Bernd Neumann, Ernst Schweizer, Christian Schlensak, Hans-Peter Wendel e Sandra Stoppelkamp. "A Novel C1-Esterase Inhibitor Oxygenator Coating Prevents FXII Activation in Human Blood". Biomolecules 10, n.º 7 (13 de julho de 2020): 1042. http://dx.doi.org/10.3390/biom10071042.
Texto completo da fonteStellmacher, Lena, Tatyana Sandalova, Sarah Schneider, Gunter Schneider, Georg A. Sprenger e Anne K. Samland. "Novel mode of inhibition byD-tagatose 6-phosphate through a Heyns rearrangement in the active site of transaldolase B variants". Acta Crystallographica Section D Structural Biology 72, n.º 4 (24 de março de 2016): 467–76. http://dx.doi.org/10.1107/s2059798316001170.
Texto completo da fonteBetori, Rick C., Yue Liu, Rama K. Mishra, Scott B. Cohen, Stephen J. Kron e Karl A. Scheidt. "Targeted Covalent Inhibition of Telomerase". ACS Chemical Biology 15, n.º 3 (4 de fevereiro de 2020): 706–17. http://dx.doi.org/10.1021/acschembio.9b00945.
Texto completo da fonteGhosh, Avick Kumar, Indranil Samanta, Anushree Mondal e Wenshe Ray Liu. "Covalent Inhibition in Drug Discovery". ChemMedChem 14, n.º 9 (26 de março de 2019): 889–906. http://dx.doi.org/10.1002/cmdc.201900107.
Texto completo da fonteRao, AK, e MA Kowalska. "ADP-induced platelet shape change and mobilization of cytoplasmic ionized calcium are mediated by distinct binding sites on platelets: 5'- p-fluorosulfonylbenzoyladenosine is a weak platelet agonist". Blood 70, n.º 3 (1 de setembro de 1987): 751–56. http://dx.doi.org/10.1182/blood.v70.3.751.751.
Texto completo da fonteRao, AK, e MA Kowalska. "ADP-induced platelet shape change and mobilization of cytoplasmic ionized calcium are mediated by distinct binding sites on platelets: 5'- p-fluorosulfonylbenzoyladenosine is a weak platelet agonist". Blood 70, n.º 3 (1 de setembro de 1987): 751–56. http://dx.doi.org/10.1182/blood.v70.3.751.bloodjournal703751.
Texto completo da fonteBjij, Imane, Fisayo A. Olotu, Clement Agoni, Emmanuel Adeniji, Shama Khan, Ahmed El Rashedy, Driss Cherqaoui e Mahmoud E. S. Soliman. "Covalent Inhibition in Drug Discovery: Filling the Void in Literature". Current Topics in Medicinal Chemistry 18, n.º 13 (4 de outubro de 2018): 1135–45. http://dx.doi.org/10.2174/1568026618666180731161438.
Texto completo da fonteStrelow, John M. "A Perspective on the Kinetics of Covalent and Irreversible Inhibition". SLAS DISCOVERY: Advancing the Science of Drug Discovery 22, n.º 1 (5 de outubro de 2016): 3–20. http://dx.doi.org/10.1177/1087057116671509.
Texto completo da fonteKilbourn, R., e G. Lopez-Berestein. "Protease inhibitors block the macrophage-mediated inhibition of tumor cell mitochondrial respiration." Journal of Immunology 144, n.º 3 (1 de fevereiro de 1990): 1042–45. http://dx.doi.org/10.4049/jimmunol.144.3.1042.
Texto completo da fonteColman, RW, WR Figures, LM Scearce, AM Strimpler, FX Zhou e AK Rao. "Inhibition of collagen-induced platelet activation by 5'-p- fluorosulfonylbenzoyl adenosine: evidence for an adenosine diphosphate requirement and synergistic influence of prostaglandin endoperoxides". Blood 68, n.º 2 (1 de agosto de 1986): 565–70. http://dx.doi.org/10.1182/blood.v68.2.565.565.
Texto completo da fonteColman, RW, WR Figures, LM Scearce, AM Strimpler, FX Zhou e AK Rao. "Inhibition of collagen-induced platelet activation by 5'-p- fluorosulfonylbenzoyl adenosine: evidence for an adenosine diphosphate requirement and synergistic influence of prostaglandin endoperoxides". Blood 68, n.º 2 (1 de agosto de 1986): 565–70. http://dx.doi.org/10.1182/blood.v68.2.565.bloodjournal682565.
Texto completo da fonteTian, Yafeng, Mi Zhang, Panpan Heng, Hua Hou e Baoshan Wang. "Computational Investigations on Reaction Mechanisms of the Covalent Inhibitors Ponatinib and Analogs Targeting the Extracellular Signal-Regulated Kinases". International Journal of Molecular Sciences 24, n.º 20 (16 de outubro de 2023): 15223. http://dx.doi.org/10.3390/ijms242015223.
Texto completo da fonteZhou, X. Edward, Kelly Suino-Powell, Chad R. Schultz, Bilal Aleiwi, Joseph S. Brunzelle, Jared Lamp, Irving E. Vega, Edmund Ellsworth, André S. Bachmann e Karsten Melcher. "Structural basis of binding and inhibition of ornithine decarboxylase by 1-amino-oxy-3-aminopropane". Biochemical Journal 478, n.º 23 (6 de dezembro de 2021): 4137–49. http://dx.doi.org/10.1042/bcj20210647.
Texto completo da fonteKinoshita, T., A. W. Dodds, S. K. A. Law e K. Inoue. "The low C5 convertase activity of the C4A6 allotype of human complement component C4". Biochemical Journal 261, n.º 3 (1 de agosto de 1989): 743–48. http://dx.doi.org/10.1042/bj2610743.
Texto completo da fonteStevic, Ivan, Howard H. W. Chan, Ankush Chander, Leslie R. Berry e Anthony K. C. Chan. "Covalently linking heparin to antithrombin enhances prothrombinase inhibition on activated platelets". Thrombosis and Haemostasis 109, n.º 06 (2013): 1016–24. http://dx.doi.org/10.1160/th12-10-0766.
Texto completo da fonteSim, E., A. W. Dodds e A. Goldin. "Inhibition of the covalent binding reaction of complement component C4 by penicillamine, an anti-rheumatic agent". Biochemical Journal 259, n.º 2 (15 de abril de 1989): 415–19. http://dx.doi.org/10.1042/bj2590415.
Texto completo da fonteLu, Jia-Hui, Zhen Li, Jia-Hui Chen, Shu-Liang Li, Jie-Hao He, Song Gu, Bo-Wen Liu, Li Chen e Yu-Zhong Wang. "Adaptable Phosphate Networks towards Robust, Reprocessable, Weldable, and Alertable-Yet-Extinguishable Epoxy Vitrimer". Research 2022 (6 de outubro de 2022): 1–12. http://dx.doi.org/10.34133/2022/9846940.
Texto completo da fonteRuddraraju, Kasi Viswanatharaju, e Zhong-Yin Zhang. "Covalent inhibition of protein tyrosine phosphatases". Molecular BioSystems 13, n.º 7 (2017): 1257–79. http://dx.doi.org/10.1039/c7mb00151g.
Texto completo da fonteZhao, Yuguang, Fredrik Svensson, David Steadman, Sarah Frew, Amy Monaghan, Magda Bictash, Tiago Moreira et al. "Structural Insights into Notum Covalent Inhibition". Journal of Medicinal Chemistry 64, n.º 15 (22 de julho de 2021): 11354–63. http://dx.doi.org/10.1021/acs.jmedchem.1c00701.
Texto completo da fonteWestover, Kenneth D., Pasi A. Jänne e Nathanael S. Gray. "Progress on Covalent Inhibition of KRASG12C". Cancer Discovery 6, n.º 3 (março de 2016): 233–34. http://dx.doi.org/10.1158/2159-8290.cd-16-0092.
Texto completo da fonteJacobs, Amy. "Covalent Inhibition of HIV Membrane Fusion". Biophysical Journal 96, n.º 3 (fevereiro de 2009): 359a. http://dx.doi.org/10.1016/j.bpj.2008.12.1814.
Texto completo da fonteHuang, Huang, Christina A. Howard, Sergei Zari, Hyo Je Cho, Shirish Shukla, Hao Li, Juliano Ndoj et al. "Covalent inhibition of NSD1 histone methyltransferase". Nature Chemical Biology 16, n.º 12 (31 de agosto de 2020): 1403–10. http://dx.doi.org/10.1038/s41589-020-0626-6.
Texto completo da fonteAmara, Neri, Roi Mashiach, Dotan Amar, Pnina Krief, Stéphane A. H. Spieser, Matthew J. Bottomley, Amir Aharoni e Michael M. Meijler. "Covalent Inhibition of Bacterial Quorum Sensing". Journal of the American Chemical Society 131, n.º 30 (5 de agosto de 2009): 10610–19. http://dx.doi.org/10.1021/ja903292v.
Texto completo da fonteKentner, Taryn A., Leslie R. Berry e Anthony K. C. Chan. "Inhibition of Factor Xa in Prothrombinase Is Enhanced by Covalent Linkage of Antithrombin to Heparin." Blood 104, n.º 11 (16 de novembro de 2004): 1051. http://dx.doi.org/10.1182/blood.v104.11.1051.1051.
Texto completo da fonteNAGUMO, Yoko, Hideaki KAKEYA, Mitsuru SHOJI, Yujiro HAYASHI, Naoshi DOHMAE e Hiroyuki OSADA. "Epolactaene binds human Hsp60 Cys442 resulting in the inhibition of chaperone activity". Biochemical Journal 387, n.º 3 (26 de abril de 2005): 835–40. http://dx.doi.org/10.1042/bj20041355.
Texto completo da fonteJebaraj, Billy Michael Chelliah, Annika Müller, Rashmi Priyadharshini Dheenadayalan, Sascha Endres, Philipp M. Roessner, Felix Seyfried, Claudia Walliser et al. "Evaluation of vecabrutinib as a model for noncovalent BTK/ITK inhibition for treatment of chronic lymphocytic leukemia". Blood 139, n.º 6 (10 de fevereiro de 2022): 859–75. http://dx.doi.org/10.1182/blood.2021011516.
Texto completo da fonteWágner, Gábor, Tamara A. M. Mocking, Albert J. Kooistra, Inna Slynko, Péter Ábrányi-Balogh, György M. Keserű, Maikel Wijtmans, Henry F. Vischer, Iwan J. P. de Esch e Rob Leurs. "Covalent Inhibition of the Histamine H3 Receptor". Molecules 24, n.º 24 (11 de dezembro de 2019): 4541. http://dx.doi.org/10.3390/molecules24244541.
Texto completo da fonteThøgersen, I. B., G. Salvesen, F. H. Brucato, S. V. Pizzo e J. J. Enghild. "Purification and characterization of an α-macroglobulin proteinase inhibitor from the mollusc Octopus vulgaris". Biochemical Journal 285, n.º 2 (15 de julho de 1992): 521–27. http://dx.doi.org/10.1042/bj2850521.
Texto completo da fonteShatan, Anastasiia B., Vitalii Patsula, Hana Macková, Andrii Mahun, Renáta Lehotská, Elena Piecková e Daniel Horák. "Silver-Sulfamethazine-Conjugated β-Cyclodextrin/Dextran-Coated Magnetic Nanoparticles for Pathogen Inhibition". Nanomaterials 14, n.º 4 (17 de fevereiro de 2024): 371. http://dx.doi.org/10.3390/nano14040371.
Texto completo da fonteLee, Jesang, e Seung Bum Park. "Extended Applications of Small-Molecule Covalent Inhibitors toward Novel Therapeutic Targets". Pharmaceuticals 15, n.º 12 (27 de novembro de 2022): 1478. http://dx.doi.org/10.3390/ph15121478.
Texto completo da fonteWalderveen, Maria Christina Van, Leslie Roy Berry, Helen Mary Atkinson e Anthony Kam Chuen Chan. "Covalent antithrombin-heparin effect on thrombin-thrombomodulin and activated protein C reaction with factor V/Va". Thrombosis and Haemostasis 103, n.º 05 (2010): 910–19. http://dx.doi.org/10.1160/th09-07-0473.
Texto completo da fonteAllgardsson, Anders, Lotta Berg, Christine Akfur, Andreas Hörnberg, Franz Worek, Anna Linusson e Fredrik J. Ekström. "Structure of a prereaction complex between the nerve agent sarin, its biological target acetylcholinesterase, and the antidote HI-6". Proceedings of the National Academy of Sciences 113, n.º 20 (2 de maio de 2016): 5514–19. http://dx.doi.org/10.1073/pnas.1523362113.
Texto completo da fonteLee, Chang-Uk, e Tom N. Grossmann. "Reversible Covalent Inhibition of a Protein Target". Angewandte Chemie International Edition 51, n.º 35 (13 de julho de 2012): 8699–700. http://dx.doi.org/10.1002/anie.201203341.
Texto completo da fonteAhmed, Vanessa F., Nunzio Bottini e Amy M. Barrios. "Covalent Inhibition of the Lymphoid Tyrosine Phosphatase". ChemMedChem 9, n.º 2 (8 de janeiro de 2014): 296–99. http://dx.doi.org/10.1002/cmdc.201300404.
Texto completo da fonteStevic, Ivan, Howard H. W. Chan, Ankush Chander, Leslie R. Berry e Anthony K. C. Chan. "Inhibition of Platelet-Prothrombianse by a Covalent Antithrombin-Heparin Complex." Blood 120, n.º 21 (16 de novembro de 2012): 2212. http://dx.doi.org/10.1182/blood.v120.21.2212.2212.
Texto completo da fonteZhou, Yuxin, Ji Tao, Dingshuainan Jin, Shiping Zhang, Yan He e Longlong Niu. "The Inhibition Effect and Mechnism of a Thiadiazole Derivative on Q235 Carbon Steel in 1 M HCl Solution". Applied Sciences 13, n.º 4 (6 de fevereiro de 2023): 2103. http://dx.doi.org/10.3390/app13042103.
Texto completo da fonteBuneeva, O. A., L. N. Aksenova e A. E. Medvedev. "A Simple Approach for Pilot Analysis of Time-dependent Enzyme Inhibition: Discrimination Between Mechanism-based Inactivation and Tight Binding Inhibitor Behavior". Biomedical Chemistry: Research and Methods 3, n.º 1 (2020): e00115. http://dx.doi.org/10.18097/bmcrm00115.
Texto completo da fonteWang, Qian, Guofeng Chen, Jian He, Jiameng Li, Muya Xiong, Haixia Su, Minjun Li, Hangchen Hu e Yechun Xu. "Structure-Based Design of Potent Peptidomimetic Inhibitors Covalently Targeting SARS-CoV-2 Papain-like Protease". International Journal of Molecular Sciences 24, n.º 10 (11 de maio de 2023): 8633. http://dx.doi.org/10.3390/ijms24108633.
Texto completo da fonteAbdeldayem, Ayah, Yasir S. Raouf, Stefan N. Constantinescu, Richard Moriggl e Patrick T. Gunning. "Advances in covalent kinase inhibitors". Chemical Society Reviews 49, n.º 9 (2020): 2617–87. http://dx.doi.org/10.1039/c9cs00720b.
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