Articles de revues sur le sujet « Macrodomains »
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Delgado-Rodriguez, Sofia E., Andrew P. Ryan, and Matthew D. Daugherty. "Recurrent Loss of Macrodomain Activity in Host Immunity and Viral Proteins." Pathogens 12, no. 5 (2023): 674. http://dx.doi.org/10.3390/pathogens12050674.
Texte intégralHaikarainen, Teemu, Mirko M. Maksimainen, Ezeogo Obaji, and Lari Lehtiö. "Development of an Inhibitor Screening Assay for Mono-ADP-Ribosyl Hydrolyzing Macrodomains Using AlphaScreen Technology." SLAS DISCOVERY: Advancing the Science of Drug Discovery 23, no. 3 (2017): 255–63. http://dx.doi.org/10.1177/2472555217737006.
Texte intégralHammond, Robert G., Norbert Schormann, Robert Lyle McPherson, Anthony K. L. Leung, Champion C. S. Deivanayagam, and Margaret A. Johnson. "ADP-ribose and analogues bound to the deMARylating macrodomain from the bat coronavirus HKU4." Proceedings of the National Academy of Sciences 118, no. 2 (2021): e2004500118. http://dx.doi.org/10.1073/pnas.2004500118.
Texte intégralRack, Johannes Gregor Matthias, Valentina Zorzini, Zihan Zhu, Marion Schuller, Dragana Ahel, and Ivan Ahel. "Viral macrodomains: a structural and evolutionary assessment of the pharmacological potential." Open Biology 10, no. 11 (2020): 200237. http://dx.doi.org/10.1098/rsob.200237.
Texte intégralEkblad, Torun, Patricia Verheugd, Anders E. Lindgren, Tomas Nyman, Mikael Elofsson, and Herwig Schüler. "Identification of Poly(ADP-Ribose) Polymerase Macrodomain Inhibitors Using an AlphaScreen Protocol." SLAS DISCOVERY: Advancing the Science of Drug Discovery 23, no. 4 (2018): 353–62. http://dx.doi.org/10.1177/2472555217750870.
Texte intégralKuri, Thomas, Klara K. Eriksson, Akos Putics, et al. "The ADP-ribose-1″-monophosphatase domains of severe acute respiratory syndrome coronavirus and human coronavirus 229E mediate resistance to antiviral interferon responses." Journal of General Virology 92, no. 8 (2011): 1899–905. http://dx.doi.org/10.1099/vir.0.031856-0.
Texte intégralHussain, Irfan, Nashaiman Pervaiz, Abbas Khan, et al. "Evolutionary and structural analysis of SARS-CoV-2 specific evasion of host immunity." Genes & Immunity 21, no. 6-8 (2020): 409–19. http://dx.doi.org/10.1038/s41435-020-00120-6.
Texte intégralLeung, Anthony K. L., Diane E. Griffin, Jürgen Bosch, and Anthony R. Fehr. "The Conserved Macrodomain Is a Potential Therapeutic Target for Coronaviruses and Alphaviruses." Pathogens 11, no. 1 (2022): 94. http://dx.doi.org/10.3390/pathogens11010094.
Texte intégralZapata-Pérez, Rubén, Fernando Gil-Ortiz, Ana Belén Martínez-Moñino, Antonio Ginés García-Saura, Jordi Juanhuix, and Álvaro Sánchez-Ferrer. "Structural and functional analysis of Oceanobacillus iheyensis macrodomain reveals a network of waters involved in substrate binding and catalysis." Open Biology 7, no. 4 (2017): 160327. http://dx.doi.org/10.1098/rsob.160327.
Texte intégralAlhammad, Yousef M. O., and Anthony R. Fehr. "The Viral Macrodomain Counters Host Antiviral ADP-Ribosylation." Viruses 12, no. 4 (2020): 384. http://dx.doi.org/10.3390/v12040384.
Texte intégralMcPherson, Robert Lyle, Rachy Abraham, Easwaran Sreekumar, et al. "ADP-ribosylhydrolase activity of Chikungunya virus macrodomain is critical for virus replication and virulence." Proceedings of the National Academy of Sciences 114, no. 7 (2017): 1666–71. http://dx.doi.org/10.1073/pnas.1621485114.
Texte intégralJia, Su-Jie, Si Jin, Fan Zhang, Fan Yi, William L. Dewey, and Pin-Lan Li. "Formation and function of ceramide-enriched membrane platforms with CD38 during M1-receptor stimulation in bovine coronary arterial myocytes." American Journal of Physiology-Heart and Circulatory Physiology 295, no. 4 (2008): H1743—H1752. http://dx.doi.org/10.1152/ajpheart.00617.2008.
Texte intégralGamble, Matthew J. "Expanding the functional repertoire of macrodomains." Nature Structural & Molecular Biology 20, no. 4 (2013): 407–8. http://dx.doi.org/10.1038/nsmb.2552.
Texte intégralXu, Guisheng, Haosu Luo, Zhenyi Qi, Haiqing Xu, and Zhiwen Yin. "Domain configurations in relaxor ferroelectric single crystals Pb(Mg1/3Nb2/3)O3–PbTiO3." Journal of Materials Research 16, no. 4 (2001): 932–37. http://dx.doi.org/10.1557/jmr.2001.0132.
Texte intégralZhang, Sixue, Atefeh Garzan, Nicole Haese, et al. "Pyrimidone inhibitors targeting Chikungunya Virus nsP3 macrodomain by fragment-based drug design." PLOS ONE 16, no. 1 (2021): e0245013. http://dx.doi.org/10.1371/journal.pone.0245013.
Texte intégralRack, Johannes Gregor Matthias, Dragutin Perina, and Ivan Ahel. "Macrodomains: Structure, Function, Evolution, and Catalytic Activities." Annual Review of Biochemistry 85, no. 1 (2016): 431–54. http://dx.doi.org/10.1146/annurev-biochem-060815-014935.
Texte intégralIqbal, Saleem, and Sheng-Xiang Lin. "Deep Drug Discovery of Mac Domain of SARS-CoV-2 (WT) Spike Inhibitors: Using Experimental ACE2 Inhibition TR-FRET Assay, Screening, Molecular Dynamic Simulations and Free Energy Calculations." Bioengineering 10, no. 8 (2023): 961. http://dx.doi.org/10.3390/bioengineering10080961.
Texte intégralWang, Xu-Ting, and Bin-Guang Ma. "Spatial Chromosome Organization and Adaptation of Escherichia coli under Heat Stress." Microorganisms 12, no. 6 (2024): 1229. http://dx.doi.org/10.3390/microorganisms12061229.
Texte intégralWazir, Sarah, Mirko M. Maksimainen, Heli I. Alanen, Albert Galera-Prat, and Lari Lehtiö. "Activity-Based Screening Assay for Mono-ADP-Ribosylhydrolases." SLAS DISCOVERY: Advancing the Science of Drug Discovery 26, no. 1 (2020): 67–76. http://dx.doi.org/10.1177/2472555220928911.
Texte intégralHoch, Nicolas C. "Host ADP-ribosylation and the SARS-CoV-2 macrodomain." Biochemical Society Transactions 49, no. 4 (2021): 1711–21. http://dx.doi.org/10.1042/bst20201212.
Texte intégralPardo, Lorena, Alvaro García, Klaus Brebøl, Elisa Mercadelli, and Carmen Galassi. "Characterization of Nanostructured Phases and Peculiar Phase Transitions in BNBT Lead-Free Piezoceramics." Advances in Science and Technology 90 (October 2014): 12–18. http://dx.doi.org/10.4028/www.scientific.net/ast.90.12.
Texte intégralLee, Hyunmi, Jimmy A. Rotolo, Judith Mesicek, et al. "Mitochondrial Ceramide-Rich Macrodomains Functionalize Bax upon Irradiation." PLoS ONE 6, no. 6 (2011): e19783. http://dx.doi.org/10.1371/journal.pone.0019783.
Texte intégralGarab, G., and L. Mustárdy. "Role of LHCII-containing macrodomains in the structure, function and dynamics of grana." Functional Plant Biology 26, no. 7 (1999): 649. http://dx.doi.org/10.1071/pp99069.
Texte intégralGarab, G., and L. Mustárdy. "Role of LHCII-containing macrodomains in the structure, function and dynamics of grana." Functional Plant Biology 27, no. 7 (2000): 723. http://dx.doi.org/10.1071/pp99069_c1.
Texte intégralGarab, G., and L. Mustárdy. "Role of LHCII-containing macrodomains in the structure, function and dynamics of grana." Functional Plant Biology 27, no. 3 (2000): 279. http://dx.doi.org/10.1071/pp99069_co.
Texte intégralLee, Hyunmi, Jimmy A. Rotolo, Judith Mesicek, et al. "Correction: Mitochondrial Ceramide-Rich Macrodomains Functionalize Bax upon Irradiation." PLOS ONE 10, no. 12 (2015): e0146210. http://dx.doi.org/10.1371/journal.pone.0146210.
Texte intégralFehr, Anthony R., Gytis Jankevicius, Ivan Ahel, and Stanley Perlman. "Viral Macrodomains: Unique Mediators of Viral Replication and Pathogenesis." Trends in Microbiology 26, no. 7 (2018): 598–610. http://dx.doi.org/10.1016/j.tim.2017.11.011.
Texte intégralLapaque, Nicolas, Frederique Forquet, Chantal de Chastellier, et al. "Characterization of Brucella abortus lipopolysaccharide macrodomains as mega rafts." Cellular Microbiology 8, no. 2 (2006): 197–206. http://dx.doi.org/10.1111/j.1462-5822.2005.00609.x.
Texte intégralJiang, A. Q., Z. H. Chen, W. H. Song, and L. D. Zhang. "Imaging the collapse of macrodomains from coupling defect-dipole relaxation." Physical Review B 61, no. 9 (2000): 5835–38. http://dx.doi.org/10.1103/physrevb.61.5835.
Texte intégralForst, Alexandra H., Tobias Karlberg, Nicolas Herzog, et al. "Recognition of Mono-ADP-Ribosylated ARTD10 Substrates by ARTD8 Macrodomains." Structure 21, no. 3 (2013): 462–75. http://dx.doi.org/10.1016/j.str.2012.12.019.
Texte intégralHuang, Yuwei, Ben Zucker, Shaojin Zhang, et al. "Migrasome formation is mediated by assembly of micron-scale tetraspanin macrodomains." Nature Cell Biology 21, no. 8 (2019): 991–1002. http://dx.doi.org/10.1038/s41556-019-0367-5.
Texte intégralSolymosi, K., K. Lenti, B. Myśliwa‐Kurdziel, J. Fidy, K. Strzałka, and B. Böddi. "Hg2+Reacts with Different Components of the NADPH: Protochlorophyllide Oxidoreductase Macrodomains." Plant Biology 6, no. 3 (2004): 358–68. http://dx.doi.org/10.1055/s-2004-817893.
Texte intégralZuev, L. B. "Kinetics of Localized Plasticity Macrodomains at the Prefracture Stage in Metals." Technical Physics 50, no. 12 (2005): 1636. http://dx.doi.org/10.1134/1.2148568.
Texte intégralMitra, Rishav, and James Fraser. "Role of conformational dynamics in the catalytic mechanism of viral macrodomains." Biophysical Journal 123, no. 3 (2024): 356a—357a. http://dx.doi.org/10.1016/j.bpj.2023.11.2156.
Texte intégralLesterlin, Christian, Romain Mercier, Frédéric Boccard, François‐Xavier Barre, and François Cornet. "Roles for replichores and macrodomains in segregation of the Escherichia coli chromosome." EMBO reports 6, no. 6 (2005): 557–62. http://dx.doi.org/10.1038/sj.embor.7400428.
Texte intégralIvry, Yachin, Vera Lyahovitskaya, Ilya Zon, Igor Lubomirsky, Ellen Wachtel, and Alexander L. Roytburd. "Enhanced pyroelectric effect in self-supported films of BaTiO3 with polycrystalline macrodomains." Applied Physics Letters 90, no. 17 (2007): 172905. http://dx.doi.org/10.1063/1.2730749.
Texte intégralAkbas, Mehmet A., Ian M. Reaney, and William E. Lee. "Domain structure-property relations in lead lanthanum zirconate titanate ceramics." Journal of Materials Research 11, no. 9 (1996): 2293–301. http://dx.doi.org/10.1557/jmr.1996.0292.
Texte intégralFijal, J., M. Zyla, and M. Tokarz. "Chemical, sorptive and morphological properties of montmorillonite treated with ammonium bifluoride (NH4HF2) solutions." Clay Minerals 20, no. 1 (1985): 81–92. http://dx.doi.org/10.1180/claymin.1985.020.1.07.
Texte intégralEspéli, Olivier, and Frédéric Boccard. "Organization of the Escherichia coli chromosome into macrodomains and its possible functional implications." Journal of Structural Biology 156, no. 2 (2006): 304–10. http://dx.doi.org/10.1016/j.jsb.2006.07.010.
Texte intégralHuang, Yuwei, Ben Zucker, Shaojin Zhang, et al. "Publisher Correction: Migrasome formation is mediated by assembly of micron-scale tetraspanin macrodomains." Nature Cell Biology 21, no. 10 (2019): 1301. http://dx.doi.org/10.1038/s41556-019-0389-z.
Texte intégralGhitescu, Lucian, Bruce S. Jacobson, and Philippe Crine. "A Novel, 85 KDA Endothelial Antigen Differentiates Plasma Membrane Macrodomains in Lung Alveolar Capillaries." Endothelium 6, no. 3 (1999): 241–50. http://dx.doi.org/10.3109/10623329909053414.
Texte intégralTan, Jinzhi, Clemens Vonrhein, Oliver S. Smart, et al. "The SARS-unique domain of SARS-CoV contains two macrodomains that bind G-quadruplexes." Acta Crystallographica Section A Foundations of Crystallography 65, a1 (2009): s143. http://dx.doi.org/10.1107/s0108767309097128.
Texte intégralYang, Hongyuan. "Abstract 1538 Phosphatidylserine regulates plasma membrane repair through the assembly of tetraspanin-enriched macrodomains." Journal of Biological Chemistry 300, no. 3 (2024): 106350. http://dx.doi.org/10.1016/j.jbc.2024.106350.
Texte intégralEnoki, Thais A., Haden L. Scott, Gerald W. Feigenson, and Frederick A. Heberle. "Inter- and Intra-Plane Interactions Control the Existence of Macrodomains in Asymmetric Giant Unilamellar Vesicles." Biophysical Journal 120, no. 3 (2021): 147a. http://dx.doi.org/10.1016/j.bpj.2020.11.1080.
Texte intégralDame, Remus T., Olga J. Kalmykowa, and David C. Grainger. "Chromosomal Macrodomains and Associated Proteins: Implications for DNA Organization and Replication in Gram Negative Bacteria." PLoS Genetics 7, no. 6 (2011): e1002123. http://dx.doi.org/10.1371/journal.pgen.1002123.
Texte intégralTan, Jinzhi, Clemens Vonrhein, Oliver S. Smart, et al. "The SARS-Unique Domain (SUD) of SARS Coronavirus Contains Two Macrodomains That Bind G-Quadruplexes." PLoS Pathogens 5, no. 5 (2009): e1000428. http://dx.doi.org/10.1371/journal.ppat.1000428.
Texte intégralKaramyshev, Dmytro, Valentyn Suvorov, and Roman Sobol. "OVERCOMING SYSTEMIC VULNERABILITIES OF THE SPHERES OF INFLUENCE OF HYBRID THREATS IN ENSURING STABILITY AND COMPREHENSIVE SECURITY IN THE CONDITIONS OF EUROPEAN INTEGRATION." Public Administration and Regional Development, no. 24 (February 7, 2024): 628–47. http://dx.doi.org/10.34132/pard2024.24.14.
Texte intégralPileni, M. P. "Control of the Size and Shape of Inorganic Nanocrystals at Various Scales from Nano to Macrodomains." Journal of Physical Chemistry C 111, no. 26 (2007): 9019–38. http://dx.doi.org/10.1021/jp070646e.
Texte intégralBoekema, Egbert J., Jan F. L. van Breemen, Henny van Roon, and Jan P. Dekker. "Arrangement of photosystem II supercomplexes in crystalline macrodomains within the thylakoid membrane of green plant chloroplasts." Journal of Molecular Biology 301, no. 5 (2000): 1123–33. http://dx.doi.org/10.1006/jmbi.2000.4037.
Texte intégralSpiliotis, Elias T., and Michael A. McMurray. "Masters of asymmetry – lessons and perspectives from 50 years of septins." Molecular Biology of the Cell 31, no. 21 (2020): 2289–97. http://dx.doi.org/10.1091/mbc.e19-11-0648.
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