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Supramolecular chemistry, v.28 no.5/6, 2016년, pp.575 - 581
Peacock, Hayden (Chemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK) , Thinnes, Cyrille C. (Chemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK) , Kawamura, Akane (Chemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK) , Hamilton, Andrew D. (Chemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK)
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Tessarz, Peter, Kouzarides, Tony. Histone core modifications regulating nucleosome structure and dynamics. Nature reviews. Molecular cell biology, vol.15, no.11, 703-708.
Zhang, Xi, Huang, Yaling, Shi, Xiaobing. Emerging roles of lysine methylation on non-histone proteins. Cellular and molecular life sciences : CMLS, vol.72, no.22, 4257-4272.
Greer, Eric L., Shi, Yang. Histone methylation: a dynamic mark in health, disease and inheritance. Nature reviews. Genetics, vol.13, no.5, 343-357.
Barski, Artem, Cuddapah, Suresh, Cui, Kairong, Roh, Tae-Young, Schones, Dustin E., Wang, Zhibin, Wei, Gang, Chepelev, Iouri, Zhao, Keji. High-Resolution Profiling of Histone Methylations in the Human Genome. Cell, vol.129, no.4, 823-837.
Musselman, Catherine A, Lalonde, Marie-Eve, C척t챕, Jacques, Kutateladze, Tatiana G. Perceiving the epigenetic landscape through histone readers. Nature structural & molecular biology, vol.19, no.12, 1218-1227.
Bannister, Andrew J., Kouzarides, Tony. Reversing histone methylation. Nature, vol.436, no.7054, 1103-1106.
Wagner, Tobias, Robaa, Dina, Sippl, Wolfgang, Jung, Manfred. Mind the Methyl: Methyllysine Binding Proteins in Epigenetic Regulation. ChemMedChem : Chemistry Enabling Drug Discovery, vol.9, no.3, 466-483.
Allen, Hillary F., Daze, Kevin D., Shimbo, Takashi, Lai, Anne, Musselman, Catherine A., Sims, Jennifer K., Wade, Paul A., Hof, Fraser, Kutateladze, Tatiana G.. Inhibition of histone binding by supramolecular hosts. The Biochemical journal, vol.459, no.3, 505-512.
Thinnes, Cyrille C., England, Katherine S., Kawamura, Akane, Chowdhury, Rasheduzzaman, Schofield, Christopher J., Hopkinson, Richard J.. Targeting histone lysine demethylases — Progress, challenges, and the future ☆. Biochimica et biophysica acta. Gene regulatory mechanisms, vol.1839, no.12, 1416-1432.
Shaurya, Alok, Dubicki, Krystyn I., Hof, Fraser. Chemical agents for binding post-translationally methylated lysines and arginines. Supramolecular chemistry, vol.26, no.7, 583-590.
Beshara, Cory S., Jones, Catherine E., Daze, Kevin D., Lilgert, Brandin J., Hof, Fraser. A Simple Calixarene Recognizes Post-translationally Methylated Lysine. Chembiochem : a European journal of chemical biology, vol.11, no.1, 63-66.
Daze, Kevin D., Pinter, Thomas, Beshara, Cory S., Ibraheem, Andreas, Minaker, Samuel A., Ma, Manuel C. F., Courtemanche, Rebecca J. M., Campbell, Robert E., Hof, Fraser. Supramolecular hosts that recognize methyllysines and disrupt the interaction between a modified histone tail and its epigenetic reader protein. Chemical science, vol.3, no.9, 2695-.
Pinkin, Nicholas K., Waters, Marcey L.. Development and mechanistic studies of an optimized receptor for trimethyllysine using iterative redesign by dynamic combinatorial chemistry. Organic & biomolecular chemistry, vol.12, no.36, 7059-7067.
Gamal-Eldin, Mona A., Macartney, Donal H.. Selective molecular recognition of methylated lysines and arginines by cucurbit[6]uril and cucurbit[7]uril in aqueous solution. Organic & biomolecular chemistry, vol.11, no.3, 488-495.
Tan, Song-De, Chen, Wen-Hua, Satake, Akiharu, Wang, Bo, Xu, Zun-Le, Kobuke, Yoshiaki. Tetracyanoresorcin[4]arene as a pH dependent artificial acetylcholine receptor. Organic & biomolecular chemistry, vol.2, no.19, 2719-2721.
Chen, Wen-Hua, Nishikawa, Masanori, Tan, Song-De, Yamamura, Mika, Satake, Akiharu, Kobuke, Yoshiaki. Tetracyanoresorcin[4]arene ion channel shows pH dependent conductivity change. Chemical communications : Chem comm, vol.2004, no.7, 872-873.
Yoshida, Isao, Yamamoto, Nobuhiro, Sagara, Fumio, Ishii, Daido, Ueno, Keihei, Shinkai, Seiji. Re-evaluation of the Acid Dissociation Constants of the Hydroxyl Groups in Tetrasodium 25,26,27,28-Tetrahydroxycalix[4]arene-5,11,17,23-tetrasulfonate. Bulletin of the Chemical Society of Japan, vol.65, no.4, 1012-1015.
McGovern, R처ise E., Fernandes, Humberto, Khan, Amir R., Power, Nicholas P., Crowley, Peter B.. Protein camouflage in cytochrome c？?calixarene complexes. Nature chemistry, vol.4, no.7, 527-533.
Chen, Wen-Hua, Wei, Ying, Tan, Song-De, Wang, Bo, Xu, Zun-Le. Spectrometric Study of the Size Discrimination of Quaternary Ammonium Cations by Tetracyanoresorcin[4]arene. Supramolecular chemistry, vol.17, no.6, 469-473.
McGovern, Róise E., Snarr, Brendan D., Lyons, Joseph A., McFarlane, James, Whiting, Amanda L., Paci, Irina, Hof, Fraser, Crowley, Peter B.. Structural study of a small molecule receptor bound to dimethyllysine in lysozyme. Chemical science, vol.6, no.1, 442-449.
Murayama, Kazutaka, Aoki, Katsuyuki. Molecular recognition involving multiple cation–π interactions: the inclusion of the acetylcholine trimethylammonium moiety in resorcin[4]arene. Chemical communications : Chem comm, vol.1997, no.1, 119-120.
The trimethylammonium group of Lys(Me 3 ) was located in the centre of the host’s cavity in all of the generated docking poses. However, the location of the remaining atoms of Lys(Me 3 ) varied significantly, indicating that there is conformational flexibility within the ligand.
10.1023/A:1020404220640
Job’s plots (included in Supplementary Information) confirmed a 1:1 binding stiochiometry for the guests. The Cε methylene proton signals were plotted in favor of the N -methyl proton signals because these became too broad to observe during the middle points of the titration.
10.1002/chem.201502302 Pinkin, N.K.; Liu, I.; Abron, J.D.; Waters, M.L. Chem. Eur. J. 2015, 21 , 17981-17986.http://dx.doi.org/10.1002/chem.201502302 (Epub ahead of print).
Guerra-Calderas, L., Gonzalez-Barrios, R., Herrera, L.A., Cantu de Leon, D., Soto-Reyes, E.. The role of the histone demethylase KDM4A in cancer. Cancer genetics, vol.208, no.5, 215-224.
Ng, Stanley S., Kavanagh, Kathryn L., McDonough, Michael A., Butler, Danica, Pilka, Ewa S., Lienard, Benoit M. R., Bray, James E., Savitsky, Pavel, Gileadi, Opher, von Delft, Frank, Rose, Nathan R., Offer, John, Scheinost, Johanna C., Borowski, Tomasz, Sundstrom, Michael, Schofield, Christopher J., Oppermann, Udo. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Nature, vol.448, no.7149, 87-91.
Molecular Operating Environment (MOE). 2014.09; Chemical Computing Group Inc., Montreal, 2015. Ed.
http://community.dur.ac.uk/j.m.sanderson/science/downloads.html
Chowdhury, Rasheduzzaman, Yeoh, Kar Kheng, Tian, Ya‐Min, Hillringhaus, Lars, Bagg, Eleanor A, Rose, Nathan R, Leung, Ivanhoe K H, Li, Xuan S, Woon, Esther C Y, Yang, Ming, McDonough, Michael A, King, Oliver N, Clifton, Ian J, Klose, Robert J, Claridge, Timothy D W, Ratcliffe, Peter J, Schofield, Christopher J, Kawamura, Akane. The oncometabolite 2‐hydroxyglutarate inhibits histone lysine demethylases. EMBO reports, vol.12, no.5, 463-469.
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