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| Y. Fujioka, J. M. Alam, D. Noshiro, K. Mouri, T. Ando, Y. Okada, A. I. May, R. L. Knorr, K. Suzuki, Y. Ohsumi, N. N. Noda, “Phase separation organizes the site of autophagosome formation”, Nature 578, 301-305 (2020). |
| S. Sakamoto, T. Komatsu, R. Watanabe, Y. Zhang, T. Inoue, M. Kawaguchi, H. Nakagawa, T. Ueno, T. Okusaka, K. Honda, H. Noji, and Y. Urano, “Multiplexed single-molecule enzyme activity analysis for counting disease-related proteins in biological samples”, Science Advances 6, eaay0888 (2020). |
| T. Hamaguchi and K. Yonekura, “Tidy up cryo-EM sample grids with 3D printed tools”, J. Struct. Biol. 209, 107414 (2020). |
| R. Umeda, Y. Satouh, M. Takemoto, Y. Nakada-Nakura, K. Liu, T. Yokoyama, M. Shirouzu, S. Iwata, N. Nomura, K. Sato, M. Ikawa, T. Nishizawa and O. Nureki, “Structural insights into tetraspanin CD9 function.”, Nat Commun 11(1), 1606 (2020) DOI: 10.1038/s41467-020-15459-7. |
| A. Marintchev and T. Ito, “eIF2B and the integrated stress response: a structural and mechanistic view”, Biochemistry 59, 1299-1308 (2020) DOI: 10.1021/acs.biochem.0c00132 |
| T. Mori and S. Sekine “Overview of the “1SBA: integrative approaches towards understanding of gene expression” session at the 57th BSJ meeting”, Biophys Rev. (2020) DOI: 10.1007/s12551-020-00644-1. |
| K. Weiss, HP. Lazar, A. Kurolap, AF. Martinez, T. Paperna, L. Cohen, MF. Smeland, S. Wallen, H. Solveig, B. Keren, P. Terhal, M. Irving, M. Takaku, JD. Roberts, RM. Petrovich, SA. Schrier Vergano, A. Kenney, H. Hove, E. DeChene, SC. Quinonez, E. Colin, A. Ziegler, M. Rumple, M. Jain, D. Monteil, ER. Roeder, K. Nugent, A. van Haeringen, M. Gambello, A. Santani, L. Medne, B. Krock, CM. Skraban, EH. Zackai, HA. Dubbs, T. Smol, J. Ghoumid, MJ. Parker, M. Wright, P. Turnpenny, J. Clayton-Smith, K. Metcalfe, H. Kurumizaka, BD. Gelb, H. Baris Feldman, PM. Campeau, M. Muenke, PA. Wade, and K. Lachlan. “The CHD4-related syndrome: a comprehensive investigation of the clinical spectrum, genotype-phenotype correlations, and molecular basis”, Genet Med. 22, 389-397 (2020) |
| Y. Takizawa, CH. Ho, H. Tachiwana, H. Matsunami, W. Kobayashi, M. Suzuki, Y. Arimura, T. Hori, T. Fukagawa, MD. Ohi, M. Wolf, and H. Kurumizaka. “Cryo-EM Structures of Centromeric Tri-nucleosomes Containing a Central CENP-A Nucleosome” Structure, 28, 44-53 (2020) |
| T. Kujirai, and H. Kurumizaka, “Transcription through the nucleosome” Current Opinion in Structural Biology, 61, 42-49 (2020) |
| H. Yuzurihara, Y. Aizawa, M. Saotome, Y. Ichikawa, H. Yokoyama, Y. Chikashige, T. Haraguchi, Y. Hiraoka, H. Kurumizaka, and W. Kagawa, Improved Methods for Preparing the Telomere Tethering Complex Bqt1-Bqt2 for Structural Studies. Protein J., 39, 174-181 (2020) |
| R. Fujita, T. Yamamoto, Y. Arimura, S. Fujiwara, H. Tachiwana, Y. Ichikawa, Y. Sakata, L. Yang, R. Maruyama, M. Hamada, M. Nakao, N. Saitoh, and H. Kurumizaka, Nucleosome destabilization by nuclear non-coding RNAs. Commun. Biol., 3, 60. (2020) |
| K. Saikusa, D. Kato, A. Nagadoi, H. Kurumizaka, and Akashi, S. Native Mass Spectrometry of Protein and DNA Complexes Prepared in Nonvolatile Buffers. J. Am. Soc. Mass Spectrom., 31, 711-718 (2020) |
| T. Mori and Y. Sugita, “Implicit micelle model for membrane proteins using superellipsoid approximation”, J. Chem. Theory Comput., 16, 711-724 (2020). |
| D. Matsuoka, M. Kamiya, T. Sato, Y. Sugita, “Role of the N-Terminal Transmembrane Helix Contacts in the Activation of FGFR3”, J. Comput. Chem., 41, 561-572 (2020). |
| Tiwari SP, Chhabra S, Tama F, Miyashita O. “Computational Protocol for Assessing the Optimal Pixel Size to Improve the Accuracy of Single-particle Cryo-electron Microscopy Maps”, J Chem Inf Model., 60, 2570-2580 (2020). |
| Dasgupta B, Miyashita O, Tama F. “Reconstruction of low-resolution molecular structures from simulated atomic force microscopy images”, Biochim Biophys Acta Gen Subj. 1864, 129420 (2020). |
| H. Kouno, K. Orihashi, K. Nishimura, Y. Kawashima, K. Tateishi, T. Uesaka, N. Kimizuka, N. Yanai, “Triplet dynamic nuclear polarization of crystalline ice using water-soluble polarizing agents”, Chem. Commum. 56, 3717-3720 (2020). |
| M. Inoue, T. Hayashi, S. Hikiri, M. Ikeguchi, and M. Kinoshita, “Hydration properties of a protein at low and high pressures: Physics of pressure denaturation”, J. Chem. Phys., 152, 065103 (2020). |
| T. Sunami, Y. Hirano, T. Tamada, and H. Kono, “Structural basis for an array of engrailed homeodomains”. Acta Crystallographica Section D (Accepted). |
| H. Ehara, T. Kujirai, Y. Fujino, M. Shirouzu, H. Kurumizaka, S-I. Sekine, “Structural insight into nucleosome transcription by RNA polymerase II with elongation factors”, Science 363, 744-747 (2019). |
| B. G. David, H. Fujita, K. Yasuda, K. Okamoto, Y. Panina, J. Ichinose, O. Sato, M. Horie, T. Ichimura, Y. Okada, T. M. Watanabe, “Linking substrate and nucleus via actin cytoskeleton in pluripotency maintenance of mouse embryonic stem cells”, Stem Cell Research 41, 101614-101614 (2019). |
| J. Kaneshiro, Y. Okada, T. Shima, M. Tsuji, K. Imada, T. Ichimura, T. M. Watanabe, “Second harmonic generation polarization microscopy as a tool for protein structure analysis”, Biophys Physbiol. 16, 147-157 (2019). |
| C. Wang, M. Taki, Y. Sato, Y. Tamura, H. Yaginuma, Y. Okada, S. Yamaguchi, “A photostable fluorescent marker for the superresolution live imaging of the dynamic structure of the mitochondrial cristae”, Proc Natl Acad Sci U S A 116, 15817-15822 (2019). |
| H. Tanaka, T. Okazaki, S. Aoyama, M. Yokota, M. Koike, Y. Okada, Y. Fujiki, Y. Gotoh, “Peroxisomes control mitochondrial dynamics and the mitochondrion-dependent apoptosis pathway”, J Cell Sci 132, jcs224766 (2019). |
| K. Kono, S. Yoshiura, I. Fujita, Y. Okada, A. Shitamukai, T. Shibata, F. Matsuzaki, “Reconstruction of Par-dependent polarity in apolar cells reveals a dynamic process of cortical polarization”, eLife 8, e45559 (2019). |
| C. H. Lu, W. C. Tang, Y. T. Liu, S. W. Chang, F. C. M. Wu, C. Y. Chen, Y. C. Tsai, S. M. Yang, C. W. Kuo, Y. Okada, Y. K. Hwu, P. Chen, B. C. Chen, “Lightsheet localization microscopy enables fast, large-scale, and three-dimensional super-resolution imaging”, Commun Biol 2, 177 (2019). |
| J. Li, K. Suda, I. Ueoka, R. Tanaka, H. Yoshida, Y. Okada, Y. Okamoto, Y. Hiramatsu, H. Takashima, M. Yamaguchi, “Neuron-specific knockdown of Drosophila HADHB induces a shortened lifespan, deficient locomotive ability, abnormal motor neuron terminal morphology and learning disability”, Exp Cell Res 379, 150-158 (2019). |
| S. Hasegawa, T. Sagawa, K. Ikeda, Y. Okada, K. Hayashi, “Investigation of multiple-dynein transport of melanosomes by non-invasive force measurement using fluctuation unit χ”, Sci. Rep 9, 5099, (2019). |
| Suga, M., Akita, F., Yamashita, K., Nakajima, Y., Ueno, G., Li, H., Yamane, T., Hirata, K., Umena, Y., Yonekura, S., Yu, L.-J., Murakami, H., Nomura, T., Kimura, T., Kubo, M., Baba, S., Kumasaka, T., Tono, K., Yabashi, M., Isobe, H., Yamaguchi, K. Yamamoto, M., Ago, H., Shen, J.-R. “An oxyl/oxo mechanism for oxygen-oxygen coupling in PSII revealed by an X-ray free electron laser”, Science 366, 334-338 (2019). |
| T. Yokoyama, K. Machida, W. Iwasaki, T. Shigeta, M. Nishimoto, M. Takahashi, A. Sakamoto, M. Yonemochi, Y. Harada, H. Shigematsu, M. Shirouzu, H. Tadakuma, H. Imataka, and T. Ito, “HCV IRES Captures an Actively Translating 80S Ribosome”, Mol. Cell 74, 1205-1214 (2019). DOI: 10.1016/j.molcel.2019.04.022 |
| K. Kashiwagi, T. Yokoyama, M. Nishimoto, M. Takahashi, A. Sakamoto, M. Yonemochi, M. Shirouzu, and T. Ito, “Structural basis for eIF2B inhibition in integrated stress response”, Science 364, 495-499 (2019). DOI: 10.1126/science.aaw4104. |
| S. Iwasaki, W. Iwasaki, M. Takahashi, A. Sakamoto, C. Watanabe, Y. Shichino, S. N. Floor, K. Fujiwara, M. Mito, K. Dodo, M. Sodeoka, H. Imataka, T. Honma, K. Fukuzawa, T. Ito and N. T. Ingolia, “The Translation Inhibitor Rocaglamide Targets a Bimolecular Cavity between eIF4A and Polypurine RNA”, Mol. Cell 73, 738-748 (2019). DOI: 10.1016/j.molcel.2018.11.026. |
| R. Hirano, T. Kujirai, L. Negishi, and H. Kurumizaka. “Biochemical characterization of the placeholder nucleosome for DNA hypomethylation maintenance” Biochem Biophys Rep., 18, 100634, (2019) |
| Kobayashi W, Takizawa Y, Aihara M, Negishi L, Ishii H, and Kurumizaka H. “Structural and biochemical analyses of the nuclear pore complex component ELYS identify residues responsible for nucleosome binding” Commun Biol., 2, 163, (2019) |
| N. Horikoshi, T. Kujirai, K. Sato, H. Kimura, and H. Kurumizaka. “Structure-based design of an H2A.Z.1 mutant stabilizing a nucleosome in vitro and in vivo” Biochem Biophys Res Commun., 515, 719-724, (2019) |
| CI. Chung, Y. Sato, Y. Ohmuro-Matsuyama, S. Machida, H. Kurumizaka, H. Kimura, H. and Ueda. “Intrabody-based FRET probe to visualize endogenous histone acetylation” Sci Rep. 9, 10188 (2019) |
| S. Sato, Y. Arimura, T. Kujirai, A. Harada, K. Maehara, J. Nogami, Y. Ohkawa, and H. Kurumizaka. “Biochemical analysis of nucleosome targeting by Tn5 transposase” Open Biol. 9, 190116, (2019) |
| R. Sugiyama, K. Kasho, K. Miyoshi, S. Ozaki, W. Kagawa, and H. Kurumizaka, T. Katayama. “A novel mode of DnaA–DnaA interaction promotes ADP dissociation for reactivation of replication initiation activity” Nucleic Acids Res., 47, 11209-11224 (2019) |
| E. Oya, R. Nakagawa, Y. Yoshimura, M. Tanaka, G. Nishibuchi, S. Machida, A. Shirai, K. Ekwall, H. Kurumizaka, H. Tagami, and JI. Nakayama. “H3K14 ubiquitylation promotes H3K9 methylation for heterochromatin assembly” EMBO Rep., 20, e48111 (2019) |
| W. Kobayashi, and H. Kurumizaka. “Structural transition of the nucleosome during chromatin remodeling and transcription” Curr Opin Struct Biol., 29, 107-114 (2019) |
| M. Saotome, N. Horikoshi, K. Urano, T. Kujirai, H. Yuzurihara, H. Kurumizaka, and W. Kagawa. “Structure determination of the nucleosome core particle by selenium SAD phasing” Acta Crystallogr D Struct Biol. 75, 930-936 (2019) |
| M. Dacher, H. Tachiwana, N. Horikoshi, T. Kujirai, H. Taguchi, H. Kimura, H. Kurumizaka. “Incorporation and influence of Leishmania histone H3 in chromatin” Nucleic Acids Res., 47, 11637-11648 (2019) |
| S. Matsumoto, S. Cavadini, RD. Bunker, RS. Grand, A. Potenza, J. Rabl, J. Yamamoto, AD. Schenk, D. Schübeler, S. Iwai, K. Sugasawa, H. Kurumizaka, and NH. Thomä. “DNA damage detection in nucleosomes involves DNA register shifting” Nature, 571, 79-84 (2019) |
| A. Kumar, K. Y. J. Zhang, “Improving ligand 3D shape similarity-based pose prediction with a continuum solvent model”. J. Comput-Aided Mol. Des., 33, 1045-1055 (2019). |
| A. Kumar, K. Y. J. Zhang, “Shape similarity guided pose prediction: Lessons from D3R Grand Challenge 3”. J. Comput-Aided Mol. Des., 33, 47-59 (2019). |
| T. Mori, M. Kulik, O. Miyashita, J. Jung, F. Tama, and Y. Sugita, “Acceleration of cryo-EM flexible fitting for large biomolecular systems by efficient space partitioning”, Structure, 27, 161-174 (2019). |
| M. Sakakura, Y. Ohkubo, H. Oshima, S. Re, M. Ito, Y. Sugita, H. Takahashi “Structural mechanisms underlying activity changes in an AMPA-type glutamate receptor induced by substitutions in its ligand-binding domain”, Structure, 27, 1698–1709 (2019). |
| H. Oshima, S. Re, M. Sakakura, H. Takahashi, Y. Sugita, “Population Shift Mechanism for Partial Agonism of AMPA Receptor”, Biophys. J., 116, 57-68 (2019). |
| K. Tateishi, M. Negoro, H. Nonaka, A. Kagawa, S. Sando, S. Wada, M. Kitagawa, T. Uesaka, “Dynamic nuclear polarization with photo-excited triplet electrons using 6,13-diphenylpentacene”, Phys. Chem. Chem. Phys. 21, 19737-19741 (2019). |
| K. Nishimura, H. Kouno, K. Tateishi, T. Uesaka, K. Ideta, N. Kimizuka, N. Yanai, “Triplet dynamic nuclear polarization of nanocrystals dispersed in water at room temperature”, Phys. Chem. Chem. Phys. 21, 16408-16412 (2019). |
| H. Kouno, Y. Kawashima, K. Tateishi, T. Uesaka, N. Kimizuka, N. Yanai, “Non-Pentacene Polarizing Agents with Improved Air-Stability for Triplet Dynamic Nuclear Polarization at Room Temperature”, J. Phys. Chem. Lett. 10, 2208-2213 (2019). |
| W. Li, J. Wang, J. Zhang, S. Takada, W. Wang, “Overcoming the Bottleneck of the Enzymatic Cycle by Steric Frustration”, Phys. Rev. Lett., 122, 238102 (2019). |
| R. Kanada, T. Terakawa, H. Kenzaki, S. Takada, “Nucleosome Crowding in Chromatin Slows the Diffusion but Can Promote Target Search of Proteins”, Biophys. J., 116, 2285 (2019) |
| T. Yamada, T. Hayashi, S. Hikiri, N. Kobayashi, H. Yanagawa, M. Ikeguchi, M. Katahira, T. Nagata, and M. Kinoshita, “How Does the Recently Discovered Peptide MIP Exhibit Much Higher Binding Affinity than an Anticancer Protein p53 for an Oncoprotein MDM2?”, J. Chem. Inf. Model., 59, 3533-3544 (2019). |
| T. Ekimoto, Y. Kokabu, T. Oroguchi, M. Ikeguchi, “Combination of coarse-grained molecular dynamics simulations and small-angle x-ray scattering experiments”, Biophys. Physicobiol., 16, 377-390 (2019). |
| S. Hikiri, T. Hayashi, M.Inoue, T. Ekimoto, M. Ikeguchi, and M. Kinoshita, “An accurate and rapid method for calculating hydration free energies of a variety of solutes including proteins”, J. Chem. Phys., 150, 175101-1-12 (2019). |
| A. Singharoy, C. Chipot, T. Ekimoto, K. Suzuki, M. Ikeguchi, I. Yamato, and T. Murata, “Rotational mechanism model of the bacterial V1 motor based on structural and computational analyses”, Front. Physiol., 10:46, 1-12 (2019). |
| T. Sunami and H. Kono, “Balance between DNA-binding affinity and specificity enables selective recognition of longer target sequences in vivo”. Protein Science, 28, 1630-1639 (2019). |
| T. Kujirai, H. Ehara, Y. Fujino, M. Shirouzu, S. Sekine, and H. Kurumizaka, “Structural basis of the nucleosome transition during RNA polymerase II passage”, Science 362, 595-598 (2018). |
| T. Shima, M. Morikawa, J. Kaneshiro, T. Kambara, S. Kamimura, T. Yagi, H. Iwamoto, S. Uemura, H. Shigematsu, M. Shirouzu, T. Ichimura, TM. Watanabe, R. Nitta, Y. Okada, and N. Hirokawa, “Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport”, J. Cell Biol. jcb.201711178 (2018). |
| H. Ehara, and S. Sekine, “Architecture of the RNA polymerase II elongation complex new insights into Spt4/5 and Elf1”, Transcription 9, 286-291 (2018). |
| S. Inouye, Y. Tomabechi, T. Hosoya, S. Sekine, and M. Shirouzu, “Slow luminescence kinetics of semi-synthetic aequorin: expression, purification and structure determination of cf3-aequorin”, J. Biochem. 164, 247-255 (2018). |
| G. Kasuya, T. Nakane, T. Yokoyama, Y. Jia, M. Inoue, K. Watanabe, R. Nakamura, T. Nishizawa, T. Kusakizako, A. Tsutsumi, H. Yanagisawa, N. Dohmae, M. Hattori, H. Ichijo, Z. Yan, M. Kikkawa, M. Shirouzu, R. Ishitani, and O. Nureki, “Cryo-EM structures of the human volume-regulated anion channel LRRC8”, Nat. Struct. Mol. Biol. 25, 797-804 (2018). |
| K. Katsura, Y. Tomabechi, T. Matsuda, M. Yonemochi, J. Mikuni, N. Ohsawa, T. Terada, S. Yokoyama, M. Kukimoto-Niino, C. Takemoto, and M. Shirouzu, “Phosphorylated and non-phosphorylated HCK kinase domains produced by cell-free protein expression”, Protein Expr. Purif. 150, 92-99 (2018). |
| T. Matsuda, T. Ito, C. Takemoto, K. Katsura, M. Ikeda, M. Wakiyama, M. Kukimoto-Niino, S. Yokoyama, Y. Kurosawa, and M. Shirouzu, “Cell-free synthesis of functional antibody fragments to provide a structural basis for antibody-antigen interaction”, PLoS One. 13, e0193158 (2018). |
| N. Ohbayashi, K. Murayama, M. Kato-Murayama, M. Kukimoto-Niino, T. Uejima, T. Matsuda, N. Ohsawa, S. Yokoyoma, H. Nojima, and M. Shirouzu, “Structural Basis for the Inhibition of Cyclin G-Associated Kinase by Gefitinib”, ChemistryOpen. 7, 721-727 (2018). |
| W.-Y. Ooi, Y. Murayama, V. Mekler, L. Minakhin, K. Severinov, S. Yokoyama, and S. Sekine, “A Thermus phage protein inhibits host RNA polymerase by preventing template DNA strand loading during open promoter complex formation”, Nucleic Acids Res. 46, 431-441 (2018). |
| H. Shigematsu, T. Imasaki, C. Doki, T. Sumi, M. Aoki, T. Uchikubo-Kamo, A. Sakamoto, K. Tokuraku, M. Shirouzu and R. Nitta, “Structural insight into microtubule stabilization and kinesin inhibition by Tau family MAPs”, J. Cell Biol. jcb.201711182 (2018). |
| T. Sumi, T. Imasaki, M. Aoki, N. Sakai, E. Nitta, M. Shirouzu, and R. Nitta, “Structural Insights into the Altering Function of CRMP2 by Phosphorylation”, Cell Struct. Funct. 43, 15-23 (2018). |
| J. Tamogami, T. Kikukawa, K. Ohkawa, N. Ohsawa, T. Nara, M. Demura, S. Miyauchi, T. Kimura-Someya, M. Shirouzu, S. Yokoyama, K. Shimono, and N. Kamo, “Interhelical interactions between D92 and C218 in the cytoplasmic domain regulate proton uptake upon N-decay in the proton transport of Acetabularia rhodopsin II”, J. Photochem. Photobiol. B 183, 35-45 (2018). |
| A. Yamagata, Y. Miyazaki, N. Yokoi, H. Shigematsu, Y. Sato, S. Goto-Ito, A. Maeda, T. Goto, M. Sanbo, M. Hirabayashi, M. Shirouzu, Y. Fukata, M. Fukata, S. Fukai, “Structural basis of epilepsy-related ligand-receptor complex LGI1-ADAM22”, Nat. Commun. 9, 1546 (2018). |
| K. Hayashi, Y. Tsuchizawa, M. Iwaki, and Y. Okada, “Application of the fluctuation theorem for non-invasive force measurement in living neuronal axons”, Mol. Biol. Cell. 10.1091/mbc.E18-01-0022 (2018). |
| M. Gzrybowski, M. Taki, K. Senda, Y. Sato, T. Ariyoshi, Y. Okada, R. Kawakami, T. Imamura, and S. Yamaguchi, “A highly photostable near-infrared labeling agent based on a phospha-rhodamine for long-term and deep imaging”, Angew. Chem. 57,10137-10141 (2018). |
| H. Asada, S. Horita, K. Hirata, M. Shiroishi, Y. Shiimura, H. Iwanari, T. Hamakubo, T. Shimamura, N. Nomura, O. Kusano-Arai, T. Uemura, C. Suno, T. Kobayashi, and S. Iwata, “Crystal structure of the human angiotensin II type 2 receptor bound to an angiotensin II analog”, Nat. Struct. Mol. Biol. 25, 570-576 (2018). |
| K. Yamashita, K. Hirata, and M. Yamamoto, “KAMO: towards automated data processing for microcrystals”, Acta Cryst. D74, 441–449 (2018). |
| T. Hori, T. Okuno, K. Hirata, K. Yamashita, Y. Kawano, M. Yamamoto, M. Hato, M. Nakamura, T. Shimizu, T. Yokomizo, M. Miyano, and S. Yokoyama, “Na+-mimicking ligands stabilize the inactive state of leukotriene B4 receptor BLT1”, Nat. Chem. Biol. 14, 262-269 (2018). |
| T. P. Halsted, K. Yamashita, K. Hirata, H. Ago, G. Ueno, T. Tosha, R. Eady, S. Antonyuk, M. Yamamoto, and S. S. Hasnain, “An unprecedented dioxygen species revealed by serial femtosecond rotation crystallography in copper nitrite reductase”, IUCrJ 5, 22-31 (2018). |
| S. Machida, Y. Takizawa, M. Ishimaru, Y. Sugita, S. Sekine, J. Nakayama, M. Wolf, and H. Kurumizaka, “Structural Basis of Heterochromatin Formation by Human HP1”, Mol. Cell. 69, 385-397 (2018). |
| K. Shiraishi, A. Shindo, A. Harada, H. Kurumizaka, H. Kimura, Y. Ohkawa, and H. Matsuyama, “Roles of histone H3.5 in human spermatogenesis and spermatogenic disorders”, Andrology 6, 158-165 (2018). |
| A. Fukuto, M. Ikura, T. Ikura, J. Sun, Y. Horikoshi, H. Shima, K. Igarashi, M. Kusakabe, M. Harata, N. Horikoshi, H. Kurumizaka, Y. Kiuchi, and S. Tashiro, “SUMO modification system facilitates the exchange of histone variant H2A.Z-2 at DNA damage sites”, Nucleus 9, 87-94 (2018). |
| M. Saotome, K. Saito, T. Yasuda, H. Ohtomo, S. Sugiyama, Y. Nishimura, H. Kurumizaka, and W. Kagawa, “Structural Basis of Homology-based DNA Repair Mediated by RAD52”, iScience, 3, 50-62 (2018). |
| Y. Takizawa, H. Tanaka, S. Machida, M. Koyama, K. Maehara, Y. Ohkawa, P. A. Wade, M. Wolf, and H. Kurumizaka, “Cryo-EM structure of the nucleosome containing the ALB1 enhancer DNA sequence”, Open Biology 8, 170255 (2018). |
| Y. Okamoto, M. W. Iwasaki, K. Kugou, K. K. Takahashi, A. Oda, K. Sato, W. Kobayashi, H. Kawai, R. Sakasai, A. Takaori-Kondo, T. Yamamoto, M. T. Kanemaki, M. Taoka, T. Isobe, H. Kurumizaka, H. Innan, K. Ohta, M. Ishiai, and M. Takata, “Replication stress induces accumulation of FANCD2 at central region of large fragile genes”, Nucleic Acids Res. 46, 2932-2944 (2018). |
| M. Koyama and H. Kurumizaka, “Structural diversity of the nucleosome”, J. Biochem.163, 85-95 (2018). |
| M. Ishiai, K. Sato, J. Tomida, H. Kitao, H. Kurumizaka, and M. Takata, “Activation of the FA pathway mediated by phosphorylation and ubiquitination”, Mutat Res. 803-805, 89-95 (2018). |
| A. Harada, K. Maehara, Y. Ono, H. Taguchi, K. Yoshioka, Y. Kitajima, Y. Xie, Y. Sato, T. Iwasaki, J. Nogami, S. Okada, T. Komatsu, Y. Semba, T. Takemoto, H. Kimura, H. Kurumizaka, and Y. Ohkawa, “Histone H3.3 sub-variant H3mm7 is required for normal skeletal muscle regeneration”, Nat. Commun. 9, 1400 (2018). |
| K. Saikusa, A. Osakabe, D. Kato, S. Fuchigami, A. Nagadoi, Y. Nishimura, H. Kurumizaka, and S. Akashi, “Structural Diversity of Nucleosomes Characterized by Native Mass Spectrometry”, Anal. Chem. 90, 8217-8226 (2018). |
| D. Luo, D. Kato, J. Nogami, Y. Ohkawa, H. Kurumizaka, and H. Kono, “MNase, as a probe to study the sequence-dependent site exposures in the +1 nucleosomes of yeast”, Nucleic Acids Res. 46, 7124-7137 (2018). |
| M. R. Higgs, K. Sato, J. J. Reynolds, S. Begum, R. Bayley, A. Goula, A. Vernet, K. L. Paquin, D. G. Skalnik, W. Kobayashi, M. Takata, N. G. Howlett, H. Kurumizaka, H. Kimura, and G. S. Stewart, “Histone Methylation by SETD1A Protects Nascent DNA through the Nucleosome Chaperone Activity of FANCD2”, Mol. Cell. 71, 25-41.e6 (2018). |
| A. Osakabe, Z. J. Lorkovic, W. Kobayashi, H. Tachiwana, R. Yelagandula, H. Kurumizaka, and F. Berger, “Histone H2A variants confer specific properties to nucleosomes and impact on chromatin accessibility”, Nucleic Acids Res. 46, 7675-7685 (2018). |
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