Ken Kitano Research Works
Investigating Protein-DNA Structures
Ken Kitano, Ph.D.
Nara Inst. of Sci. & Tech. (NAIST), Japan
Researcher IDs
Research History
2011.04 -
Nara Institute of Science & Technology, Biological Science, Assistant Professor2002.05 - 2011.03
Nara Institute of Science & Technology, Information Science, Assistant Professor2001.04 - 2002.04
University of Texas Southwestern Medical Center, Postdoctoral Fellow1998.04 - 2001.03
Kyoto University, Graduate School of Science, Ph.D. student (JSPS Research Fellow)1997.07 - 1997.09
University of Toronto Ontario Cancer Institute, Researcher (IAESTE Internship Fellow)1996.04 - 1998.03
Kyoto University, Graduate School of Science, Master Student1992.04 - 1996.03
Kyoto University, Faculty of Science, Undergraduate Student
Membership / Award / License
2015.04 -
Scientific Reports, Editorial Board Member (Structural and Molecular Biology)2007.07
奈良先端科学技術大学院大学 バイオサイエンス研究科 梅園賞 (NAIST Biological Science Umesono Prize)2004.04
エックス線作業主任者 免許取得 (License for Operations Chief of Radiography with X-rays)
Publications
北野 健
タンパク質のかたちから探るウェルナー症のしくみ.
有森記念財団 研究紹介, (2021).Suzuki T., Abe A., Kawasaki S., Uchino M., Yoshimura E., Watanabe A., Kitano, K., Mochizuki D., Takeda K., Satoh J., Kimata S., Niimura Y.
Free Flavin Participates in Iron and Also Oxygen Metabolism in Bacteria.
J. Bacteriol. & Parasitol., (2020), 11(4), 377.Kimata S., Mochizuki D., Satoh J., Kitano, K., Kanesaki Y., Takeda K., Abe A., Kawasaki S., Niimura Y.
Intracellular free flavin and its associated enzymes participate in oxygen and iron metabolism in Amphibacillus xylanus lacking a respiratory chain.
FEBS Open Bio, (2018), 8(6), 947-961. (PubMed)Terawaki, S., Kitano, K., Aoyama, M., Mori, T., Hakoshima, T.
MT1-MMP recognition by ERM proteins and its implication in CD44 shedding.
Genes Cells, (2015), 20(10), 847-859. (PubMed, PDB)Kitano, K.*
Structural mechanisms of human RecQ helicases WRN and BLM.
Front. Genet., (2014), 5, 366. (PubMed)北野 健
ヒトRecQヘリカーゼWRNとBLMの結晶構造解析.
日本結晶学会誌, (2014), 56(2), 133-138.北野 健
環状ペプチドによる三量体Gタンパク質の新しい阻害機構.
生物物理, (2014), 54(5), 265-266.Kim, SY., Hakoshima, T., Kitano, K.*
Structure of the RecQ C-terminal domain of human Bloom syndrome protein.
Sci. Rep., (2013), 3, 3294. (PubMed, PDB-1, 2)Sato, A., Mishima, M., Nagai, A., Kim, SY., Ito, Y., Hakoshima, T., Jee, JG., Kitano, K.*
Solution structure of the HRDC domain of human Bloom syndrome protein BLM.
J. Biochem., (2010), 148(4), 517-525. (PubMed, PDB)Kitano, K.*, Kim, SY., Hakoshima, T.
Structural basis for DNA strand separation by the unconventional winged-helix domain of RecQ helicase WRN.
Structure, (2010), 18(2), 177-187. (Preview, PubMed, PDB)Nishimura, A.#, Kitano, K.#, Takasaki, J., Taniguchi, M., Mizuno, N., Tago, K., Hakoshima, T., Itoh, H. (#Both authors equally contributed).
Structural basis for the specific inhibition of heterotrimeric Gq protein by a small molecule.
Proc. Natl. Acad. Sci. USA., (2010), 107(31), 13666-13671. (PubMed, PDB)Terawaki, S., Kitano, K., Mori, T., Zhai, Y., Higuchi, Y., Itoh, N., Watanabe, T., Kaibuchi, K., Hakoshima, T.
The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module.
EMBO J., (2010), 29(1), 236-250. (PubMed, PDB-1, 2, 3)Kitano, K.
Mechanism of DNA unwinding by the Werner syndrome protein WRN.
J. Synchrotron Rad., (2010), 17(3), Facility inform. SPring-8.Mori, T., Kitano, K., Terawaki, S., Maesaki, R., Fukami, Y., Hakoshima, T.
Structural basis for CD44 recognition by ERM proteins.
J. Biol. Chem., (2008), 283(43), 29602-29612. (PubMed, PDB)Takai, Y., Kitano, K., Terawaki, S., Maesaki, R., Hakoshima, T.
Structural basis of the cytoplasmic tail of adhesion molecule CD43 and its binding to ERM proteins.
J. Mol. Biol., (2008), 381(3), 634-644. (PubMed, PDB)Terawaki, S., Kitano, K., Hakoshima, T.
Crystallographic characterization of the membrane-targeting domains of the Rac-specific guanine nucleotide-exchange factors Tiam1 and Tiam2.
Acta Crystallogr. F., (2008), 64(11), 1039-1042. (PubMed)Terawaki, S., Kitano, K., Aoyama, M., Hakoshima, T.
Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of membrane-type 1 matrix metalloproteinase (MT1-MMP).
Acta Crystallogr. F., (2008), 64(10), 911-913. (PubMed)Sakurai, S., Kitano, K., Morioka, H., Hakoshima, T.
Crystallization and preliminary crystallographic analysis of the catalytic domain of human flap endonuclease 1 in complex with a nicked DNA product.
Acta Crystallogr. F., (2008), 64(1), 39-43. (PubMed)Kitano, K.*, Yoshihara, N., Hakoshima, T.*
Crystal structure of the HRDC domain of human Werner syndrome protein, WRN.
J. Biol. Chem., (2007), 282(4), 2717-2728. (Cover, PubMed, PDB-1, 2)Terawaki, S., Kitano, K., Hakoshima, T.
Structural basis for type II membrane protein binding by ERM proteins revealed by the radixin-neutral endopeptidase 24.11 (NEP) complex.
J. Biol. Chem., (2007), 282(27), 19854-19862. (PubMed, PDB)Takai, Y., Kitano, K., Terawaki, S., Maesaki, R., Hakoshima, T.
Structural basis of PSGL-1 binding to ERM proteins.
Genes Cells, (2007), 12(12), 1329-1338. (PubMed, PDB)Nishino, TG., Kitano, K., Kojima, K., Ogishima, T., Ito, A., Kitada S.
Spatial orientation of mitochondrial processing peptidase and a preprotein revealed by fluorescence resonance energy transfer.
J. Biochem., (2007), 141(6), 889-895. (PubMed)Mori T., Kitano, K., Terawaki S., Maesaki R., Hakoshima T.
Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of adhesion molecule CD44.
Acta Crystallogr. F., (2007), 63(10), 844-847. (PubMed)Takai, Y., Kitano, K., Terawaki, S., Maesaki, R., Hakoshima, T.
Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1.
Acta Crystallogr. F., (2007), 63(1), 49-51. (PubMed)Kitano, K., Yusa, F., Hakoshima, T.
Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304.
Acta Crystallogr. F., (2006), 62(4), 340-345. (PubMed, PDB)Yanuar, A., Sakurai, S., Kitano, K., Hakoshima, T. (2006).
Crystal structure of human Rad GTPase of the RGK-family.
Genes Cells, (2006), 11(8), 961-968. (PubMed, PDB)Yamaguchi, H., Miwa, Y., Kasa, M., Kitano, K., Amano, M., Kaibuchi, K., Hakoshima, T.
Structural basis for induced-fit binding of Rho-kinase to the inhibitor Y27632.
J. Biochem., (2006), 140(3), 305-311. (PubMed, PDB)Kitano, K., Sakurai, S., Hakoshima, T.
Crystal structure of human flap endonuclease-1 (FEN1) complexed to PCNA.
SPring-8 Res. Front., (2006), 18-19.北野 健, 箱嶋敏雄
ヒトFEN1-PCNA複合体の結晶構造が示すスイング活性化機構.
日本結晶学会誌, (2006), 48(5), 367-372.Kitano, K., Kita, A., Hakoshima, T., Niimura, Y., Miki, K.
Crystal structure of decameric peroxiredoxin (AhpC) from Amphibacillus xylanus.
Proteins, (2005), 59(3), 644-647. (PubMed, PDB)Sakurai, S.#, Kitano, K.#, Yamaguchi, H., Hamada, K., Okada, K., Fukuda, K., Uchida, M., Ohtsuka, E., Morioka, H., Hakoshima, T. (#Both authors equally contributed).
Structural basis for recruitment of human flap endonuclease 1 to PCNA.
EMBO J., (2005), 24(4), 683-693. (PubMed, PDB)Yanuar, A., Sakurai, S., Kitano, K., Hakoshima, T.
Expression, purification, crystallization and preliminary crystallographic analysis of human Rad GTPase.
Acta Crystallogr. F., (2005), 61(11), 978-980. (PubMed)北野 健, 沼本修孝, 三木邦夫
微小重力下でのタンパク質結晶化と放射光による構造解析.
日本マイクログラビティ応用学会誌, (2005), 22(2), 78-85.Sakurai, S., Kitano, K., Okada, K., Hamada, K., Morioka H., Hakoshima, T.
Preparation and crystallization of human flap endonuclease FEN-1 in complex with proliferating-cell nuclear antigen, PCNA.
Acta Crystallogr. D., (2003), 59(5), 933-935. (PubMed)北野 健, 箱嶋敏雄
タンパク質の構造解析法.
ポストシークエンス・タンパク質実験法 (東京化学同人), (2002), 第3巻, pp.1-23.Kitano, K., Maeda, N., Fukui, T., Atomi, H., Imanaka, T., Miki, K.
Crystal structure of a novel-type archaeal Rubisco with pentagonal symmetry.
Structure, (2001), 9(6), 473-481. (PubMed, PDB)Kitano, K., Sasaki, R., Nogi, T., Fukami, T. A., Nakagawa, A., Miki, K., Tanaka, I.
Utilization of microgravity to improve the crystal quality of biologically important proteins: chaperonin-60, GrpE, B-subunit of V-type ATPase, and MIF.
J. Crystal Growth, (2000), 210(4), 819-823.北野 健, 三木邦夫
蛋白質結晶化における微小重力利用.
日本マイクログラビティ応用学会誌, (2000), 17(2), 114-120.Kitano, K., Niimura, Y., Nishiyama, Y., Miki K.
Stimulation of peroxidase activity by decamerization related to ionic strength: AhpC protein from Amphibacillus xylanus.
J. Biochem., (1999), 126(2), 313-319. (PubMed)Maeda, N., Kitano, K., Fukui, T., Ezaki, S., Atomi, H., Miki, K., Imanaka, T.
Ribulose bisphosphate carboxylase/oxygenase from hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1 is composed solely of large subunits and forms a pentagonal structure.
J. Mol. Biol., (1999), 293(1), 57-66. (PubMed)Kitano, K., Motohashi, K., Yoshida, M., Miki. K.
A novel approach to crystallizing proteins with temperature induction method: GrpE protein from Thermus thermophilus.
J. Crystal Growth, (1998), 186(3), 456-460.北野 健, 三木邦夫
タンパク質X線結晶学における微小重力利用.
材料科学, (1998), 35(2), 53-59.
(* Corresponding Author)