2023

  1. Yamada S, Ko T, Ito M, Sassa T, Nomura S, Okuma H, Sato M, Imasaki T, Kikkawa S, Zhang B, Yamada T, Seki Y, Fujita K, Katoh M, Kubota M, Hatsuse S, Katagiri M, Hayashi H, Hamano M, Takeda N, Morita H, Takada S, Toyoda M, Uchiyama M, Ikeuchi M, Toyooka K, Umezawa A, Yamanishi Y, Nitta R, Aburatani H, Komuro I. TEAD1 trapping by the Q353R-Lamin A/C causes dilated cardiomyopathy. Sci Adv. 2023 Apr 14;9(15):eade7047. doi: 10.1126/sciadv.ade7047. PMID: 37058558
  2. Komori S, Saito Y, Nishimura T, Respatika A, Endoh H, Yoshida H, Sugihara R, Iida-Norita R, Afroj T, Takai T, Oduori O, Nitta E, Kotani T, Murata Y, Kaneko Y, Nitta R, Ohnishi H, Matozaki T. CD47 promotes peripheral T cell survival by preventing dendritic cell-mediated T cell necroptosis. PNAS. 2023 August 7;120(33):e2304943120. doi: 10.1073/pnas.2304943120. PMID: 37549290
  3. 仁田 亮，丹羽 伸介，小田 賢幸．クロススケール計測の生物・医学的応用．顕微鏡（58巻2号）［特集］新時代の生命科学・医学におけるクロススケールバイオロジーと人のネットワークの必要性　doi: 10.11.410/kenbikyo.58.2_60 (2023)
  4. 今崎 剛，仁田 亮．非中心体性微小管形成の分子機構．日本生化学会誌みにれびゅう　doi:10.14952/SEIKAGAKU.2023.950541
  5. Nishikage S, Fujisawa A, Endoh H, Sakamoto H, Suzuki T, Kanzawa M, Ishii S, Okano M, Nitta E, Yakushijin K, Asakura H, Nozu K, Nitta R, Katayama Y, Sakaguchi K. Amyloid deposition through endocytosis in vascular endothelial cells. Exp. Hematol. 2023 Nov 10:S0301-472X(23)01762-9. doi: 10.1016/j.exphem.2023.11.003. PMID: 37952890
  6. Okuma H, Saijo-Hamano Y, Yamada H, Sherif AA, Hashizaki E, Sakai N, Kato T, Imasaki T, Kikkawa S, Nitta E, Sasai M, Abe T, Sugihara F, Maniwa Y, Kosako H, Takei K, Standley DM, Yamamoto M, Nitta R. Structural basis of Irgb6 inactivation by Toxoplasma gondii through the phosphorylation of switch I. Genes Cells. 2023 Nov 20. doi: 10.1111/gtc.13080.

2022

  1. Taguchi S, Nakano J, Imasaki T, Kita T, Saijo-Hamano Y, Sakai N, Shigematsu H, Okuma H, Shimizu T, Nitta E, Kikkawa S, Mizobuchi S, Niwa S, Nitta R. Structural model of microtubule dynamics inhibition by kinesin-4 from the crystal structure of KLP-12 -tubulin complex. eLife. 2022 Sep 6;11:e77877. doi: 10.7554/eLife.77877. PMID: 36065637
  2. Yamada H, Abe T, Nagaoka H, Takashima E, Nitta R, Yamamoto M, Takei K. Recruitment of Irgb6 to the membrane is a direct trigger for membrane deformation. Front. Cell. Infect. Microbiol. 2022 doi: 10.3389/fcimb.2022.992198. PMID: 36159643
  3. Imasaki T, Kikkawa S, Niwa S, Saijo-Hamano Y, Shigematsu, H  Aoyama K, Mitsuoka K, Shimizu T, Aoki M, Sakamoto A, Tomabechi Y, Sakai N, Shirouzu M, Taguchi S, Yamagishi Y,  Setsu T, Sakihama Y, Nitta E, Takeichi M, Nitta R. CAMSAP2 organizes a γ-tubulin-independent microtubule nucleation centre through phase separation. eLife. 2022 Jun 28;11:e77365. doi: 10.7554/eLife.77365. PMID: 35762204

2021

  1. Saijo-Hamano Y, Sherif AA, Pradipta A, Sasai M, Sakai N, Sakihama Y, Yamamoto M, Standley DM, Nitta R. Structural basis of membrane recognition of Toxoplasma gondii vacuole by Irgb6. Life Sci Alliance. 2021 Nov 9;5(1):e202101149. doi: 10.26508/lsa.202101149. PMID: 34753804.
  2. 宮地 洋希，仁田英里子．エピジェネティクス機構による造血幹細胞の老化制御メカニズム．MSD（2021年2月号）小川誠司 編　骨髄異形成症候群の最新の知見．ニュー・サイエンス社 Vol. 47, No.2.

 

 

 

2020

  1. 仁田 亮，今崎 剛．細胞骨格が制御する細胞内の営みをトランススケールに理解する．実験医学（2020年3月増刊号）田中啓二，若槻壮市 編　イメージング時代の構造生命科学．羊土社 Vol. 38, No.5.
  2. 吉川知志, 仁田英里子, 今崎 剛, 仁田 亮. 微小管結合タンパク質. 生体の科学（2020年8月15日発行）[特集]細胞機能の構造生物学. Vol.71 No.4 (pp. 298-303) 公益財団法人金原一郎記念医学医療振興財団/医学書院　ISSN 0370-9531

 

 

 

2019

Biomolecules, Vol. 9 (7) (July 2019)
表紙に採択されました！
  1. Nitta E, Itokawa N, Yabata S, Koide S, Hou LB, Oshima M, Aoyama K, Saraya A, Iwama A. Bmi1 counteracts hematopoietic stem cell aging by repressing target genes and enforcing the stem cell gene signature. BBRC. 2019 Oct 29; 521(3):612-619. doi: 10.1016/j.bbrc.2019.10.153.
  2. Kato Y, Hou LB, Miyagi S, Nitta E, Aoyama K, Shinoda D, Yamazaki S, Kuribayashi W, Isshiki Y, Koide S, Si S, Saraya A, Matsuzaki Y, van Lohuizen M, Iwama A. Bmi1 restricts the adipogenic differentiation of bone marrow stromal cells to maintain the integrity of the hematopoietic stem cell niche. Exp Hematol. 2019 Aug;76:24-37. doi: 10.1016/j.exphem.2019.07.006.
  3. Saijo-Hamano Y, Matsunami H, Namba K, Imada K. Architecture of the Bacterial Flagellar Distal Rod and Hook of Salmonella. Biomolecules. 2019 Jul 7;9(7). pii: E260. doi: 10.3390/biom9070260. PMID:31284631
  4. 今崎 剛，仁田英里子，仁田 亮．分子構造解析で何が見えるか．小室一成　編．新しい臨床を開拓するための分子循環器病学 1版 Cutting Edge of Molecular Cardiology. 2019．南山堂.

2018

実験医学　2018年5月号表紙　
  1. Shima T, Morikawa M, Kaneshiro J, Kambara T, Kamimura S, Yagi T, Iwamoto H, Uemura S, Shigematsu H, Shirouzu M, Ichimura T, Watanabe TM, Nitta R, Okada Y, Hirokawa N. Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport. J Cell Biol. 2018 Oct 8. pii: jcb.201711178.
  2. Shigematsu H, Imasaki T, Doki C, Sumi T, Aoki M, Kamo TU, Sakamoto A, Tokuraku K, Shirouzu M, Nitta R. Structural insight into microtubule stabilization and kinesin inhibition by Tau-family MAPs. J. Cell Biol. doi: 10.1083/ jcb. 201711182.
  3. 仁田 亮. キネシンスーパーファミリータンパク質の多様な機能を支える分子構造基盤. 顕微鏡 (解説), 53巻2号
  4. Nitta R, Imasaki T, Nitta E. Recent Progress of Structural Biology: Lessons from Our Research History. Microscopy, 2018, 1–9 doi: 10.1093/jmicro/dfy022.
  5. 仁田 亮．実験医学（2018年5月号）クライオ電子顕微鏡による構造解析が拓く次世代の生命科学・創薬．X線とクライオ電顕で微小管モーターの動きに迫る．X-ray and cryo-EM visualize the motility of microtubule-based motors. 羊土社 Vol.36 No.8，PP.1323-1327.
  6. Sumi T, Imasaki T, Aoki M, Sakai N, Nitta E, Shirouzu M, & Nitta R. Structural Insights into the Altering Function of CRMP2 by Phosphorylation. Cell Struct. Funct. 43:15-23. doi: 10.1247/csf.17025, 2018.
  7. Imasaki T, Wenzel S, Yamada K, Bryant ML, Takagi Y. Titer estimation for quality control (TEQC) method: A practical approach for optimal production of protein complexes using the baculovirus expression vector system. PLOS ONE 13: e0195356. doi: 10.1371/journal.pone.0195356. eCollection 2018.

2017

  1. Niwa S, Nakamura F, Tomabechi Y, Aoki M, Shigematsu H, Matsumoto T, Yamagata A, Fukai S, Hirokawa N, Goshima Y, Shirouzu M, Nitta R. Structural basis for CRMP2-induced axonal microtubule formation. Sci. Rep. 7: 10681. doi:10.1038/s41598-017-11031-4, 2017.
  2. Rogers CM, Wang JC, Noguchi H, Imasaki T, Takagi Y, Bochman ML. Yeast Hrq1 shares structural and functional homology with the disease-linked human RecQ4 helicase. Nucleic Acids Research 45, 5217–5230. doi: 10.1093/nar/gkx151. 2017.

  3. Mito K, Sato Y, Kobayashi T, Miyamoto K, Nitta E, Iwama A, Matsumoto M, Nakamura M, Sato K, Miyamoto T. The nicotinic acetylcholine receptor α7 subunit is an essential negative regulator of bone mass. Sci Rep. 2017 Mar 28;7:45597. doi: 10.1038/srep45597.

2016

  1. Wang D, Nitta R, Morikawa M, Yajima H, Inoue S, Shigematsu H, Kikkawa M, Hirokawa N. Motility and Microtubule Depolymerization Mechanisms of the Kinesin-8 motor, KIF19A. ELife 2016 pii: e18101. doi: 10.7554/eLife.18101.
  2. Yamagishi M, Shigematsu H, Yokoyama T, Kikkawa M, Sugawa M, Aoki M, Shirouzu M, Yajima J, Nitta R. Structural basis of backwards motion in kinesin-1–kinesin-14 chimera: implication for kinesin-14 motility. Structure 2016 24;1322-34.
  3. Koide S, Oshima M, Takubo K, Yamazaki S, Nitta E, Saraya A, Aoyama K, Kato Y, Miyagi S, Nakajima-Takagi Y, Chiba T, Matsui H, Arai F, Suzuki Y, Kimura H, Nakauchi H, Suda T, Shinkai Y, Iwama A. Setdb1 maintains hematopoietic stem and progenitor cells by restricting the ectopic activation of non-hematopoietic genes. Blood. 128(5), pp 638-49. 2016.
  4. Yamashita M, Nitta E, Suda T. Regulation of hematopoietic stem cell integrity through p53 and its related factors. Ann N Y Acad Sci. 1370(1), pp 45-54. 2016.
  5. 仁田英里子，岩間厚志　造血幹細胞を制御する遺伝子 1. ポリコーム遺伝子ほか エピジェネティクス制御遺伝子 造血器腫瘍アトラス第5版. p 37-44. 2016 日本医事新報社.

2015

  1. Morikawa M, Yajima H, Nitta R, Inoue S, Ogura T, Sato C, Hirokawa N. X-ray and Cryo-EM Structures Reveal Mutual Conformational Changes of Kinesin and GTP-Microtubule upon binding. EMBO J. 2015 34: 1270-86.
  2. Yamashita M, Nitta E, Suda T. Maintenance of hematopoietic stem cell integrity and regulation of leukemogenesis by p53 and its coactivator Aspp1. Rinsho Ketsueki. 56(12), pp 2426-33. 2015.
  3. Yamashita M, Nitta E* and Suda T.* Aspp1 preserves hematopoietic stem cell pool integrity and prevents malignant transformation. Cell Stem Cell. 17(1), pp23-34. 2015 (*corresponding authors) .
  4. 仁田英里子，岩間厚志 The cancer stem cell model in hematological malignancies. 日本臨床 73(5), pp 733-8. 2015.
  5. 仁田英里子，岩間厚志　骨髄の構造.　Principles and practice 血液・造血器・リンパ系. p 38-43. 2015. 文光堂.
  6. Hirade Y, Kotoku N, Terasaka K, Saijo-Hamano Y, Fukumoto A, Mizukami H. Identification and functional analysis of 2-hydroxyflavanone C-glucosyltransferase in soybean (Glycine max) FEBS Lett. 2015, 589: 1778-1786.

2014

  1. 仁田 亮 キネシン型分子モーターの構造変化と動作機構. 生物物理 (解説), 2014 54:133-9.
  2. Inoue S, Nitta R, Hirokawa N. Crystal Structure of the KIF5C Motor Domain Without Any Nucleotide. Photon Factory Activity Report 2014 PART B #32.
  3. Ogura T, Yajima H, Nitta R, Hirokawa N, Sato C. New Simulated Annealing Approach Considering Helix Bending Applied to Determine the 8.8 Å Structure of 15-Protofilament Microtubules. J. Struct. Biol. 2014 165-76. # Selected as a cover article.
  4. Yunus J, Setsu T, Kikkawa S, Sakisaka T, Terashima T (2014) Cytoarchitecture of Olfactory Bulb in laggard Mutant Mouse. Neuroscience 275:259–271.
  5. Nitta E and Iwama A. Diploid, not polyploid: new platelet producers. Blood. 124(17), pp 2620-2. 2014.
  6. Cheong J-W, Nakamura-Ishizu A, Nitta E, Suda T Hematopoietic Stem Cell Aging and Oxidative Stress. Stem Cells: From Basic Research to Therapy: Basic Stem Cell Biology, Tissue Formation during Development, and Model Organisms. Vol.1, p88-107. 2014 CRC Press.
  7. Fukumura T, Furukawa Y, Kawaguchi T, Saijo-Hamano Y, Namba K, Imada K, Minamino T. Crystallization and preliminary X-ray analysis of the periplasmic domain of FliP, an integral membrane component of the bacterial flagellar type III protein-export apparatus Acta Crystallogr F Struct Biol Commun. 2014, F70: 1215-1218.

2013

  1. Chang Q, Nitta R, Inoue S, Hirokawa N. Structural Basis for the ATP-induced Isomerization of Kinesin. J. Mol. Biol. 2013 425:1869-80.
  2. Yamashita M, Nitta E*, Nagamatsu G, Ikushima YM, Hosokawa K, Arai F and Suda T.* Nucleostemin is indispensable for the maintenance of hematopoietic stem cells and genetic stability. Biochem Biophys Res Commun. 441(1), pp 196-201. 2013 　 (*corresponding authors).
  3. Woon AP, Tohidpour A, Alonso H, Saijo-Hamano Y, Kwok T, Roujeinikova A. Conformational analysis of isolated domains of Helicobacter pylori CagA PLoS One. 2013, 8: e79367.
  4. *Saijo-Hamano Y, Matsunami H, Namba K and Imada K. (*corresponding author) Expression, purification, crystallization and preliminary X-ray diffraction analysis of a core fragment of FlgG, a bacterial flagellar rod protein Acta Crystallogr F Struct Biol Commun. 2013, F69: 547-550. (本稿のFlgG 結晶の写真が世界結晶年である2014年初号表紙に採用されました）



  5. Martinez-Argudo I, Veenendaal AK, Liu X, Roehrich AD, Ronessen MC, Franzoni G, van Rietschoten KN, Morimoto YV, Saijo-Hamano Y, Avison MB, Studholme DJ, Namba K, Minamino T, Blocker AJ. Isolation of Salmonella mutants resistant to the inhibitory effect of Salicylidene acylhydrazides on flagella-mediated motility. PLoS One. 2013, 8: e52179.

2012

  1. Nitta R, Hirokawa N. Fundamental Properties and Structure of Kinesin. Encyclopedia of Biophysics. Roberts, Gordon C.K. ed., Springer-Verlag Berlin Heidelberg. 2012.　DOI:10.1007/978-3-642-16712-6.
  2. Yajima H., #Ogura T, #Nitta R, Okada Y, Sato C, *Hirokawa N. Conformational Changes in Tubulin in GMPCPP and GDP-taxol Microtubules Observed by Cryo Electron Microscopy. J. Cell Biol. 2012 198:315-22. # Equal contribution. Faculty of 1000 Recommended Reading.
  3. Imai H, Oomiya Y, Kikkawa S, Shoji W, Hibi M, Terashima T, Katsuyama Y (2012) Dynamic Changes in Gene Expression of Zebrafish Reelin Receptors during Embryogenesis and Hatching Period. Dev. Growth Diff. 54:253–263.
  4. Bieniossek C, Imasaki T, Takagi Y & Berger I. MultiBac: Expanding the research toolbox for multiprotein complexes. Trends Biochem. Sci. 37, 49–57. doi: 10.1016/j.tibs.2011.10.005. 2012.
  5. Shimada M, Saijo-Hamano Y, Furukawa Y, Minamino T, Imada K, Namba K. Functional defect and restoration of temperature-sensitive mutants of FlhA, a subunit of the flagellar protein export apparatus. J Mol Biol. 2012, 415: 855-865.

2011

  1. Nitta E, Yamashita M, Hosokawa K, Xian M, Takubo K, Arai F, Nakada S, Suda T. Telomerase reverse transcriptase protects ATM-deficient hematopoietic stem cells from ROS- induced apoptosis through a telomere independent mechanism. Blood. 117(16), pp 4169-80. 2011　(*Plenary paper).
  2. Yoshimi A, Goyama S, Watanabe-Okochi N, Yoshiki Y, Nannya Y, Nitta E, Arai S, Sato T, Shimabe M, Nakagawa M, Imai Y, Kitamura T, Kurokawa M. Evi1 represses PTEN expression and activates PI3K/AKT/mTOR via interactions with polycomb proteins. Blood. 117(13), pp 3617-28. 2011.
  3. Imasaki T, Calero G, Cai G, Tsai KL, Yamada K, Cardelli F, Erdjument-Bromage H, Tempst P, Berger I, Kornberg GL, Asturias FJ, Kornberg RD, Takagi Y. Architecture of the Mediator head module. Nature 475, 240–243. doi: 10.1038/nature10162. 2011.
  4. Aydin I, Saijo-Hamano Y, Namba K, Thomas C, Roujeinikova A. Structural analysis of the essential resuscitation promoting factor YeaZ suggests a mechanism of nucleotide regulation through dimer reorganization. PLoS One. 2011, 6: e23245.

2010

  1. 廣川信隆, 仁田 亮. 生体分子モーター. 入門 構造生物学, 加藤龍一 編 (分担執筆), 共立出版, 146-55, 2010. ISBN 978-4-320-05704-3.
  2. Kawaguchi K, Habara T, Terashima T, Kikkawa S (2010) GABA Modulates Development of Cerebellar Purkinje Cell Dendrites under Control of Endocannabinoid Signaling. J. Neurochem. 114:627–638.
  3. Kawaguchi K, Katsuyama Y, Kikkawa S, Setsu T, Terashima T (2010) PKH26 Is an Excellent Retrograde and Anterograde Fluorescent Tracer Characterized by a Small Injection Site and Strong Fluorescence Emission. Arch. Histol. Cytol. 73:65–72.
  4. Goyama S, Nitta E, Yoshino T, Kako S, Watanabe-Okochi N, Shimabe M, Imai Y, Takahashi K, Kurokawa M. EVI-1 interacts with histonemethyltransferases SUV39H1 and G9a for transcriptional repression and bone marrow immortalization. Leukemia. 24(1), pp 81-8. 2010.
  5. Saijo-Hamano Y, Imada K, Minamino T, Kihara M, Shimada M, Kitao A, Namba K. Structure of the cytoplasmic domain of FlhA and implication for flagellar type III protein export. Mol Microbiol. 2010, 76: 260-268.
  6. Minamino T, Shimada M, Okabe M, Saijo-Hamano Y, Imada K, Kihara M, Namba K. Role of the C-terminal cytoplasmic domain of FlhA in bacterial flagellar type III protein export. J Bacteriol. 2010, 192: 1929-1936.

2009

  1. Hirokawa N, Nitta R, Okada Y. The mechanisms of kinesin motor motility: lessons from the monomeric motor KIF1A. Nat. Rev. Mol. Cell Biol. 2009 10:877-84.
  2. 仁田英里子，須田年生. 白血病幹細胞の潮流 Cancer stem cell concepts—lesson from leukemia. 日本臨床 67(10),pp 1863-7.2009.
  3. 仁田英里子，須田年生. 幹細胞における老化とがんの制御機構—Aging and cancer in hematopoietic stem cells—. 日本老年医科学雑誌 46(3), pp 195-9. 2009.

2008

  1. Nitta R, Hirokawa N. Structural Mechanism of the Microtubule-Activated Nucleotide Exchange of Molecular Motor Kinesin. Photon Factory Activity Report 2008 PART A: Highlights; 56-57.
  2. Nitta R, Okada Y, Hirokawa N. Crystallization of the Mg-releasing intermediates of kinesin ATPase. Nat. protoc. 2008; DOI: 10.1038/ nprot.2008. 239.
  3. Nitta R, Okada Y, Hirokawa N. Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin. Nat. Struct. Mol. Biol. 2008 15:1067-75.
  4. Sato T, Goyama S, Nitta E, Takeshita M, Yoshimi M, Nakagawa M, Kawazu M, Ichikawa M, Kurokawa M. Evi-1 promotes para-aortic splanchnopleural hematopoiesis through up-regulation of GATA-2 and repression of TGF-β signaling. Cancer Science. 99(7), pp 1407-13. 2008.
  5. Matsuoka S, Oike Y, Onoyama I, Iwama A, Arai F, Takubo K, Mashimo Y, Oguro H, Nitta E, Ito K, Miyamoto K, Yoshihara H, Hosokawa K, Nakamura Y, Gomei Y, Iwasaki H, Hayashi Y, Matsuzaki Y, Nakayama K, Ikeda Y, Hata A, Chiba S, Nakayama KI, Suda T. Fbxw7 acts as a critical fail-safe against premature loss of hematopoietic stem cells and development of T-ALL. Genes Dev. 22(8), pp 986-991. 2008.
  6. Takeshita M, Ichikawa M, Nitta E, Goyama S, Asai T, Ogawa S, Chiba S, Kurokawa M. AML1-Evi-1 specifically transforms hematopoietic stem cells through fusion of the entire Evi-1 sequence to AML1. Leukemia. 22(6): 1241-9. 2008.

2007

  1. Shibata-Iwasaki R, Dekimoto H, Katsuyama Y, Kikkawa S, Terashima T (2007) Anterograde Labeling of Corticospinal Tract in jimpy Mutant Mice by DiI Injection into Motor Cortex. Arch. Histol. Cytol.70:297–301.
  2. Muraoka D, Katsuyama Y, Kikkawa S, Terashima T (2007) Postnatal Development of Entorhinodentate Projection of Reeler Mutant Mouse. Dev. Neurosci. 29:59–72.
  3. Katsuyama Y, Oomiya Y, Dekimoto H, Motooka E, Takano A, Kikkawa S, Hibi M, Terashima T (2007) Expression of Zebrafish ROR alpha Gene in Cerebellar-like Structures. Dev. Dyn. 236:2694–2701.
  4. Nitta E, Izutsu K, Sato T, Ota Y, Takeuchi K, Kamijo A, Takahashi K, Oshima K, Kanda Y, Chiba S, Motokura T, Kurokawa M. A high incidence of late-onset neutropenia following rituximab-containing chemotherapy as a primary treatment of CD20-positive B-cell lymphoma: a single-institution study. Ann Oncol. 18(2): 364-9. 2007.

2005

  1. Taylor MR, Kikkawa S, Diez-Juan A, Ramamurthy V, Kawakami K, Carmeliet P, Brockerhoff SE (2005) The Zebrafish pob Gene Entodes a Novel Protein Required for Survival of Red Cone Photoreceptor Cells. Genetics 170:263–273.
  2. Nitta E, Izutsu K, Yamaguchi Y, Imai Y, Ogawa S, Chiba S, Kurokawa M, Hirai H. Oligomerization of Evi-1 regulated by the PR domain contributes to recruitment of corepressor CtBP. Oncogene. 24(40), pp 6165-73. 2005 .
  3. Ogawa T, Nitta R, Okada Y, Hirokawa N. A Common Mechanism for Microtubule Destabilizers- M Type Kinesins Stabilize Curling of the Protofilament Using the Class-Specific Neck and Loops. Cell 2004 116: 591-602. #Faculty of 1000 Recommended Reading.
  4. Saijo-Hamano Y, Imada K, Minamino T, Kihara M, Macnab RM, Namba K. Crystallization and preliminary X-ray analysis of the C-terminal cytoplasmic domain of FlhA, a membrane-protein subunit of the bacterial flagellar type III protein-export apparatus. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005, 61: 599-602.

2004

  1. Nitta R, Kikkawa M, Okada Y, Hirokawa N. KIF1A alternately uses two loops to bind microtubules. Science 2004 305: 678-83.
  2. Misaki K, Kikkawa S, Terashima T (2004) Reelin-expressing Neurons in the Anterior Commissure and Corpus Callosum of the Rat. Dev. Brain Res. 148:89–96.
  3. Yamaguchi Y, Kurokawa M, Imai Y, Izutsu K, Asai T, Ichikawa M, Yamamoto G, Nitta E, Yamagata T, Sasaki K, Mitani K, Ogawa S, Chiba S, Hirai H. AML1 is functionally regulated through p300-mediated acetylation on specific lysine residues. J Biol Chem. 279(15): 15630-8. 2004.
  4. Imai Y, Kurokawa M, Yamaguchi Y, Izutsu K, Nitta E, Mitani K, Satake M, Noda T, Ito Y, Hirai H. The corepressor mSin3A regulates phosphorylation-induced activation, intranuclear location, and stability of AML1. Mol Cell Biol. 24(3): 1033-43. 2004.
  5. Saijo-Hamano Y, Minamino T, Macnab RM, Namba K. Structural and functional analysis of the C-terminal cytoplasmic domain of FlhA, an integral membrane component of the type III flagellar protein export apparatus in Salmonella. J Mol Biol. 2004, 343: 457-66.
  6. Saijo-Hamano Y, Minamino T, Macnab RM, Namba K. Structural and functional analysis of the C-terminal cytoplasmic domain of FlhA, an integral membrane component of the type III flagellar protein export apparatus in Salmonella. J Mol Biol. 2004, 343: 457-66.
  7. Minamino T, Saijo-Hamano Y, Furukawa Y, González-Pedrajo B, Macnab RM, Namba K. Domain organization and function of Salmonella FliK, a flagellar hook-length control protein. J Mol Biol. 2004, 341: 491-502.
  8. Saijo-Hamano Y, Uchida N, Namba K, Oosawa K. In vitro characterization of FlgB, FlgC, FlgF, FlgG, and FliE, flagellar basal body proteins of Salmonella. J Mol Biol. 2004, 339: 423-435.

2003

  1. Nitta R, Ogawa T, Kikkawa M, Okada Y, Hirokawa N. X-ray crystallography of kinesin motors. Photon Factory Activity Report 2003 PART A: Highlights; 29-31.
  2. Kikkawa S, Yamamoto T, Misaki K, Ikeda Y, Okado H, Ogawa M, Woodhams PL, Terashima T (2003) Missplicing Resulting from a Short Deletion in the Reelin Gene Causes Reeler-like Neuronal Disorders in the Mutant Shaking Rat Kawasaki. J. Comp. Neurol. 463: 303–315.

– 2002

  1. Ohkubo N, Lee YD, Morishima A, Terashima T, Kikkawa S, Tohyama M, Sakanaka M, Tanaka J, Maeda N, Vitek MP, Mitsuda N (2002) Apolipoprotein E and Reelin Ligands Modulate Tau Phosphorylation through an Apolipoprotein E Receptor/Disabled-1/Glycogen Synthase Kinase-3 Cascade. FASEB J. 17: 295–297.
  2. Rina-Susilowati, Jusuf AA, Sakagami H, Kikkawa S, Kondo H, Minami Y, Terashima T (2001) Distribution of Ca2+/Calmodulin-Dependent Protein Kinase I Beta 2 in the Central Nervous System of the Rat. Brain Res. 911: 1–11.
  3. 若海美智, 志賀 剛, 鈴木 豪, 保坂文駿, 仁田 亮, 佐藤太彦, 今村仁治, 松田直樹, 笠 貫宏, 土谷隆紀, 西方かおり, 長沼美代子 アミオダロン経口投与導入時の初期投与量の検討(第2報). 臨床薬理 2000; 31: 407-8.
  4. Iwasa T, Yanai T, Nakagawa M, Kikkawa S, Obata S, Usukura J, Tsuda M (2000) G Protein α Subunit Genes in Octopus Photoreceptor Cells. Zool. Sci. 17:711–716.
  5. Saijo-Hamano Y, Namba K, Oosawa K. A new purification method for overproduced proteins sensitive to endogenous proteases. J Struct Biol. 2000, 132: 142-146.
  6. 寺島俊雄，薛 富義，吉川知志，池田やよい (1999) リーラーマウス顔面神経核の細胞構築，解剖学雑誌 74: 411–20.
  7. 寺島俊雄，吉川知志 (1999) マウス大脳皮質の形成異常 —リーラーマウスを中心に —，脳の科学 21: 1319–1324.
  8. Nakagawa M, Iwasa T, Kikkawa S, Tsuda M, Ebrey TG (1999) How Vertebrate and Invertebrate Visual Pigments Differ in their Mechanism of Photoactivation. Proc. Natl. Acad. Sci. USA 96: 6189–6192.
  9. Nitta R, Sakomura Y, Tanimoto K, Hidai T, Kasanuki H, Aomi S, Nishikawa T. Primary cardiac angiosarcoma of the right atrium undiagnosed by transvenous endocardial tumor biopsy. Intern. Med. 1998. 37: 1023-6. 
  10. Kikkawa S, Yoshida N, Nakagawa M, Iwasa T, Tsuda M (1998) A Novel Rhodopsin Kinase in Octopus Photoreceptor Possesses a Pleckstrin Homology Domain and Is Activated by G Protein βγ-Subunits. J. Biol. Chem. 273: 7441–7447.
  11. Nakagawa M, Kikkawa S, Tominaga K, Tsugi N, Tsuda M (1998) A Novel Photointermediate of Octopus Rhodopsin Activates Its G-protein FEBS Lett. 436: 259–262.
  12. Iwasa T, Colmenares LU, Hirata K, Arime Y, Nakagawa M, Kikkawa S, Takashima H, Nosaka A, Naito A, Saito H, Liu RSH, Tsuda M (1998) 19F NMR and UV-Vis Absorption Spectroscopic Studies of Fluorinated Octopus Rhodopsin and Its Photoproducts. J. Phys. Chem. A 102: 5602–5610.
  13. 吉川知志，中川将司 (1997) トランスデューサー；情報変換分子Ｇタンパク質，「知覚のセンサー；生物の巧みなシグナルの獲得」，津田基之 編，吉岡書店 pp. 15–23.
  14. Nakagawa M, Kikkawa S, Iwasa T, Tsuda M (1997) Light-induced Protein Conformational Changes in the Photolysis of Octopus Rhodopsin. Biophys. J. 72: 2320–2328.
  15. Nakagawa M, Iwasa T, Kikkawa S, Takao T, Shimonishi Y, Tsuda M (1997) Identification of Two Palmitoyl Groups in Octopus Rhodopsin. Photochem. Photobiol. 65:185–189.
  16. Saijo Y, Takeda S, Scherer A, Kobayashi T, Maéda Y, Taniguchi H, Yao M, Wakatsuki S. Production, crystallization, and preliminary X-ray analysis of rabbit skeletal muscle troponin complex consisting of troponin C and fragment (1-47) of troponin I. Protein Sci. 1997, 6: 916-918.
  17. 津田基之，岩佐達郎，中川将司，吉川知志 (1996) タンパク質超分子システムの構造と機能，「新タンパク質応用工学」，籏野昌弘 編，フィジテクノシステム pp. 290–295.
  18. Kikkawa S, Tominaga K, Nakagawa M, Iwasa T, Tsuda M (1996) Simple Purification and Functional Reconstitution of Octopus Photoreceptor Gq Which Couples Rhodopsin To Phospholipase C. Biochemistry 35: 15857–15864.
  19. Kikkawa S, Nakagawa M, Iwasa T, Kaneko A, Tsuda M (1993) GTP-binding Protein Couples with Metabotropic Glutamate Receptor in Bovine Retinal On-bipolar Cell. Biochem. Biophys. Res. Commun. 195:374–379.
  20. Tsuda M, Iwasa T, Nakagawa M, Kikkawa S, Tsuda T (1993) Regulaion of signal coupling proteins in octopus photoreceptors. in “Frontiers of Photobiology” Eds. Shima A et al., Elsevier Science Publishers pp. 189–194.
  21. Tsuda M, Nakagawa M, Iwasa T, Kikkawa S (1992) Light induced conformational changes of octopus rhodopsin. in “Structures and Functions of Retinal Proteins” Ed. Rigaud JL, John Libbey Eurotext Ltd. pp. 287–290.
  22. 津田基之，岩佐達郎，中川将司，吉川知志 (1992) 光センサーロドプシンの機能，電子写真 31:572–577.
  23. Kikkawa S, Takahashi K, Takahashi K, Shimada N, Ui M, Kimura N, Katada T (1992) Activation of Nucleoside Diphosphate Kinase by Mastoparan a Peptide Isolated from Wasp Venom FEBS Lett. 305: 237–240.
  24. Kikkawa S, Takahashi K, Takahashi K, Shimada N, Ui M, Kimura N, Katada T (1990) Conversion of GDP into GTP by Nucleoside Diphosphate Kinase on GTP-binding Proteins. J. Biol. Chem. 265: 21536–21540.
  25. Hoshino S, Kikkawa S, Takahashi K, Itoh H, Kaziro Y, Kawasaki H, Suzuki K, Katada T, Ui M (1990) Identification of Sites for Alkylation by N-Ethylmaleimide and Pertussis Toxin-catalyzed ADP-ribosylation on GTP-binding Proteins. FEBS Lett. 276: 227–231.
  26. Kikkawa S, Takahashi K, Katada T, Inada Y (1989) Esterification of Chiral Secondary Alcohols with Fatty-acid in Organic Solvents by Polyethylene Glycol-modified Lipase. Biochem. Int. 19: 1125–1131.
  27. Kobayashi I, Shibasaki H, Takahashi K, Kikkawa S, Ui M, Katada T (1989) Purification of GTP-binding Proteins from Bovine Brain Membranes – Identification of Heterogeneity of α-Subunit of Go Proteins. FEBS Lett. 257: 177–180.
  28. 大和田きみ子，吉川知志，高橋勝宣 (1988) 酵素蛋白質の有機溶媒可溶化と磁性化, 化学と生物 26: 454–455.