原著論文
・Fast and Easy Transient Mammalian Cell Expression and Purification of Cytoplasmic Dynein
A. Furuta, *K. Furuta, Methods Mol Biol. , 2623,157-173(2023), DOI: 10.1007/978-1-0716-2958-1_10

・Tackle “Molecular Engine” by early-career researchers
*A. Otomo, *T. Kosugi, BPPB , 19,e190039, DOI: 10.2142/biophysico.bppb-v19.0039

・Dynamic control of microbial movement by photoswitchable ATP antagonists
S. Thayyil,Y. Nishigami, M. J. Islam, P.K. Hashim, Y. Nishigami, K. Furuta, K. Oiwa, J. Yu, M. Yao, T. Nakagaki, N. Tamaoki, Chem. Eur. J. , 28,e202200807 (2022), DOI: 10.1002/chem.202200807

・Programmable molecular transport achieved by engineering protein motors to move on DNA nanotubes
R. Ibusuki, T. Morishita, A. Furuta, S. Nakayama, M. Yoshio, H. Kojima, K. Oiwa, *K Furuta, Science , 375, 1159-1164 (2022), DOI: 10.1126/science.abj5170

・State-Targeting Stabilization of Adenosine A2A Receptor by Fusing a Custom-Made De Novo Designed α-Helical Protein"
M. Mitsumoto, K. Sugaya, K. Kazama, R. Nakano, T. Kosugi, T. Murata, *N. Koga, Int. J. Mol. Sci. , 22, 12906 (2021), DOI: 10.3390/ijms222312906

・The register shift rules for βαβ-motifs for de novo protein design
H. Murata, H. Imakawa, N. Koga, *G. Chikenji, PLoS One , 16, e0256895 (2021), DOI: 10.1371/journal.pone.0256895

・Positive charge introduction on the surface of thermostabilized PET hydrolase facilitates PET binding and degradation
*A. Nakamura, N. Kobayashi, N. Koga, *R. Iino, ACS Catal. , 11, 8550–8564 (2021), DOI: 10.1021/acscatal.1c01204

・Role of backbone strain in de novo design of complex α/β protein structures
*N. Koga, R. Koga, G. Liu, J. Castellanos, G. T Montelione, *D. Baker, Nat.Commun. , 12, 3921 (2021), DOI: 10.1038/s41467-021-24050-7

・Planar cell polarity induces local microtubule bundling for coordinated ciliary beating
S. Nakayama, T. Yano , T. Namba, S. Konishi, M. Takagishi, E. Herawati, T. Nishida, Y. Imoto, S. Ishihara, M. Takahashi, K. Furuta, K. Oiwa, A. Tamura, S. Tsukita, J. Cell Biol. , 220, e202010034.(2021), DOI: 10.1083/jcb.202010034

・Robust folding of a de novo designed ideal protein even with most of the core mutated to valine
R. Koga, M. Yamamoto, T. Kosugi, N. Kobayashi, T. Sugiki, T. Fujiwara, N. Koga, PNAS , 117, 31149-31156 (2020), DOI: 10.1073/pnas.2002120117

・Collective motility of dynein linear arrays built on DNA nanotubes
R. Ibusuki, M. Shiraga, A. Furuta, M. Yoshio, H. Kojima, K. Oiwa, *K. Furuta, Biochem. Biophys. Res. Commun., 523, 1014-1019 (2020), DOI: 10.1016/j.bbrc.2019.12.125

・Gliding filament system giving both global orientational order and clusters in collective motion
S. Tanida, K. Furuta, K. Nishikawa, *T. Hiraiwa, H. Kojima, K. Oiwa, *M. Sano, Phys. Rev. E, 101, 032607 (2020), DOI: 10.1103/PhysRevE.101.032607

・Different motilities of microtubules driven by kinesin-1 and kinesin-14 motors patterned on nanopillars
T. Kaneko, K. Furuta, K. Oiwa, H. Shintaku, H. Kotera, *R. Yokokawa, Sci. Adv., 6, eaax7413 (2020), DOI: 10.1126/sciadv.aax7413

・ShadowR: a novel chromoprotein with reduced non-specific binding and improved expression in living cells
*H. Murakoshi, H. Horiuchi, T. Kosugi, M. Onda, A. Sato, N. Koga, J. Nabekura, Sci. Rep., 9, 12072 (2019), DOI: 10.1038/s41598-019-48604-4

・Kinesin-6 Klp9 plays motor-dependent and -independent roles in collaboration with Kinesin-5 Cut7 and the microtubule crosslinker Ase1 in fission yeast
*M. Yukawa, M. Okazaki, Y. Teratani, K. Furuta, *T. Toda, Sci. Rep., 9, 7336 (2019), DOI: 10.1038/s41598-019-43774-7

・Networks of electrostatic and hydrophobic interactions modulate the complex folding free energy surface of a designed β α protein
S. Basak, R. P. Nobrega, D. Tavella, L.M. Deveau, N. Koga, R. Tatsumi-Koga, D. Baker, F. Massi,*C. R. Matthews, Proc. Natl. Acad. Sci. USA, 116, 6806-6811 (2019), DOI: 10.1073/pnas.1818744116

・Transport of microtubules according to the number and spacing of kinesin motors on gold nano-pillars
T. Kaneko, S. Ando, K. Furuta, K. Oiwa, H. Shintaku, H. Kotera, Nanoscale, 11, 9879-9887 (2019), DOI: 10.1039/C9NR01324E

・Exploration of novel αβ-protein folds through de novo design
S. Minami, N. Kobayashi, T. Sugiki, T. Nagashima, T. Fujiwara, R. Koga, G. Chikenji, * N. Koga, bioRxiv (2021), , DOI:10.1101/2021.08.06.455475

・Design of complicated all-α protein structures
K. Sakuma, N. Kobayashi, T. Sugiki, T. Nagashima, T. Fujiwara, K. Suzuki, N. Kobayashi, T. Murata, T. Kosugi, R. Koga, *N. Koga, bioRxiv (2021), ,DOI: 10.1101/2021.07.14.449347

・De novo design of allosteric control into rotary motor V1-ATPase by restoring lost function
T. Kosugi, T. Iida, M. Tanabe, R. Iino, N. Koga, bioRxiv , (2020), DOI: 10.1101/2020.09.09.288571

書籍/総説・解説
・Making motors work – potential applications in biocomputing and synthetic biology
K. Furuta, J. Cell. Sci. , 136, jcs261035 (2023), DOI: 10.1242/jcs.261035

・DNAナノチューブのレール上をプログラム通りに自走するナノマシン
指宿良太、*古田健也, 生物物理, 63, 79-85 (2023), DOI：10.2142/biophys.63.79

・タンパク質の合理設計技術開発
古賀理恵, 古賀信康, 化学と工業 , 74, 576-578 (2021)

・整合性原理に基づくタンパク質デザイン
古賀理恵, 古賀信康, 生物物理 , 60, 325-330 (2020), DOI: 10.2142/biophys.60.325

・Synthetic biology approaches to dissecting linear motor protein function: towards the design and synthesis of artificial autonomous protein walkers
H. Linke, B. Höcker, K. Furuta, N. R. Forde, *P. M. G. Curmi, Biophys Rev., 12, 1041–1054 (2020), DOI: 10.1007/s12551-020-00717-1

・Consistency principle for protein design
R. Koga, *N. Koga, BPPB., 16, 304-309 (2019), DOI: 10.2142/biophysico.16.0_304

・「現代化学2023年, 1月号　特集 現代化学の最前線2023」,
“タンパク質設計技術で目指す未来”, 小杉貴洋,34-36, 東京化学同人 , (2022), ISBN: 4910034870134

・「実験医学2022年9月号」,
“カレントトピックス - DNAナノ構造体をレールとして動く新規分子モーターの設計”, 指宿良太, *古田健也, 2284-2287, 羊土社 , (2022), ISBN: 978-4-7581-2559-8

・「実験医学増刊　タンパク質の新常識」,
“de novoデザインタンパク質-生物がもたないタンパク質を設計できる時代”, 古賀理恵、小杉貴洋、古賀信康, 2046-2054, 羊土社 , (2022), ISBN: 978-4-7581-0404-3

・「実験医学 2019年11月号　再定義されるタンパク質の常識」,
“合理デザインによる新規タンパク質の創出：現状とその可能性”, 小杉貴洋・古賀理恵・古賀信康, 3089-3095, 羊土社 , (2019), ISBN: 978-4-7581-2525-3