Denesyuk AI, Dimitriou PS, Johnson MS, Nakayama T, Denessiouk K (2020)
The acid-base-nucleophile catalytic triad in ABH-fold enzymes is coordinated by a set of structural elements
PLoS ONE 15: e0229376

Dimitriou PS, Denesyuk AI, Nakayama T, Johnson MS, Denessiouk K (2019)
Distinctive structural motifs co-ordinate the catalytic nucleophile and the residues of the oxyanion hole in the alpha/beta-hydrolase fold enzymes
Protein Science 28: 344

Dimitriou PS, Denesyuk AI, Takahashi S, Yamashita S, Johnson MS, Nakayama T, Denessiouk K (2017)
Alpha/beta-hydrolases: A unique structural motif coordinates catalytic acid residue in 40 protein fold families
Proteins 85: 1845

Session AM, Uno Y, Kwon T, Chapman JA, Toyoda A, Takahashi S, Fukui A, Hikosaka A, Suzuki A, Kondo M, van Heeringen SJ, Quigley I, Heinz S, Ogino H, Ochi H, Hellsten U, Lyons JB, Simakov O, Putnam N, Stites J, Kuroki Y, Tanaka T, Michiue T, Watanabe M, Bogdanovic O, Lister R, Georgiou G, Paranjpe SS, van Kruijsbergen I, Shu S, Carlson J, Kinoshita T, Ohta Y, Mawaribuchi S, Jenkins J, Grimwood J, Schmutz J, Mitros T, Mozaffari SV, Suzuki Y, Haramoto Y, Yamamoto TS, Takagi C, Heald R, Miller K, Haudenschild C, Kitzman J, Nakayama T, Izutsu Y, Robert J, Fortriede J, Burns K, Lotay V, Karimi K, Yasuoka Y, Dichmann DS, Flajnik MF, Houston DW, Shendure J, DuPasquier L, Vize PD, Zorn AM, Ito M, Marcotte EM, Wallingford JB, Ito Y, Asashima M, Ueno N, Matsuda Y, Veenstra GJ, Fujiyama A, Harland RM, Taira M, Rokhsar DS (2016)
Genome evolution in the allotetraploid frog Xenopus laevis
Nature 538: 336

Ohara K, Unno H, Oshima Y, Hosoya M, Fujino N, Hirooka K, Takahashi S, Yamashita S, Kusunoki M, Nakayama T (2014)
Structural Insights into the Low pH Adaptation of a Unique Carboxylesterase from Ferroplasma: Altering the pH optima of two carboxylesterases
Journal of Biological Chemistry 289: 24499

Curtis BA, Tanifuji G, Burki F, Gruber A, Irimia M, Maruyama S, Arias MC, Ball SG, Gile GH, Hirakawa Y, Hopkins JF, Kuo A, Rensing SA, Schmutz J, Symeonidi A, Elias M, Eveleigh RJ, Herman EK, Klute MJ, Nakayama T, Obornik M, Reyes-Prieto A, Armbrust EV, Aves SJ, Beiko RG, Coutinho P, Dacks JB, Durnford DG, Fast NM, Green BR, Grisdale CJ, Hempel F, Henrissat B, Hoppner MP, Ishida K, Kim E, Koreny L, Kroth PG, Liu Y, Malik SB, Maier UG, McRose D, Mock T, Neilson JA, Onodera NT, Poole AM, Pritham EJ, Richards TA, Rocap G, Roy SW, Sarai C, Schaack S, Shirato S, Slamovits CH, Spencer DF, Suzuki S, Worden AZ, Zauner S, Barry K, Bell C, Bharti AK, Crow JA, Grimwood J, Kramer R, Lindquist E, Lucas S, Salamov A, McFadden GI, Lane CE, Keeling PJ, Gray MW, Grigoriev IV, Archibald JM (2012)
Algal genomes reveal evolutionary mosaicism and the fate of nucleomorphs
Nature 492: 59

Nakayama T, Kamachi T, Jitsumori K, Omi R, Hirotsu K, Esaki N, Kurihara T, Yoshizawa K (2012)
Substrate specificity of fluoroacetate dehalogenase: an insight from crystallographic analysis, fluorescence spectroscopy, and theoretical computations
Chemistry 18: 8392

Shoji K, Morita H, Ishigaki Y, Rivard CJ, Takayasu M, Nakayama K, Nakayama T, Inoue Y, Ayaki M, Yoshimura A (2011)
Lecithin-cholesterol acyltransferase (LCAT) deficiency without mutations in the coding sequence: a case report and literature review
Clin Nephrol 76: 323

Kamachi T, Nakayama T, Shitamichi O, Jitsumori K, Kurihara T, Esaki N, Yoshizawa K (2009)
The catalytic mechanism of fluoroacetate dehalogenase: a computational exploration of biological dehalogenation
Chemistry 15: 7394

Guo H, Wlodawer A, Nakayama T, Xu Q (2006)
Catalytic role of proton transfers in the formation of a tetrahedral adduct in a serine carboxyl peptidase
Biochemistry 45: 9129

Ejima K, Liu J, Oshima Y, Hirooka K, Shimanuki S, Yokota Y, Hemmi H, Nakayama T, Nishino T (2004)
Molecular cloning and characterization of a thermostable carboxylesterase from an archaeon, Sulfolobus shibatae DSM5389: non-linear kinetic behavior of a hormone-sensitive lipase family enzyme
J Biosci Bioeng 98: 445

Kulakova L, Galkin A, Nakayama T, Nishino T, Esaki N (2004)
Cold-active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly-->Pro substitution near the active site on its catalytic activity and stability
Biochimica & Biophysica Acta 1696: 59

Suzuki T, Nakayama T, Choo DW, Hirano Y, Kurihara T, Nishino T, Esaki N (2003)
Cloning, heterologous expression, renaturation, and characterization of a cold-adapted esterase with unique primary structure from a psychrotroph Pseudomonas sp. strain B11-1
Protein Expr Purif 30: 171

Suzuki T, Nakayama T, Kurihara T, Nishino T, Esaki N (2002)
Primary structure and catalytic properties of a cold-active esterase from a psychrotroph, Acinetobacter sp. strain No. 6. isolated from Siberian soil
Biosci Biotechnol Biochem 66: 1682

Suzuki T, Nakayama T, Kurihara T, Nishino T, Esaki N (2001)
Cold-active lipolytic activity of psychrotrophic Acinetobacter sp. strain no. 6
J Biosci Bioeng 92: 144

Hirai K, Kato K, Nakayama T, Hayako H, Ishihara Y, Goto G, Miyamoto M (1997)
Neurochemical effects of 3-[1-(phenylmethyl)-4-piperidinyl]-1-(2,3,4,5-tetrahydro-1H-1-b enzazepin-8-yl)-1-propanone fumarate (TAK-147), a novel acetylcholinesterase inhibitor, in rats
Journal of Pharmacology & Experimental Therapeutics 280: 1261

Nakayama T, Takahashi H, Miyamoto M, Goto G, Nagai Y (1996)
Effect of TAK-147, a novel AChE inhibitor, on cerebral energy metabolism
Neurobiology of Aging 17: 849

Ishihara Y, Miyamoto M, Nakayama T, Goto G (1993)
Central cholinergic agents. IV. Synthesis and acetylcholinesterase inhibitory activities of omega-[N-ethyl-N-(phenylmethyl)amino]-1-phenyl-1-alkanones and their analogues with partial conformational restriction
Chem Pharm Bull (Tokyo) 41: 529