Nakayama T

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References (18)

Title : The acid-base-nucleophile catalytic triad in ABH-fold enzymes is coordinated by a set of structural elements - Denesyuk_2020_PLoS.One_15_e0229376
Author(s) : Denesyuk AI , Dimitriou PS , Johnson MS , Nakayama T , Denessiouk K
Ref : PLoS ONE , 15 :e0229376 , 2020
Abstract : Denesyuk_2020_PLoS.One_15_e0229376
ESTHER : Denesyuk_2020_PLoS.One_15_e0229376
PubMedSearch : Denesyuk_2020_PLoS.One_15_e0229376
PubMedID: 32084230

Title : Distinctive structural motifs co-ordinate the catalytic nucleophile and the residues of the oxyanion hole in the alpha\/beta-hydrolase fold enzymes - Dimitriou_2019_Protein.Sci_28_344
Author(s) : Dimitriou PS , Denesyuk AI , Nakayama T , Johnson MS , Denessiouk K
Ref : Protein Science , 28 :344 , 2019
Abstract : Dimitriou_2019_Protein.Sci_28_344
ESTHER : Dimitriou_2019_Protein.Sci_28_344
PubMedSearch : Dimitriou_2019_Protein.Sci_28_344
PubMedID: 30311984

Title : Alpha\/beta-hydrolases: A unique structural motif coordinates catalytic acid residue in 40 protein fold families - Dimitriou_2017_Proteins_85_1845
Author(s) : Dimitriou PS , Denesyuk AI , Takahashi S , Yamashita S , Johnson MS , Nakayama T , Denessiouk K
Ref : Proteins , 85 :1845 , 2017
Abstract : Dimitriou_2017_Proteins_85_1845
ESTHER : Dimitriou_2017_Proteins_85_1845
PubMedSearch : Dimitriou_2017_Proteins_85_1845
PubMedID: 28643343

Title : Genome evolution in the allotetraploid frog Xenopus laevis - Session_2016_Nature_538_336
Author(s) : 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
Ref : Nature , 538 :336 , 2016
Abstract : Session_2016_Nature_538_336
ESTHER : Session_2016_Nature_538_336
PubMedSearch : Session_2016_Nature_538_336
PubMedID: 27762356
Gene_locus related to this paper: xenla-a0a1l8f4t7 , xenla-a0a1l8fbc6 , xenla-a0a1l8fct2 , xenla-q2tap9 , xenla-q4klb6 , xenla-q5xh09 , xenla-q6ax59 , xenla-q6dcw6 , xenla-q6irp4 , xenla-q6pad5 , xenla-q7sz70 , xenla-Q7ZXQ6 , xenla-q66kx1 , xenla-q640y7 , xenla-q642r3 , xenla-Q860X9 , xenla-BCHE2 , xenla-a0a1l8g7v4 , xenla-a0a1l8g1u7 , xenla-a0a1l8fmc5 , xenla-a0a1l8g467 , xenla-a0a1l8g4e4 , xenla-a0a1l8ga66 , xenla-a0a1l8gaw4 , xenla-a0a1l8gt68 , xenla-a0a1l8h0b2 , xenla-a0a1l8fdr1 , xenla-a0a1l8fdt7 , xenla-a0a1l8fi72 , xenla-a0a1l8fi73 , xenla-a0a1l8fi77 , xenla-a0a1l8fi96 , xenla-a0a1l8hc38 , xenla-a0a1l8hn27 , xenla-a0a1l8hry6 , xenla-a0a1l8hw96 , xenla-a0a1l8i2x6 , xenla-a0a1l8hei7 , xenla-a0a1l8gnd1 , xenla-a0a1l8i2g3 , xenla-a0a1l8hdn0 , xenla-a0a1l8h622

Title : Structural Insights into the Low pH Adaptation of a Unique Carboxylesterase from Ferroplasma: Altering the pH optima of two carboxylesterases - Ohara_2014_J.Biol.Chem_289_24499
Author(s) : Ohara K , Unno H , Oshima Y , Hosoya M , Fujino N , Hirooka K , Takahashi S , Yamashita S , Kusunoki M , Nakayama T
Ref : Journal of Biological Chemistry , 289 :24499 , 2014
Abstract : Ohara_2014_J.Biol.Chem_289_24499
ESTHER : Ohara_2014_J.Biol.Chem_289_24499
PubMedSearch : Ohara_2014_J.Biol.Chem_289_24499
PubMedID: 25043762
Gene_locus related to this paper: 9eury-q2pce5 , sulsh-q5nu42

Title : Substrate specificity of fluoroacetate dehalogenase: an insight from crystallographic analysis, fluorescence spectroscopy, and theoretical computations - Nakayama_2012_Chemistry_18_8392
Author(s) : Nakayama T , Kamachi T , Jitsumori K , Omi R , Hirotsu K , Esaki N , Kurihara T , Yoshizawa K
Ref : Chemistry , 18 :8392 , 2012
Abstract : Nakayama_2012_Chemistry_18_8392
ESTHER : Nakayama_2012_Chemistry_18_8392
PubMedSearch : Nakayama_2012_Chemistry_18_8392
PubMedID: 22674735
Gene_locus related to this paper: bursp-deha

Title : Lecithin-cholesterol acyltransferase (LCAT) deficiency without mutations in the coding sequence: a case report and literature review - Shoji_2011_Clin.Nephrol_76_323
Author(s) : Shoji K , Morita H , Ishigaki Y , Rivard CJ , Takayasu M , Nakayama K , Nakayama T , Inoue Y , Ayaki M , Yoshimura A
Ref : Clin Nephrol , 76 :323 , 2011
Abstract : Shoji_2011_Clin.Nephrol_76_323
ESTHER : Shoji_2011_Clin.Nephrol_76_323
PubMedSearch : Shoji_2011_Clin.Nephrol_76_323
PubMedID: 21955868
Gene_locus related to this paper: human-LCAT

Title : The catalytic mechanism of fluoroacetate dehalogenase: a computational exploration of biological dehalogenation - Kamachi_2009_Chemistry_15_7394
Author(s) : Kamachi T , Nakayama T , Shitamichi O , Jitsumori K , Kurihara T , Esaki N , Yoshizawa K
Ref : Chemistry , 15 :7394 , 2009
Abstract : Kamachi_2009_Chemistry_15_7394
ESTHER : Kamachi_2009_Chemistry_15_7394
PubMedSearch : Kamachi_2009_Chemistry_15_7394
PubMedID: 19551770
Gene_locus related to this paper: bursp-deha

Title : Catalytic role of proton transfers in the formation of a tetrahedral adduct in a serine carboxyl peptidase - Guo_2006_Biochemistry_45_9129
Author(s) : Guo H , Wlodawer A , Nakayama T , Xu Q
Ref : Biochemistry , 45 :9129 , 2006
Abstract : Guo_2006_Biochemistry_45_9129
ESTHER : Guo_2006_Biochemistry_45_9129
PubMedSearch : Guo_2006_Biochemistry_45_9129
PubMedID: 16866358

Title : 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 - Kulakova_2004_Biochim.Biophys.Acta_1696_59
Author(s) : Kulakova L , Galkin A , Nakayama T , Nishino T , Esaki N
Ref : Biochimica & Biophysica Acta , 1696 :59 , 2004
Abstract : Kulakova_2004_Biochim.Biophys.Acta_1696_59
ESTHER : Kulakova_2004_Biochim.Biophys.Acta_1696_59
PubMedSearch : Kulakova_2004_Biochim.Biophys.Acta_1696_59
PubMedID: 14726205
Gene_locus related to this paper: psysp-lip

Title : 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 - Ejima_2004_J.Biosci.Bioeng_98_445
Author(s) : Ejima K , Liu J , Oshima Y , Hirooka K , Shimanuki S , Yokota Y , Hemmi H , Nakayama T , Nishino T
Ref : J Biosci Bioeng , 98 :445 , 2004
Abstract : Ejima_2004_J.Biosci.Bioeng_98_445
ESTHER : Ejima_2004_J.Biosci.Bioeng_98_445
PubMedSearch : Ejima_2004_J.Biosci.Bioeng_98_445
PubMedID: 16233734
Gene_locus related to this paper: sulsh-q5nu42

Title : Cloning, heterologous expression, renaturation, and characterization of a cold-adapted esterase with unique primary structure from a psychrotroph Pseudomonas sp. strain B11-1 - Suzuki_2003_Protein.Expr.Purif_30_171
Author(s) : Suzuki T , Nakayama T , Choo DW , Hirano Y , Kurihara T , Nishino T , Esaki N
Ref : Protein Expr Purif , 30 :171 , 2003
Abstract : Suzuki_2003_Protein.Expr.Purif_30_171
ESTHER : Suzuki_2003_Protein.Expr.Purif_30_171
PubMedSearch : Suzuki_2003_Protein.Expr.Purif_30_171
PubMedID: 12880765

Title : Primary structure and catalytic properties of a cold-active esterase from a psychrotroph, Acinetobacter sp. strain No. 6. isolated from Siberian soil - Suzuki_2002_Biosci.Biotechnol.Biochem_66_1682
Author(s) : Suzuki T , Nakayama T , Kurihara T , Nishino T , Esaki N
Ref : Biosci Biotechnol Biochem , 66 :1682 , 2002
Abstract : Suzuki_2002_Biosci.Biotechnol.Biochem_66_1682
ESTHER : Suzuki_2002_Biosci.Biotechnol.Biochem_66_1682
PubMedSearch : Suzuki_2002_Biosci.Biotechnol.Biochem_66_1682
PubMedID: 12353628
Gene_locus related to this paper: acisp-AEST

Title : Cold-active lipolytic activity of psychrotrophic Acinetobacter sp. strain no. 6 - Suzuki_2001_J.Biosci.Bioeng_92_144
Author(s) : Suzuki T , Nakayama T , Kurihara T , Nishino T , Esaki N
Ref : J Biosci Bioeng , 92 :144 , 2001
Abstract : Suzuki_2001_J.Biosci.Bioeng_92_144
ESTHER : Suzuki_2001_J.Biosci.Bioeng_92_144
PubMedSearch : Suzuki_2001_J.Biosci.Bioeng_92_144
PubMedID: 16233074

Title : 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 - Hirai_1997_J.Pharmacol.Exp.Ther_280_1261
Author(s) : Hirai K , Kato K , Nakayama T , Hayako H , Ishihara Y , Goto G , Miyamoto M
Ref : Journal of Pharmacology & Experimental Therapeutics , 280 :1261 , 1997
Abstract : Hirai_1997_J.Pharmacol.Exp.Ther_280_1261
ESTHER : Hirai_1997_J.Pharmacol.Exp.Ther_280_1261
PubMedSearch : Hirai_1997_J.Pharmacol.Exp.Ther_280_1261
PubMedID: 9067312

Title : Effect of TAK-147, a novel AChE inhibitor, on cerebral energy metabolism - Nakayama_1996_Neurobiol.Aging_17_849
Author(s) : Nakayama T , Takahashi H , Miyamoto M , Goto G , Nagai Y
Ref : Neurobiology of Aging , 17 :849 , 1996
Abstract : Nakayama_1996_Neurobiol.Aging_17_849
ESTHER : Nakayama_1996_Neurobiol.Aging_17_849
PubMedSearch : Nakayama_1996_Neurobiol.Aging_17_849
PubMedID: 9363795

Title : 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 - Ishihara_1993_Chem.Pharm.Bull.(Tokyo)_41_529
Author(s) : Ishihara Y , Miyamoto M , Nakayama T , Goto G
Ref : Chem Pharm Bull (Tokyo) , 41 :529 , 1993
Abstract : Ishihara_1993_Chem.Pharm.Bull.(Tokyo)_41_529
ESTHER : Ishihara_1993_Chem.Pharm.Bull.(Tokyo)_41_529
PubMedSearch : Ishihara_1993_Chem.Pharm.Bull.(Tokyo)_41_529
PubMedID: 8477504