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Author Report for: Nakayama T

No contact information in database for Nakayama T

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


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


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


    Title: Genome evolution in the allotetraploid frog Xenopus laevis
    Session AM, Uno Y, Kwon T, Chapman JA, Toyoda A, Takahashi S, Fukui A, Hikosaka A, Suzuki A and Rokhsar DS <64 more author(s)>
    Ref: Nature, 538:336, 2016 : PubMed


    Title: Structural Insights into the Low pH Adaptation of a Unique Carboxylesterase from Ferroplasma: Altering the pH optima of two carboxylesterases
    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 : PubMed


    Title: Algal genomes reveal evolutionary mosaicism and the fate of nucleomorphs
    Curtis BA, Tanifuji G, Burki F, Gruber A, Irimia M, Maruyama S, Arias MC, Ball SG, Gile GH and Archibald JM <63 more author(s)>
    Ref: Nature, 492:59, 2012 : PubMed


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


    Title: Lecithin-cholesterol acyltransferase (LCAT) deficiency without mutations in the coding sequence: a case report and literature review
    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 : PubMed


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


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


    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 K, Liu J, Oshima Y, Hirooka K, Shimanuki S, Yokota Y, Hemmi H, Nakayama T, Nishino T
    Ref: J Biosci Bioeng, 98:445, 2004 : PubMed


    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 L, Galkin A, Nakayama T, Nishino T, Esaki N
    Ref: Biochimica & Biophysica Acta, 1696:59, 2004 : PubMed


    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 T, Nakayama T, Choo DW, Hirano Y, Kurihara T, Nishino T, Esaki N
    Ref: Protein Expr Purif, 30:171, 2003 : PubMed


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


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


    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 K, Kato K, Nakayama T, Hayako H, Ishihara Y, Goto G, Miyamoto M
    Ref: Journal of Pharmacology & Experimental Therapeutics, 280:1261, 1997 : PubMed


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


    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 Y, Miyamoto M, Nakayama T, Goto G
    Ref: Chem Pharm Bull (Tokyo), 41:529, 1993 : PubMed


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Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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