Nakajima M - Search Results

1

Mechanistic insight into the substrate specificity of 1,2-β-oligoglucan phosphorylase from Lachnoclostridium phytofermentans.

Nakajima M, Tanaka N, Furukawa N, Nihira T, Kodutsumi Y, Takahashi Y, Sugimoto N, Miyanaga A, Fushinobu S, Taguchi H, Nakai H. Nakajima M, et al. Sci Rep. 2017 Feb 15;7:42671. doi: 10.1038/srep42671. Sci Rep. 2017. PMID: 28198470 Free PMC article.

2

Crystallization and preliminary X-ray analysis of cytosolic alpha-mannosidase from Thermotoga maritima.

Nakajima M, Fushinobu S, Imamura H, Shoun H, Wakagi T. Nakajima M, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Feb 1;62(Pt 2):104-5. doi: 10.1107/S1744309105042508. Epub 2006 Jan 27. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006. PMID: 16511275 Free PMC article.

3

Colorimetric quantification of alpha-D-galactose 1-phosphate.

Nihira T, Nakajima M, Inoue K, Nishimoto M, Kitaoka M. Nihira T, et al. Among authors: nakajima m. Anal Biochem. 2007 Dec 15;371(2):259-61. doi: 10.1016/j.ab.2007.07.012. Epub 2007 Jul 25. Anal Biochem. 2007. PMID: 17709092 No abstract available.

4

Identification of galacto-N-biose phosphorylase from Clostridium perfringens ATCC13124.

Nakajima M, Nihira T, Nishimoto M, Kitaoka M. Nakajima M, et al. Appl Microbiol Biotechnol. 2008 Mar;78(3):465-71. doi: 10.1007/s00253-007-1319-8. Epub 2008 Jan 9. Appl Microbiol Biotechnol. 2008. PMID: 18183385

5

The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase.

Miyanaga A, Fujisawa S, Furukawa N, Arai K, Nakajima M, Taguchi H. Miyanaga A, et al. Among authors: nakajima m. Biochem Biophys Res Commun. 2013 Sep 13;439(1):109-14. doi: 10.1016/j.bbrc.2013.08.019. Epub 2013 Aug 13. Biochem Biophys Res Commun. 2013. PMID: 23954635

6

1,2-β-Oligoglucan phosphorylase from Listeria innocua.

Nakajima M, Toyoizumi H, Abe K, Nakai H, Taguchi H, Kitaoka M. Nakajima M, et al. PLoS One. 2014 Mar 19;9(3):e92353. doi: 10.1371/journal.pone.0092353. eCollection 2014. PLoS One. 2014. PMID: 24647662 Free PMC article.

7

The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenase.

Ikehara Y, Arai K, Furukawa N, Ohno T, Miyake T, Fushinobu S, Nakajima M, Miyanaga A, Taguchi H. Ikehara Y, et al. Among authors: nakajima m. J Biol Chem. 2014 Nov 7;289(45):31550-64. doi: 10.1074/jbc.M114.599092. Epub 2014 Sep 25. J Biol Chem. 2014. PMID: 25258319 Free PMC article.

8

Crystallization and preliminary X-ray diffraction analysis of Lin1840, a putative β-glucosidase from Listeria innocua.

Nakajima M, Yoshida R, Miyanaga A, Taguchi H. Nakajima M, et al. Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1398-401. doi: 10.1107/S2053230X14018597. Epub 2014 Sep 25. Acta Crystallogr F Struct Biol Commun. 2014. PMID: 25286948 Free PMC article.

9

Diverse allosteric and catalytic functions of tetrameric d-lactate dehydrogenases from three Gram-negative bacteria.

Furukawa N, Miyanaga A, Togawa M, Nakajima M, Taguchi H. Furukawa N, et al. Among authors: nakajima m. AMB Express. 2014 Oct 28;4:76. doi: 10.1186/s13568-014-0076-1. eCollection 2014. AMB Express. 2014. PMID: 25401076 Free PMC article.

10

Functional and Structural Analysis of a β-Glucosidase Involved in β-1,2-Glucan Metabolism in Listeria innocua.

Nakajima M, Yoshida R, Miyanaga A, Abe K, Takahashi Y, Sugimoto N, Toyoizumi H, Nakai H, Kitaoka M, Taguchi H. Nakajima M, et al. PLoS One. 2016 Feb 17;11(2):e0148870. doi: 10.1371/journal.pone.0148870. eCollection 2016. PLoS One. 2016. PMID: 26886583 Free PMC article.

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