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Items: 1 to 20 of 103

1.

The crystal structure of human transketolase and new insights into its mode of action.

Mitschke L, Parthier C, Schröder-Tittmann K, Coy J, Lüdtke S, Tittmann K.

J Biol Chem. 2010 Oct 8;285(41):31559-70. doi: 10.1074/jbc.M110.149955. Epub 2010 Jul 28.

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New function of the amino group of thiamine diphosphate in thiamine catalysis.

Meshalkina LE, Kochetov GA, Hübner G, Tittmann K, Golbik R.

Biochemistry (Mosc). 2009 Mar;74(3):293-300.

PMID:
19364324
5.

A δ38 deletion variant of human transketolase as a model of transketolase-like protein 1 exhibits no enzymatic activity.

Schneider S, Lüdtke S, Schröder-Tittmann K, Wechsler C, Meyer D, Tittmann K.

PLoS One. 2012;7(10):e48321. doi: 10.1371/journal.pone.0048321. Epub 2012 Oct 31.

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Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution.

Lindqvist Y, Schneider G, Ermler U, Sundström M.

EMBO J. 1992 Jul;11(7):2373-9.

8.

A review on research progress of transketolase.

Zhao J, Zhong CJ.

Neurosci Bull. 2009 Apr;25(2):94-9. doi: 10.1007/s12264-009-1113-y. Review.

PMID:
19290028
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Homology modeling of human transketolase: description of critical sites useful for drug design and study of the cofactor binding mode.

Obiol-Pardo C, Rubio-Martinez J.

J Mol Graph Model. 2009 Feb;27(6):723-34. doi: 10.1016/j.jmgm.2008.11.005. Epub 2008 Nov 19. Erratum in: J Mol Graph Model. 2009 Jun-Jul;27(8):983.

PMID:
19111488
12.

Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution.

Nikkola M, Lindqvist Y, Schneider G.

J Mol Biol. 1994 May 6;238(3):387-404.

PMID:
8176731
13.

Identification of catalytically important residues in yeast transketolase.

Wikner C, Nilsson U, Meshalkina L, Udekwu C, Lindqvist Y, Schneider G.

Biochemistry. 1997 Dec 16;36(50):15643-9.

PMID:
9398292
14.

Structure and functioning mechanism of transketolase.

Kochetov GA, Solovjeva ON.

Biochim Biophys Acta. 2014 Sep;1844(9):1608-18. doi: 10.1016/j.bbapap.2014.06.003. Epub 2014 Jun 11. Review.

PMID:
24929114
15.

Structure and function of the transketolase from Mycobacterium tuberculosis and comparison with the human enzyme.

Fullam E, Pojer F, Bergfors T, Jones TA, Cole ST.

Open Biol. 2012 Jan;2(1):110026. doi: 10.1098/rsob.110026.

17.

Influence of donor substrate on kinetic parameters of thiamine diphosphate binding to transketolase.

Ospanov RV, Kochetov GA, Kurganov BI.

Biochemistry (Mosc). 2007 Jan;72(1):84-92.

PMID:
17309441
18.

Effect of coenzyme modification on the structural and catalytic properties of wild-type transketolase and of the variant E418A from Saccharomyces cerevisiae.

Golbik R, Meshalkina LE, Sandalova T, Tittmann K, Fiedler E, Neef H, König S, Kluger R, Kochetov GA, Schneider G, Hübner G.

FEBS J. 2005 Mar;272(6):1326-42.

19.

New evidence for cofactor's amino group function in thiamin catalysis by transketolase.

Meshalkina LE, Kochetov GA, Brauer J, Hübner G, Tittmann K, Golbik R.

Biochem Biophys Res Commun. 2008 Feb 15;366(3):692-7. Epub 2007 Dec 10.

PMID:
18070592
20.

Kinetic study of the H103A mutant yeast transketolase.

Selivanov VA, Kovina MV, Kochevova NV, Meshalkina LE, Kochetov GA.

FEBS Lett. 2004 Jun 4;567(2-3):270-4.

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