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Items: 1 to 20 of 108

1.

A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinase.

Zerrad L, Merli A, Schröder GF, Varga A, Gráczer É, Pernot P, Round A, Vas M, Bowler MW.

J Biol Chem. 2011 Apr 22;286(16):14040-8. doi: 10.1074/jbc.M110.206813. Epub 2011 Feb 24.

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4.

Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability.

Auerbach G, Huber R, Grättinger M, Zaiss K, Schurig H, Jaenicke R, Jacob U.

Structure. 1997 Nov 15;5(11):1475-83.

5.

Conformational dynamics in phosphoglycerate kinase, an open and shut case?

Bowler MW.

FEBS Lett. 2013 Jun 27;587(13):1878-83. doi: 10.1016/j.febslet.2013.05.012. Epub 2013 May 15. Review.

6.

A bisubstrate analog induces unexpected conformational changes in phosphoglycerate kinase from Trypanosoma brucei.

Bernstein BE, Williams DM, Bressi JC, Kuhn P, Gelb MH, Blackburn GM, Hol WG.

J Mol Biol. 1998 Jun 26;279(5):1137-48.

PMID:
9642090
7.

Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation.

Bernstein BE, Michels PA, Hol WG.

Nature. 1997 Jan 16;385(6613):275-8.

PMID:
9000079
8.
9.

Substrate-assisted movement of the catalytic Lys 215 during domain closure: site-directed mutagenesis studies of human 3-phosphoglycerate kinase.

Flachner B, Varga A, Szabó J, Barna L, Hajdú I, Gyimesi G, Závodszky P, Vas M.

Biochemistry. 2005 Dec 27;44(51):16853-65.

PMID:
16363799
11.

Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase.

Varga A, Flachner B, Gráczer E, Osváth S, Szilágyi AN, Vas M.

FEBS J. 2005 Apr;272(8):1867-85.

13.

Communication between the nucleotide site and the main molecular hinge of 3-phosphoglycerate kinase.

Szabó J, Varga A, Flachner B, Konarev PV, Svergun DI, Závodszky P, Vas M.

Biochemistry. 2008 Jul 1;47(26):6735-44. doi: 10.1021/bi800411w. Epub 2008 Jun 10.

PMID:
18540639
14.

Two crystal structures of Escherichia coli N-acetyl-L-glutamate kinase demonstrate the cycling between open and closed conformations.

Gil-Ortiz F, Ramón-Maiques S, Fernández-Murga ML, Fita I, Rubio V.

J Mol Biol. 2010 Jun 11;399(3):476-90. doi: 10.1016/j.jmb.2010.04.025. Epub 2010 Apr 18. Erratum in: J Mol Biol. 2011 Apr 8;407(4):621.

PMID:
20403363
15.
16.

Complete catalytic cycle of cofactor-independent phosphoglycerate mutase involves a spring-loaded mechanism.

Roychowdhury A, Kundu A, Bose M, Gujar A, Mukherjee S, Das AK.

FEBS J. 2015 Mar;282(6):1097-110. doi: 10.1111/febs.13205. Epub 2015 Feb 6.

17.

Interconversion of ATP binding and conformational free energies by tryptophanyl-tRNA synthetase: structures of ATP bound to open and closed, pre-transition-state conformations.

Retailleau P, Huang X, Yin Y, Hu M, Weinreb V, Vachette P, Vonrhein C, Bricogne G, Roversi P, Ilyin V, Carter CW Jr.

J Mol Biol. 2003 Jan 3;325(1):39-63.

PMID:
12473451
18.

Crystal structure, SAXS and kinetic mechanism of hyperthermophilic ADP-dependent glucokinase from Thermococcus litoralis reveal a conserved mechanism for catalysis.

Rivas-Pardo JA, Herrera-Morande A, Castro-Fernandez V, Fernandez FJ, Vega MC, Guixé V.

PLoS One. 2013 Jun 20;8(6):e66687. doi: 10.1371/journal.pone.0066687. Print 2013.

19.

The importance of dynamic light scattering in obtaining multiple crystal forms of Trypanosoma brucei PGK.

Bernstein BE, Michels PA, Kim H, Petra PH, Hol WG.

Protein Sci. 1998 Feb;7(2):504-7.

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