Vas M - Search Results

1

Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus.

Merli A, Manikandan K, Gráczer E, Schuldt L, Singh RK, Závodszky P, Vas M, Weiss MS. Merli A, et al. Among authors: vas m. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jun 1;66(Pt 6):738-43. doi: 10.1107/S174430911001626X. Epub 2010 May 29. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010. PMID: 20516614 Free PMC article.

2

Atomic level description of the domain closure in a dimeric enzyme: thermus thermophilus 3-isopropylmalate dehydrogenase.

Gráczer É, Merli A, Singh RK, Karuppasamy M, Závodszky P, Weiss MS, Vas M. Gráczer É, et al. Among authors: vas m. Mol Biosyst. 2011 May;7(5):1646-59. doi: 10.1039/c0mb00346h. Epub 2011 Mar 8. Mol Biosyst. 2011. PMID: 21387033

3

Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase.

Gráczer É, Palló A, Oláh J, Szimler T, Konarev PV, Svergun DI, Merli A, Závodszky P, Weiss MS, Vas M. Gráczer É, et al. Among authors: vas m. FEBS Lett. 2015 Jan 16;589(2):240-5. doi: 10.1016/j.febslet.2014.12.005. Epub 2014 Dec 10. FEBS Lett. 2015. PMID: 25497013 Free article.

4

Dual Role of the Active Site Residues of Thermus thermophilus 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure.

Gráczer É, Szimler T, Garamszegi A, Konarev PV, Lábas A, Oláh J, Palló A, Svergun DI, Merli A, Závodszky P, Weiss MS, Vas M. Gráczer É, et al. Among authors: vas m. Biochemistry. 2016 Jan 26;55(3):560-74. doi: 10.1021/acs.biochem.5b00839. Epub 2016 Jan 14. Biochemistry. 2016. PMID: 26731489 Free article.

5

Symmetrical refolding of protein domains and subunits: example of the dimeric two-domain 3-isopropylmalate dehydrogenases.

Gráczer E, Varga A, Melnik B, Semisotnov G, Závodszky P, Vas M. Gráczer E, et al. Among authors: vas m. Biochemistry. 2009 Feb 10;48(5):1123-34. doi: 10.1021/bi801857t. Biochemistry. 2009. PMID: 19154118

6

Essential role of the metal-ion in the IPM-assisted domain closure of 3-isopropylmalate dehydrogenase.

Gráczer E, Konarev PV, Szimler T, Bacsó A, Bodonyi A, Svergun DI, Závodszky P, Vas M. Gráczer E, et al. Among authors: vas m. FEBS Lett. 2011 Oct 20;585(20):3297-302. doi: 10.1016/j.febslet.2011.09.013. Epub 2011 Sep 17. FEBS Lett. 2011. PMID: 21939659 Free article.

7

Transient kinetic studies reveal isomerization steps along the kinetic pathway of Thermus thermophilus 3-isopropylmalate dehydrogenase.

Gráczer É, Lionne C, Závodszky P, Chaloin L, Vas M. Gráczer É, et al. Among authors: vas m. FEBS J. 2013 Apr;280(8):1764-72. doi: 10.1111/febs.12191. Epub 2013 Mar 11. FEBS J. 2013. PMID: 23421786 Free article.

8

Structural and energetic basis of isopropylmalate dehydrogenase enzyme catalysis.

Palló A, Oláh J, Gráczer E, Merli A, Závodszky P, Weiss MS, Vas M. Palló A, et al. Among authors: vas m. FEBS J. 2014 Nov;281(22):5063-76. doi: 10.1111/febs.13044. Epub 2014 Oct 4. FEBS J. 2014. PMID: 25211160 Free article.

9

Nucleotide binding to pig muscle 3-phosphoglycerate kinase in the crystal and in solution: relationship between substrate antagonism and interdomain communication.

Merli A, Szilágyi AN, Flachner B, Rossi GL, Vas M. Merli A, et al. Among authors: vas m. Biochemistry. 2002 Jan 8;41(1):111-9. doi: 10.1021/bi0115380. Biochemistry. 2002. PMID: 11772008

10

Rates of unfolding, rather than refolding, determine thermal stabilities of thermophilic, mesophilic, and psychrotrophic 3-isopropylmalate dehydrogenases.

Gráczer E, Varga A, Hajdú I, Melnik B, Szilágyi A, Semisotnov G, Závodszky P, Vas M. Gráczer E, et al. Among authors: vas m. Biochemistry. 2007 Oct 16;46(41):11536-49. doi: 10.1021/bi700754q. Epub 2007 Sep 22. Biochemistry. 2007. PMID: 17887729

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