Print preview VALIDITY EXPIRED personal data approved: 2019. IV. 17. Publications |
2019
from data base, 2019. IV. 17. |
Szimler T., Gráczer É., Györffy D., Végh B., Szilágyi A., Hajdú I, Závodszky P, Vas M: New type of interaction between the SARAH domain of the tumour suppressor RASSF1A and its mitotic kinase Aurora A, SCIENTIFIC REPORTS 9: (1) 5550 type of document: Journal paper/Article language: English URL |
2016
from data base, 2019. IV. 17. |
Graczer E, Szimler T, Garamszegi A, Konarev PV, Labas A, Olah J, Pallo A, Svergun DI, Merli A, Zavodszky P, Weiss MS, Vas M: Dual Role of the Active Site Residues of Thermus thermophilus 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure., BIOCHEMISTRY 55: (3) pp. 560-574. type of document: Journal paper/Article number of independent citations: 1 language: English URL |
2015
from data base, 2019. IV. 17. |
Gráczer Éva, Palló Anna, Oláh Julianna, Szimler Tamás, Konarev Petr V, Svergun Dmitri I, Merli Angelo, Závodszky Péter, Weiss Manfred S, Vas Mária: Glutamate 270 plays an essential role in K+-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase, FEBS LETTERS 589: (2) pp. 240-245. type of document: Journal paper/Article number of independent citations: 2 language: English URL |
2014
from data base, 2019. IV. 17. |
Graczer E, Bacso A, Konya D, Kazi A, Soos T, Molnar L, Szimler T, Beinrohr L, Szilagyi A, Zavodszky P, Vas M: Drugs Against Mycobacterium Tuberculosis 3-Isopropylmalate Dehydrogenase Can be Developed using Homologous Enzymes as Surrogate Targets., PROTEIN AND PEPTIDE LETTERS 21: (12) pp. 1295-1307. type of document: Journal paper/Article number of independent citations: 1 language: English URL |
2014
from data base, 2019. IV. 17. |
Palló A, Oláh J, Gráczer E, Merli A, Závodszky P, Weiss MS, Vas M: Structural and energetic basis of isopropylmalate dehydrogenase enzyme catalysis, FEBS JOURNAL 281: (22) pp. 5063-5076. type of document: Journal paper/Article number of independent citations: 7 language: English URL |
2011
from data base, 2019. IV. 17. |
Zerrad L, Merli A, Schroder GF, Varga A, Graczer E, Pernot P, Round A, Vas M, Bowler MW: A Spring-loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase, JOURNAL OF BIOLOGICAL CHEMISTRY 286: (16) pp. 14040-14048. type of document: Journal paper/Article number of independent citations: 23 language: English URL |
2010
from data base, 2019. IV. 17. |
Cliff MJ, Bowler MW, Varga A, Marston JP, Szabo J, Hounslow AM, Baxter NJ, Blackburn GM, Vas M, Waltho JP: Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis., JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 132: (18) pp. 6507-6516. type of document: Journal paper/Article number of independent citations: 35 language: English URL |
2005
from data base, 2019. IV. 17. |
Varga A, Flachner B, Graczer E, Osvath S, Szilagyi AN, Vas M: Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase, FEBS JOURNAL 272: (8) pp. 1867-1885. type of document: Journal paper/Article number of independent citations: 15 language: English URL |
2004
from data base, 2019. IV. 17. |
Flachner Beáta, Kovari Z, Varga Andrea, Gugolya Zoltán, Vonderviszt Ferenc, Náray-Szabó Gábor, Vas Mária: Role of Phosphate Chain Mobility of Mgatp in Completing The 3-phosphoglycerate Kinase Catalytic Site: Binding, Kinetic, And Crystallographic Studies With Atp And Mgatp, BIOCHEMISTRY 43: (12) pp. 3436-3449. type of document: Journal paper/Article number of independent citations: 29 language: English URL |
1992
from data base, 2019. IV. 17. |
HARLOS K, VAS M, BLAKE CCF: Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-Dglycerate, PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 12: (2) pp. 133-144. type of document: Journal paper/Article number of independent citations: 89 language: English URL |
| Number of independent citations to these publications: | 202 |
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