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VALIDITY EXPIRED
personal data approved: 2019. IV. 17.
Personal data
name Mária Kazinczyné Vas
name of institution
doctoral school
ELTE György Hevesy Doctoral School of Chemistry (Academic staff member)
ELTE Doctoral School of Biology (Academic staff member)
the share of work in the different doctoral schools. ELTE György Hevesy Doctoral School of Chemistry 33%
ELTE Doctoral School of Biology 67%
Contact details
E-mail address vas.mariattk.mta.hu
phone number +36 1 382-6773
own web page
Academic title
scientific degree, title CSc
year degree was obtained 1976
discipline to which degree belongs biology
institution granting the degree HAS
scientific degree, title DSc
year degree was obtained 1996
discipline to which degree belongs biology
institution granting the degree HAS
Employment
2014 - MTA TTK Enzimológiai Intézet (research institute, not university)
other (not specified) (önkéntes tudományos tanácsadó)
Thesis topic supervisor
number of doctoral students supervised until now 4.5
number of students who fulfilled course requirements 4.5
students who obtained their degrees:
(50%) Tamás Szimler PhD 2022  DSB-ELTE
Éva Laura Gráczer PhD 2010  DSB-ELTE
Judit Perbiróné Szabó PhD 2009  DSB-ELTE
(50%) Andrea Matkovicsné Varga PhD 2007  
(50%) Beáta Flachner PhD 2004  GAODSCC
(50%) Zoltán Kovári PhD 2004  
Andrea Szilágyi PhD 1999  

  Thesis topic proposals
Research
research area The role of modular organisation of proteins in formation of the three-dimensional structure and in fullfilment of the catalytic properties are investigated.
research field in which current research is conducted biology
Publications
2019

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

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

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

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

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

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

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

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

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

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 
Scientometric data
list of publications and citations
number of scientific publications that meet accreditation criteria:
89
number of scientific publications:
96
monographs and professional books:
1
monographs/books in which chapters/sections were contributed:
2 
scientific publications published abroad that meet the accreditation criteria:
74
publications not in Hungarian, published in Hungary, meeting the accreditation criteria:
10
number of independent citations to scientific publications and creative works:
747


2024. IV. 17.
ODT ülés
Az ODT következő ülésére 2024. június 14-én, pénteken 10.00 órakor kerül sor a Semmelweis Egyetem Szenátusi termében (Bp. Üllői út 26. I. emelet).

 
All rights reserved © 2007, Hungarian Doctoral Council. Doctoral Council registration number at commissioner for data protection: 02003/0001. Program version: 2.2358 ( 2017. X. 31. )