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personal data approved: 2022. V. 26.
Personal data
name Andrea Bodor
name of institution
doctoral school
ELTE György Hevesy Doctoral School of Chemistry (Supervisor)
(discipline) Habilitation Comittee
SE Doctoral School of Pharmaceutical Sciences (Academic staff member)
SE Doctoral School of University Semmelweis (Announcer of research topic)
the share of work in the different doctoral schools. ELTE György Hevesy Doctoral School of Chemistry 75%
SE Doctoral School of University Semmelweis 25%
accreditation statement submitted to: Eötvös Loránd University, Budapest
Contact details
phone number +36 1 372-2500
own web page
Academic title
scientific degree, title Ph.D.
year degree was obtained 2000
discipline to which degree belongs chemistry
institution granting the degree University of Debrecen
scientific degree, title Ph.D.
year degree was obtained 2002
discipline to which degree belongs chemistry
institution granting the degree KTH, Royal Institute of Technology, Stockholm, Sweden
scientific degree, title Habilitation
year degree was obtained 2017
discipline to which degree belongs chemistry
institution granting the degree Eötvös Loránd University
Employment
2003 - Eötvös Loránd University, Budapest
university professor or researcher
Thesis topic supervisor
number of doctoral students supervised until now 4
number of students who fulfilled course requirements 2
students who obtained their degrees:
Fanni Sebák PhD 2022  DSPS1-SE
Erika Földesné Dudás PhD 2020  DSC-ELTE
Gyula Pálfy PhD 2019  DSC-ELTE

completed course requirement:
Csenge Lilla Szabó (PhD) 2022/08  DSC-ELTE
Erika Dudás (PhD) 2017/08  DSC-ELTE
present PhD students:
Nándor Papp (PhD) (2026/08)  DSC-ELTE
Dániel Kovács (PhD) (2024/08)  DSC-ELTE
  Thesis topic proposals
Research
research area NMR spectroscopy
research field in which current research is conducted chemistry
biology
Publications
2022

Sebák Fanni, Ecsédi Péter, Bermel Wolfgang, Burkhard Luy, Nyitray László, Bodor Andrea: Selective 1Hα NMR methods to reveal functionally relevant proline cis/trans isomers in IDPs, ANGEWANDTE CHEMIE-INTERNATIONAL EDITION 61: (1) e202108361
type of document: Journal paper/Article
language: English
URL 
2022

Szabó Csenge Lilla, Sebák Fanni, Bodor Andrea: Monitoring Protein Global and Local Parameters in Unfolding and Binding Studies, ANALYTICAL CHEMISTRY
type of document: Journal paper/Article
language: English
URL 
2020

Dudás Erika F, Pálfy Gyula, Menyhárd Dóra K, Sebák Fanni, Ecsédi Péter, Nyitray László, Bodor Andrea: Tumor-Suppressor p53TAD(1-60)Forms a Fuzzy Complex with Metastasis-Associated S100A4: Structural Insights and Dynamics by an NMR/MD Approach, CHEMBIOCHEM 21: (21) pp. 3087-3095.
type of document: Journal paper/Article
number of independent citations: 6
language: English
URL 
2020

Bodor Andrea, Haller Jens D, Bouguechtouli Chafiaa, Theillet Francois-Xavier, Nyitray László, Luy Burkhard: Power of Pure Shift HαCα Correlations: A Way to Characterize Biomolecules under Physiological Conditions, ANALYTICAL CHEMISTRY 92: (18) pp. 12423-12428.
type of document: Journal paper/Article
language: English
URL 
2019

Dudás Erika F., Bodor Andrea: Quantitative, Diffusion NMR Based Analytical Tool To Distinguish Folded, Disordered, and Denatured Biomolecules, ANALYTICAL CHEMISTRY 91: (8) pp. 4929-4933.
type of document: Journal paper/Article
number of independent citations: 9
language: English
URL 
2015

Alexa Anita, Gogl Gergo, Glatz Gabor, Garai Agnes, Zeke Andras, Varga Janos, Dudas Erika, Jeszenoi Norbert, Bodor Andrea, Hetenyi Csaba, Remenyi Attila: Structural assembly of the signaling competent ERK2-RSK1 heterodimeric protein kinase complex, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 112: (9) pp. 2711-2716.
type of document: Journal paper/Article
number of independent citations: 18
language: English
URL 
2009

Biverstahl H, Lind J, Bodor A, Maler L: Biophysical studies of the membrane location of the voltage-gated sensors in the HsapBK and KvAP K+ channels, BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES 1788: (9) pp. 1976-1986.
type of document: Journal paper/Article
number of independent citations: 21
language: English
URL 
2008

Mehdi H, Fabos V, Tuba R, Bodor A, Mika LT, Horvath IT: Integration of homogeneous and heterogeneous catalytic processes for a multi-step conversion of biomass: From sucrose to levulinic acid, gamma-valerolactone, 1,4-pentanediol, 2-methyl-tetrahydrofuran, and alkanes, TOPICS IN CATALYSIS 48: (1-4) pp. 49-54.
type of document: Journal paper/Article
number of independent citations: 418
language: English
URL 
2006

Pusztai Z, Vlad G, Bodor A, Horvath I T, Laas H J, Halpaap R, Richter F U: In situ NMR spectroscopic observation of a catalytic intermediate in phosphine-catalyzed cyclo-oligomerization of isocyanates, ANGEWANDTE CHEMIE-INTERNATIONAL EDITION 45: (1) pp. 107-110.
type of document: Journal paper/Article
number of independent citations: 30
language: English
URL 
2000

Bodor A, Toth I, Banyai I, Szabo Z, Hefter GT: (19)F NMR study of the equilibria and dynamics of the Al(3+)/F(-) system, INORGANIC CHEMISTRY 39: (12) pp. 2530-2537.
type of document: Journal paper/Article
number of independent citations: 45
language: English
URL 
Number of independent citations to these publications:547 
Scientometric data
list of publications and citations
number of scientific publications that meet accreditation criteria:
83
number of scientific publications:
83
monographs and professional books:
0
monographs/books in which chapters/sections were contributed:
3 
scientific publications published abroad that meet the accreditation criteria:
79
publications not in Hungarian, published in Hungary, meeting the accreditation criteria:
0
number of independent citations to scientific publications and creative works:
1526


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. )