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Beáta G. Vértessy

Researcher at Budapest University of Technology and Economics

Publications -  193
Citations -  9352

Beáta G. Vértessy is an academic researcher from Budapest University of Technology and Economics. The author has contributed to research in topics: Gene & Enzyme. The author has an hindex of 36, co-authored 183 publications receiving 8513 citations. Previous affiliations of Beáta G. Vértessy include University of Illinois at Chicago & Hungarian Academy of Sciences.

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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases.

Beáta G. Vértessy, +1 more
- 20 Jan 2009 - 
TL;DR: The dUTPase family of enzymes shows promise as novel targets for anticancer and antimicrobial therapies and could also fight infectious diseases such as malaria and tuberculosis.
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Structural Biology and Regulation of Protein Import into the Nucleus

Mary Christie, +11 more
- 22 May 2016 - 
TL;DR: The structural basis of the principal nuclear import pathways and the molecular basis of their regulation are reviewed and post-translational modifications, particularly phosphorylation, constitute key regulatory mechanisms operating in these pathways.
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Elasticity of the human red cell membrane skeleton. Effects of temperature and denaturants

Beáta G. Vértessy, +1 more
- 01 Feb 1989 - 
TL;DR: It is concluded that the elasticity of the red cell membrane skeleton may not derive from the configurational entropy of flexible coils, Rather, the elastic energy may arise from reversible dissociations of weak but specific intramolecular and/or intermolecular contacts, presumably within deformed spectrin filaments.
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Structural Insights into the Catalytic Mechanism of Phosphate Ester Hydrolysis by dUTPase

Orsolya Barabas, +5 more
- 08 Oct 2004 - 
TL;DR: Crystal structures of substrate and product complexes of wild type and mutant dUTPases were determined to reveal how an enzyme responsible for DNA integrity functions and provide an understanding for the catalytic role of conserved residues in d UTPases.