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B.G. Vertessy

Institute of Enzymology

Hungarian Academy of Science

Hungary

[email]@enzim.hu

Name/email consistency: high

 
 
 
 
 
 
 

Affiliation

  • Institute of Enzymology, Hungarian Academy of Science, Hungary. 1997 - 1999

References

  1. Pyruvate kinase as a microtubule destabilizing factor in vitro. Vértessy, B.G., Bánkfalvi, D., Kovács, J., Löw, P., Lehotzky, A., Ovádi, J. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  2. The complete triphosphate moiety of non-hydrolyzable substrate analogues is required for a conformational shift of the flexible C-terminus in E. coli dUTP pyrophosphatase. Vertessy, B.G., Larsson, G., Persson, T., Bergman, A.C., Persson, R., Nyman, P.O. FEBS Lett. (1998) [Pubmed]
  3. Crystallization and preliminary diffraction analysis of Ca(2+)-calmodulin-drug and apocalmodulin-drug complexes. Vertessy, B.G., Böcskei, Z., Harmath, V., Náray-Szabó, G., Ovádi, J. Proteins (1997) [Pubmed]
  4. Flexible glycine rich motif of Escherichia coli deoxyuridine triphosphate nucleotidohydrolase is important for functional but not for structural integrity of the enzyme. Vertessy, B.G. Proteins (1997) [Pubmed]
 
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