Antirepressor specificity is shaped by highly efficient dimerization of the staphylococcal pathogenicity island regulating repressors: Stl repressor dimerization perturbed by dUTPa... by Kinga Nyíri, Enikő Gál, Máté Laczkovich, Beáta G. Vértessy

Get full text

In Vitro Analysis of Predicted DNA-Binding Sites for the Stl Repressor of the Staphylococcus aureus SaPIBov1 Pathogenicity Island. by Veronika Papp-Kádár, Judit Eszter Szabó, Kinga Nyíri, Beata G Vertessy

Get full text

Evidence-Based Structural Model of the Staphylococcal Repressor Protein: Separation of Functions into Different Domains. by Kinga Nyíri, Bianka Kőhegyi, András Micsonai, József Kardos, Beata G Vertessy

Get full text

Redox status of cysteines does not alter functional properties of human dUTPase but the Y54C mutation involved in monogenic diabetes decreases protein stability by Judit Eszter Szabó, Kinga Nyíri, Dániel Andrási, Judit Matejka, Olivér Ozahonics, Beáta Vértessy

Get full text

Full-length inhibitor protein is the most effective to perturb human dUTPase activity by Bianka Kőhegyi, Zoé S. Tóth, Enikő Gál, Máté Laczkovich, András Benedek, Beáta G. Vértessy, Kinga Nyíri

Get full text

Exploiting a Phage-Bacterium Interaction System as a Molecular Switch to Decipher Macromolecular Interactions in the Living Cell by Éva Viola Surányi, Rita Hírmondó, Kinga Nyíri, Szilvia Tarjányi, Bianka Kőhegyi, Judit Tóth, Beáta G. Vértessy

Get full text

The homodimerization domain of the Stl repressor is crucial for efficient inhibition of mycobacterial dUTPase by Zoé S. Tóth, Ibolya Leveles, Kinga Nyíri, Gergely N. Nagy, Veronika Harmat, Thapakorn Jaroentomeechai, Oliver Ozohanics, Rebecca L. Miller, Marina Ballesteros Álvarez, Beáta G. Vértessy, András Benedek

Get full text