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Structure and enzymatic mechanism of a moonlighting dUTPase.
Leveles I, Németh V, Szabó JE, Harmat V, Nyíri K, Bendes ÁÁ, Papp-Kádár V, Zagyva I, Róna G, Ozohanics O, Vékey K, Tóth J, Vértessy BG. Leveles I, et al. Among authors: harmat v. Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2298-308. doi: 10.1107/S0907444913021136. Epub 2013 Nov 19. Acta Crystallogr D Biol Crystallogr. 2013. PMID: 24311572
Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins.
Németh-Pongrácz V, Barabás O, Fuxreiter M, Simon I, Pichová I, Rumlová M, Zábranská H, Svergun D, Petoukhov M, Harmat V, Klement E, Hunyadi-Gulyás E, Medzihradszky KF, Kónya E, Vértessy BG. Németh-Pongrácz V, et al. Among authors: harmat v. Nucleic Acids Res. 2007;35(2):495-505. doi: 10.1093/nar/gkl1074. Epub 2006 Dec 14. Nucleic Acids Res. 2007. PMID: 17169987 Free PMC article.
Catalytically distinct states captured in a crystal lattice: the substrate-bound and scavenger states of acylaminoacyl peptidase and their implications for functionality.
Menyhárd DK, Orgován Z, Szeltner Z, Szamosi I, Harmat V. Menyhárd DK, et al. Among authors: harmat v. Acta Crystallogr D Biol Crystallogr. 2015 Mar;71(Pt 3):461-72. doi: 10.1107/S1399004714026819. Epub 2015 Feb 26. Acta Crystallogr D Biol Crystallogr. 2015. PMID: 25760596 Free article.
45 results