Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.

Insight into the Binding and Hydrolytic Preferences of hNudt16 Based on Nucleotide Diphosphate Substrates

Autor: Magdalena Chrabąszczewska, Maria Winiewska-Szajewska, Natalia Ostrowska, Elżbieta Bojarska, Janusz Stępiński, Łukasz Mancewicz, Maciej Łukaszewicz, Joanna Trylska, Michał Taube, Maciej Kozak, Edward Darżynkiewicz, Renata Grzela

Publikováno v: International Journal of Molecular Sciences, Vol 22, Iss 20, p 10929 (2021)

Nudt16 is a member of the NUDIX family of hydrolases that show specificity towards substrates consisting of a nucleoside diphosphate linked to another moiety X. Several substrates for hNudt16 and various possible biological functions have been report

Externí odkaz: https://doaj.org/article/9d81917284e84e71814b0beb925f2024

Insight into the Binding and Hydrolytic Preferences of hNudt16 Based on Nucleotide Diphosphate Substrates

Autor: Renata Grzela, Maria Winiewska-Szajewska, Elzbieta Bojarska, Michał Taube, Edward Darzynkiewicz, Joanna Trylska, Maciej Kozak, Janusz Stepinski, Magdalena Chrabąszczewska, Maciej Łukaszewicz, Natalia Ostrowska, Łukasz Mancewicz

Publikováno v: International Journal of Molecular Sciences
Volume 22
Issue 20
International Journal of Molecular Sciences, Vol 22, Iss 10929, p 10929 (2021)

Nudt16 is a member of the NUDIX family of hydrolases that show specificity towards substrates consisting of a nucleoside diphosphate linked to another moiety X. Several substrates for hNudt16 and various possible biological functions have been report

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5d7239c5ced82ee148108413c9524f8
https://doi.org/10.3390/ijms222010929

The crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms

Autor: Scott Bailey, Svetlana E. Sedelnikova, Alexander G. McLennan, Hend M. Abdelghany, G. Michael Blackburn, Patrick J. Baker, John B. Rafferty

Publikováno v: Structure (London, England : 1993). 10(4)

The crystal structure of C. elegans Ap 4 A hydrolase has been determined for the free enzyme and a binary complex at 2.0 A and 1.8 A, respectively. Ap 4 A hydrolase has a key role in regulating the intracellular Ap 4 A levels and hence potentially th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3085d3335610b656549eabba948f7853
https://pubmed.ncbi.nlm.nih.gov/11937063

Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.