Cargando…
Author Correction: Redox status of cysteines does not alter functional properties of human dUTPase but the Y54C mutation involved in monogenic diabetes decreases protein stability
Autores principales: | Szabó, Judit Eszter, Nyíri, Kinga, Andrási, Dániel, Matejka, Judit, Ozohanics, Olivér, Vértessy, Beáta |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8556281/ https://www.ncbi.nlm.nih.gov/pubmed/34716399 http://dx.doi.org/10.1038/s41598-021-01241-2 |
Ejemplares similares
-
Redox status of cysteines does not alter functional properties of human dUTPase but the Y54C mutation involved in monogenic diabetes decreases protein stability
por: Szabó, Judit Eszter, et al.
Publicado: (2021) -
HDX and Native Mass Spectrometry Reveals the Different Structural Basis for Interaction of the Staphylococcal Pathogenicity Island Repressor Stl with Dimeric and Trimeric Phage dUTPases
por: Nyíri, Kinga, et al.
Publicado: (2019) -
Structural model of human dUTPase in complex with a novel proteinaceous inhibitor
por: Nyíri, Kinga, et al.
Publicado: (2018) -
Life without dUTPase
por: Kerepesi, Csaba, et al.
Publicado: (2016) -
Highly potent dUTPase inhibition by a bacterial repressor protein reveals a novel mechanism for gene expression control
por: Szabó, Judit E., et al.
Publicado: (2014)