Sara Basse Hansen
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View article: Multi-domain O-GlcNAcase structures reveal allosteric regulatory mechanisms
Multi-domain O-GlcNAcase structures reveal allosteric regulatory mechanisms Open
Nucleocytoplasmic protein O-GlcNAcylation is a dynamic modification catalysed by O-GlcNAc transferase (OGT) and reversed by O-GlcNAc hydrolase (OGA), whose activities are regulated through largely unknown O-GlcNAc-dependent feedback mechan…
View article: An <scp><i>OGT</i></scp> Missense Variant With Impaired Enzyme Activity in a Child With Severe Developmental Delay and Hepatoblastoma
An <span><i>OGT</i></span> Missense Variant With Impaired Enzyme Activity in a Child With Severe Developmental Delay and Hepatoblastoma Open
O‐GlcNAc transferase (OGT) and its antagonist O‐GlcNAcase (OGA) regulate protein O‐GlcNAcylation, a highly conserved post‐translational modification involved in metabolic sensing. Pathogenic variants in the OGT gene cause an X‐linked conge…
View article: Multi-domain O-GlcNAcase structures reveal allosteric regulatory mechanisms
Multi-domain O-GlcNAcase structures reveal allosteric regulatory mechanisms Open
Nucleocytoplasmic protein O-GlcNAcylation is an essential modification catalysed by O -GlcNAc transferase (OGT) and reversed by O-GlcNAc hydrolase (OGA), a multi-domain enzyme that also contains a C-terminal pseudo-histone acetyltransferas…
View article: Structure of the [Ca]E2P intermediate of Ca2+-ATPase 1 from Listeria monocytogenes
Structure of the [Ca]E2P intermediate of Ca2+-ATPase 1 from Listeria monocytogenes Open
Active transport by P-type Ca 2+ -ATPases maintain internal calcium stores and a low cytosolic calcium concentration. Structural studies of mammalian sarco/endoplasmic reticulum Ca 2+ -ATPases (SERCA) have revealed several steps of the tra…
View article: Structure of a Ca<sup>2+</sup>bound phosphoenzyme intermediate in the inward-to-outward transition of Ca<sup>2+</sup>-ATPase 1 from<i>Listeria monocytogenes</i>
Structure of a Ca<sup>2+</sup>bound phosphoenzyme intermediate in the inward-to-outward transition of Ca<sup>2+</sup>-ATPase 1 from<i>Listeria monocytogenes</i> Open
Active transport by Ca 2+ -ATPases of the P-type ATPase family maintain a very low cytosolic calcium concentration and steep electrochemical gradients. Detailed mechanisms of this transport have been described from structures of mammalian …
View article: Correction: Fast-forward on P-type ATPases: recent advances on structure and function
Correction: Fast-forward on P-type ATPases: recent advances on structure and function Open
Stock, C., Heger, T., Hansen, S.B., Larsen, S.T., Habeck, M. Dieudonné, T., Driller, R. and Nissen, P. (2023) Fast-forward on P-type ATPases: recent advances on structure and function. Biochem. Soc. Trans.51; 1347–1360. doi: https://doi.or…
View article: Fast-forward on P-type ATPases: recent advances on structure and function
Fast-forward on P-type ATPases: recent advances on structure and function Open
P-type ATPase are present in nearly all organisms. They maintain electrochemical gradients for many solutes, in particular ions, they control membrane lipid asymmetry, and are crucial components of intricate signaling networks. All P-type …
View article: The crystal structure of the Ca<sup>2+</sup>-ATPase 1 from<i>Listeria monocytogenes</i>reveals a pump primed for dephosphorylation
The crystal structure of the Ca<sup>2+</sup>-ATPase 1 from<i>Listeria monocytogenes</i>reveals a pump primed for dephosphorylation Open
Many bacteria export intracellular calcium using active transporters homologous to the sarco/endoplasmic reticulum Ca 2+ -ATPase (SERCA). Here we present three crystal structures of Ca 2+ -ATPase 1 from Listeria monocytogenes (LMCA1). Stru…