Associated Papers
Structural and functional insights into γ-glutamyl carboxylase-factor IX interaction: implications for vitamin K-dependent bleeding disorders.
Liu K et al.
Haematologica, 2026
40836767 (PubMed )
Supplement: 2025_287736_LIU_SUPPL.pdf
The effects of pathogenic and likely pathogenic variants for inherited hemostasis disorders in 140 214 UK Biobank participants.
Stefanucci L et al.
Blood, 2023
37647632 (PubMed )
Supplement: BLOOD_BLD-2023-020118-mmc3.xlsx › ST3.4
γ-Glutamyl carboxylase mutations differentially affect the biological function of vitamin K-dependent proteins.
Hao Z et al.
Blood, 2021
Familial Multiple Coagulation Factor Deficiencies (FMCFDs) in a Large Cohort of Patients-A Single-Center Experience in Genetic Diagnosis.
Preisler B et al.
Journal of Clinical Medicine, 2021
Transmembrane domain interactions and residue proline 378 are essential for proper structure, especially disulfide bond formation, in the human vitamin K-dependent gamma-glutamyl carboxylase.
Tie JK et al.
Biochemistry, 2008
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