| Cold-active alkaline phosphatase is irreversibly transformed into an inactive dimer by low urea concentrations JG Hjörleifsson, B Ásgeirsson Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1864 (7), 755-765, 2016 | 20 | 2016 |
| pH-dependent binding of chloride to a marine alkaline phosphatase affects the catalysis, active site stability, and dimer equilibrium JG Hjörleifsson, B Ásgeirsson Biochemistry 56 (38), 5075-5089, 2017 | 17 | 2017 |
| X-ray crystal structure of Vibrio alkaline phosphatase with the non-competitive inhibitor cyclohexylamine B Ásgeirsson, S Markússon, SS Hlynsdóttir, R Helland, JG Hjörleifsson Biochemistry and Biophysics Reports 24, 100830, 2020 | 7 | 2020 |
| Chloride promotes refolding of active Vibrio alkaline phosphatase through an inactive dimeric intermediate with an altered interface JG Hjörleifsson, B Ásgeirsson FEBS Open bio 9 (1), 169-184, 2019 | 7 | 2019 |
| Structural Characterization of Functionally Important Chloride Binding Sites in the Marine Vibrio Alkaline Phosphatase S Markússon, JG Hjorleifsson, P Kursula, B Ásgeirsson Biochemistry 61 (20), 2248-2260, 2022 | 5 | 2022 |
| The high catalytic rate of the cold‐active Vibrio alkaline phosphatase requires a hydrogen bonding network involving a large interface loop JG Hjörleifsson, R Helland, M Magnúsdóttir, B Ásgeirsson FEBS Open bio 11 (1), 173-184, 2021 | 4 | 2021 |
| Ionic effects on subunit interactions in a cold-active alkaline phosphatase from the marine bacterium Vibrio splendidus JG Hjörleifsson Jens Guðmundur Hjörleifsson, 2018 | 1 | 2018 |
