Glyceryl ether monooxygenase resembles aromatic amino acid hydroxylases in metal ion and tetrahydrobiopterin dependence

Articles in the same Issue

1. Editor's Note
2. Editor's Note
3. Protein Structure and Function
4. Glyceryl ether monooxygenase resembles aromatic amino acid hydroxylases in metal ion and tetrahydrobiopterin dependence
5. Biochemical characterization of the catalytic domains of three different clostridial collagenases
6. Impact of detergents on the activity of acetylcholinesterase and on the effectiveness of its inhibitors
7. The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING protein
8. Membranes, Lipids, Glycobiology
9. Glycosphingolipids from bovine milk and milk fat globule membranes: a comparative study. Adhesion to enterotoxigenic Escherichia coli strains
10. Mannose 6-phosphate receptor-dependent endocytosis of lysosomal enzymes is increased in sulfatide-storing kidney cells
11. Cell Biology and Signaling
12. Heavy metals induce phosphorylation of the Bcl-2 protein by Jun N-terminal kinase
13. Fibroblast growth factor 2 (FGF-2) is a novel substrate for arginine methylation by PRMT5
14. Differential functions of the Apoer2 intracellular domain in selenium uptake and cell signaling
15. Active immunisation against gastric inhibitory polypeptide (GIP) improves blood glucose control in an animal model of obesity-diabetes
16. Novel Techniques
17. Applicability of superfolder YFP bimolecular fluorescence complementation in vitro