Location and Mechanism of α2,6-Sialyltransferase Dimer Formation
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
1. Biological roles of oligosaccharides: all of the theories are correct
2. Two Naturally Occurring α2,6-Sialyltransferase Forms with a Single Amino Acid Change in the Catalytic Domain Differ in Their Catalytic Activity and Proteolytic Processing
3. A Disulfide-bonded Dimer of the Golgi β-Galactoside α2,6-Sialyltransferase Is Catalytically Inactive yet Still Retains the Ability to Bind Galactose
4. Formation of Insoluble Oligomers Correlates with ST6Gal I Stable Localization in the Golgi
5. Letters to the Glyco-Forum Identification of two novel conserved amino acid residues in eukaryotic sialyltransferases: implications for their mechanism of action
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