The human sialyltransferase family
A Harduin-Lepers, V Vallejo-Ruiz… - Biochimie, 2001 - Elsevier
The human genome encodes probably more than 20 different sialyltransferases involved in
the biosynthesis of sialylated glycoproteins and glycolipids but to date only 15 different …
the biosynthesis of sialylated glycoproteins and glycolipids but to date only 15 different …
Protein N-glycosylation in the baculovirus-insect cell system
X Shi, DL Jarvis - Current drug targets, 2007 - ingentaconnect.com
One of the major advantages of the baculovirus-insect cell system is that it is a eukaryotic
system that can provide posttranslational modifications, such as protein N-glycosylation …
system that can provide posttranslational modifications, such as protein N-glycosylation …
The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach
A Harduin-Lepers, R Mollicone, P Delannoy… - …, 2005 - academic.oup.com
The animal sialyltransferases are Golgi type II transmembrane glycosyltransferases. Twenty
distinct sialyltransferases have been identified in both human and murine genomes. These …
distinct sialyltransferases have been identified in both human and murine genomes. These …
Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria
R Oriol, R Mollicone, A Cailleau, L Balanzino… - …, 1999 - academic.oup.com
On the basis of function and sequence similarities, the vertebrate fucosyltransferases can be
classified into three groups: α-2-, α-3-, and α-6-fucosyltransferases. Thirty new putative …
classified into three groups: α-2-, α-3-, and α-6-fucosyltransferases. Thirty new putative …
Polysialic acid: three-dimensional structure, biosynthesis and function
M Mühlenhoff, M Eckhardt… - Current opinion in …, 1998 - Elsevier
Polysialic acid is a unique cell surface polysaccharide found in the capsule of neuroinvasive
bacteria and as a highly regulated post-translational modification of the neural cell adhesion …
bacteria and as a highly regulated post-translational modification of the neural cell adhesion …
Structure/function studies of glycosyltransferases
C Breton, A Imberty - Current opinion in structural biology, 1999 - Elsevier
Glycosyltransferases are the enzymes that synthesize oligosaccharides, polysaccharides
and glycoconjugates. The analysis of the wealth of sequences that are now available in …
and glycoconjugates. The analysis of the wealth of sequences that are now available in …
Current trends in the structure–activity relationships of sialyltransferases
M Audry, C Jeanneau, A Imberty… - …, 2011 - academic.oup.com
Sialyltransferases (STs) represent an important group of enzymes that transfer N-
acetylneuraminic acid (Neu5Ac) from cytidine monophosphate-Neu5Ac to various acceptor …
acetylneuraminic acid (Neu5Ac) from cytidine monophosphate-Neu5Ac to various acceptor …
Polysialyltransferase: a new target in metastatic cancer
RA Falconer, RJ Errington… - Current cancer drug …, 2012 - ingentaconnect.com
Polysialic acid (polySia) is a carbohydrate polymer critical for neuronal cell migration and
axon pathfinding in embryonic development. Besides brain regions requiring persistent …
axon pathfinding in embryonic development. Besides brain regions requiring persistent …
Structural insight into mammalian sialyltransferases
FV Rao, JR Rich, B Rakić, S Buddai… - Nature structural & …, 2009 - nature.com
Sialic acid is the most abundant terminal monosaccharide on mammalian cell surface
glycoconjugates. The crystal structures of a mammalian sialyltransferase, that of porcine …
glycoconjugates. The crystal structures of a mammalian sialyltransferase, that of porcine …
Characterization of the second type of human β-galactoside α2, 6-sialyltransferase (ST6Gal II), which sialylates Galβ1, 4GlcNAc structures on oligosaccharides …
S Takashima, S Tsuji, M Tsujimoto - Journal of Biological Chemistry, 2002 - ASBMB
A novel member of the human β-galactoside α2, 6-sialyltransferase (ST6Gal) family,
designated ST6Gal II, was identified by BLAST analysis of expressed sequence tags and …
designated ST6Gal II, was identified by BLAST analysis of expressed sequence tags and …