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1 ugate substrates and nucleotide sugar donor, CMP-sialic acid.
2 . cerevisiae vesicles were able to transport CMP-sialic acid.
4 for polymerizing sialyl residues from donor CMP-sialic acid are not homologous glycosyltransferases.
5 rmined structure of pig ST3GAL1, including a CMP-sialic acid-binding site assembled from conserved si
6 back inhibition of GNE-epimerase activity by CMP-sialic acid causes excessive production of free sial
8 ar treatment of TNFR-IgG with alpha2,3ST and CMP-sialic acid (CMP-Sia), in the presence of MnCl(2), p
10 s were performed to predict and evaluate the CMP-sialic acid donor and glycan acceptor interactions,
11 lation of expression of the transporters for CMP-sialic acid, GDP-fucose, or both unexpectedly result
13 s are an exception, because of a mutation in CMP-sialic acid hydroxylase, which occurred after our co
15 n efficiently and effectively substitute for CMP-sialic acid in extracellular ST6Gal-1-mediated sialy
17 ans including kidney, a critical shortage of CMP-sialic acid prevented sialylation of nephrin and pod
18 back inhibition of GNE-epimerase activity by CMP-sialic acid recovered after silencing demonstrating
19 study, we characterize the first functional CMP-sialic acid synthase (DmCSAS) from any protostome li
21 sialic acid 9-phosphate synthase (SAS), and CMP-sialic acid synthetase (CSAS) were coexpressed in in
22 se compounds are subsequently activated by a CMP-sialic acid synthetase and transferred to a wide ran
23 ed in media lacking sialic acid, and a siaB (CMP-sialic acid synthetase) mutant was deficient in biof
25 ed by serum-localized nucleotide sugar donor CMP-sialic acid that is at least partially derived from
26 er Golgi membranes were incubated with [(3)H]CMP sialic acid to radiolabel endogenous soluble and mem
27 2 catalyzes the transfer of sialic acid from CMP-sialic acid to a growing chain of polysialic acid at
28 e reactions that transfer a sialic acid from CMP-sialic acid to an acceptor (a structure terminated w
29 s helix may swing down upon binding to donor CMP-sialic acid to form the binding pocket for an accept
30 the transporter supplied limited amounts of CMP-sialic acid to Golgi sialyltransferases but was unab
31 ere very similar to the previously described CMP-sialic acid transport characteristics observed with
33 viously described cDNA encoding the putative CMP-sialic acid transporter encodes the transporter prot
34 ned the interactions of nucleotides with the CMP-sialic acid transporter in order to better understan
35 tionally expressed the murine Golgi putative CMP-sialic acid transporter in Saccharomyces cerevisiae.
36 o the lumen of the Golgi complex through the CMP-sialic acid transporter, an antiporter that also fun
39 termost structures of animal cells, requires CMP-sialic acid, which is a product of the nuclear enzym
40 itutions at C-5 or C-9 of the sialic acid in CMP-sialic acid, while its acceptor substrate specificit
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