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1 ell receptor activation known as sialic acid acetylesterase.
2 ng hemicellulose- and pectin-specific fungal acetylesterases.
3  similarity to endoplasmic reticulum-derived acetylesterases.
4 ibes how one pectin-modifying enzyme, PECTIN ACETYLESTERASE 9 (PAE9), affects the Arabidopsis (Arabid
5  is enabled by Bacteroides EstA, a sialate O-acetylesterase acting on glycosidically linked sialylate
6      We determine that AlgF does not exhibit acetylesterase activity and is unable to bind to polyman
7  mRNA levels correlate with differences in O-acetylesterase activity described in adult tissues and b
8    This catalytic triad is also required for acetylesterase activity in vitro.
9 expressed Lse protein exhibits sialic-acid O-acetylesterase activity that is not attributable to a ty
10                                         Ape1 acetylesterase activity was confirmed in vitro using p-n
11  and Achromobacter insuavis and demonstrated acetylesterase activity with chromogenic substrates.
12 similar to OC43-HE, also possessed sialate-O-acetylesterase activity, and acted as a receptor-destroy
13 eviously described cytosolic sialic acid 9-O-acetylesterase activity.
14  determined that the HKU1-HE protein is an O-acetylesterase and acts as a receptor-destroying enzyme
15 rther corroborated by hydrolysis with pectin acetylesterases and by nuclear magnetic resonance spectr
16  acid degradation by Bacteroidetes sialate-O-acetylesterases and sialidases, respectively, and subseq
17  Ser carboxypeptidases, ABHD protein, pectin acetylesterase, and other SHs.
18  appended to a receptor-destroying sialate-O-acetylesterase ("esterase").
19 ouse tissues, this cytosolic sialic acid 9-O-acetylesterase form has a rather restricted distribution
20                    Thus, two sialic acid 9-O-acetylesterases found in very different subcellular comp
21                 Our data suggest that pectin acetylesterase functions as an important structural regu
22 planted mice induced for expression of the O-acetylesterase in the ALL cells exhibited a reduction of
23 olecular cloning of a sialic acid-specific O-acetylesterase in vertebrates and suggests novel roles f
24 inding of HKU1-S1 to RD cells, whereas the O-acetylesterase-inactive HKU1-HE mutant lost this capacit
25 highly expressed active Aspergillus nidulans acetylesterases localized to the apoplast and had signif
26 ptide fragments of a lysosomal sialic acid O-acetylesterase (Lse) previously purified from rat liver,
27 dues from Neu5Ac on the cell surface by an O-acetylesterase made ALL cells more vulnerable to such dr
28 hough the lysosomal sialic acid-specific 9-O-acetylesterase message has a widespread pattern of expre
29         Samples were digested by a sialate-O-acetylesterase (NanS) to confirm the presence of O-acety
30                                The GBS Sia O-acetylesterase operates cooperatively with the GBS CMP-S
31 ogues to pectin methylesterase (PME), pectin acetylesterase (PAE) and pectate lyase (PL) where all hi
32 ic sequence analysis, we identified a pectin acetylesterase (PAE1) from black cottonwood (Populus tri
33 that the HKU1-HE protein possesses sialate-O-acetylesterase RDE activity.
34 rotein possesses the corresponding sialate-O-acetylesterase RDE activity.
35                                  Sialic acid acetylesterase (SIAE) is an enzyme that negatively regul
36 -specific O-acetyltransferases (SOATs) and O-acetylesterases (SIAEs) that add and remove O-acetyl gro
37 site and the receptor-destroying enzyme (9-O-acetylesterase) sites, by using receptor analogues.
38  acting on glycosidically linked sialylate-O-acetylesterase substrates, particularly at neutral pH.
39              We now characterize a GBS Sia O-acetylesterase that modulates the degree of GBS surface
40 e gut bacteria, in turn, produce sialylate-O-acetylesterases to remove them.
41 ncoding a lysosomal sialic acid-specific 9-O-acetylesterase, which traverses the endoplasmic reticulu
42 ha/beta hydrolase fold of rhamnogalacturonan acetylesterase with which it shares esterase activity.