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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  is enabled by Bacteroides EstA, a sialate O-acetylesterase acting on glycosidically linked sialylate
     5  mRNA levels correlate with differences in O-acetylesterase activity described in adult tissues and b
  
     7 expressed Lse protein exhibits sialic-acid O-acetylesterase activity that is not attributable to a ty
  
     9 similar to OC43-HE, also possessed sialate-O-acetylesterase activity, and acted as a receptor-destroy
  
    11  determined that the HKU1-HE protein is an O-acetylesterase and acts as a receptor-destroying enzyme 
    12  acid degradation by Bacteroidetes sialate-O-acetylesterases and sialidases, respectively, and subseq
  
    14 ouse tissues, this cytosolic sialic acid 9-O-acetylesterase form has a rather restricted distribution
  
  
    17 planted mice induced for expression of the O-acetylesterase in the ALL cells exhibited a reduction of
    18 olecular cloning of a sialic acid-specific O-acetylesterase in vertebrates and suggests novel roles f
    19 inding of HKU1-S1 to RD cells, whereas the O-acetylesterase-inactive HKU1-HE mutant lost this capacit
    20 highly expressed active Aspergillus nidulans acetylesterases localized to the apoplast and had signif
    21 ptide fragments of a lysosomal sialic acid O-acetylesterase (Lse) previously purified from rat liver,
    22 dues from Neu5Ac on the cell surface by an O-acetylesterase made ALL cells more vulnerable to such dr
    23 hough the lysosomal sialic acid-specific 9-O-acetylesterase message has a widespread pattern of expre
  
  
    26 ogues to pectin methylesterase (PME), pectin acetylesterase (PAE) and pectate lyase (PL) where all hi
    27 ic sequence analysis, we identified a pectin acetylesterase (PAE1) from black cottonwood (Populus tri
  
  
  
  
    32  acting on glycosidically linked sialylate-O-acetylesterase substrates, particularly at neutral pH.  
  
  
    35 ncoding a lysosomal sialic acid-specific 9-O-acetylesterase, which traverses the endoplasmic reticulu
    36 ha/beta hydrolase fold of rhamnogalacturonan acetylesterase with which it shares esterase activity.  
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