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1 of IEPOX, 2-methyltetrol, and 2-methyltetrol sulfate ester.
2 dification for their activity in hydrolyzing sulfate esters.
3 e sulfuryl donor for the biosynthesis of all sulfate esters and also as a precursor of reduced sulfur
4 nionic groups, such as monophosphate esters, sulfate esters, and carboxylic acids, with high specific
5 for AP-catalyzed reactions of phosphate and sulfate esters are "loose" and indistinguishable from th
7 a number of tetrasaccharides confirmed that sulfate esters at C-6 are critical for binding, whereas
8 to determine that oligosaccharides with the sulfate esters at the nonreducing ends preferentially bi
10 valent sulfur was exclusively represented by sulfate esters, consistent with bacterial sulfotransfera
12 me hydrolysis of polyphenol glucuronides and sulfate esters, extraction, and dansylation of unconjuga
13 it serves as the universal sulfate donor for sulfate ester formation in higher organisms, we have und
18 determined k(cat)/K(M) for a series of aryl sulfate ester monoanions to obtain the Bronsted coeffici
19 of these organosulfates is identified as the sulfate ester of IEPOX, a second generation oxidation pr
20 ient fine aerosol are attributed to isomeric sulfate esters of 2,3-dihydroxypent-4-enoic acid, of whi
21 he MW 226 compounds are assigned to isomeric sulfate esters of 3,4-dihydroxyhex-5-enoic acid with the
22 t the HCV envelope glycoproteins rely upon O-sulfated esters of a heparin homologue to facilitate ent
25 nal anionic functional groups in the form of sulfate esters, on a polymerized liposome surface contai
27 ith the potent adjuvant raffinose fatty acid sulfate ester (RFASE) showed significant inhibition of t
28 o- and disulfide), and oxidized S (inorganic sulfate, ester sulfate, and sulfonate)-were identified i
29 Type I sulfatases catalyze the hydrolysis of sulfate esters through S-O bond cleavage and possess a c
31 talyze the cleavage of a variety of cellular sulfate esters via a novel mechanism that requires the a
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