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1 al was ten-fold less effective than the free alpha-galactosyl epitope.
2 n cells that were manipulated to express the alpha-galactosyl epitope.
3 ransferase responsible for generation of the alpha-galactosyl epitope.
4 , even if these cells express low numbers of alpha-galactosyl epitopes.
5 surface carbohydrates, such as appearance of alpha-galactosyl epitopes as a result of up-regulation o
6                  Anti-Gal interacts with the alpha-galactosyl epitope (Ga1alpha1-3Galbeta1-4GlcNAc-R)
7                           The synthetic free alpha-galactosyl epitope (Gal alpha1-3Gal beta1-4GlcNAc)
8 ge were found to express very low amounts of alpha-galactosyl epitopes (Gal alpha1-3Gal beta1-4GlcNAc
9 cDNA resulted in synthesis and expression of alpha-galactosyl epitopes (Gal(alpha)1-3Gal(beta)1-4GlcN
10 te that, like other retroviruses bearing the alpha-galactosyl epitope, HIV modified to express this e
11 ural anti-Gal antibody, which interacts with alpha-galactosyl epitopes (i.e., Gal alpha1-3Gal beta1-4
12 IV passaged through these cells acquired the alpha-galactosyl epitope in association with the envelop
13 f a synthetic disaccharide that contains the alpha-galactosyl epitope, indicating that virolysis is m
14             This carbohydrate structure (the alpha-galactosyl epitope) is expressed on the cells of m
15 00-fold, as measured in ELISA with synthetic alpha-galactosyl epitopes linked to bovine serum albumin
16 e, these data suggest that expression of the alpha-galactosyl epitope on the surface of viruses may h
17 ed HUT-78 cells expressed high levels of the alpha-galactosyl epitope on their membrane surface, rend
18            It is suggested that synthesis of alpha-galactosyl epitopes on freshly isolated human tumo
19 primate immune system responds vigorously to alpha-galactosyl epitopes on xenografts by activating ma
20                                              alpha-Galactosyl epitopes were synthesized in vitro on h

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