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1 logical assay that showed that the hCG-alpha-hCG-beta heterodimer facilitated human CG receptor-media
3 and that a conformational difference between hCG-beta and mCG-beta was recapitulated in the context o
6 ained indicate that the amount of detectable hCG-beta-chaperone complexes correlates with the rate or
8 they lead to formation of a secreted, mature hCG-beta form, and 3) what the nature of the hCG-beta-ch
9 7 were of macaque origin (PGVD), the mutated hCG-beta subunit displayed macaque-like conformational r
10 about whether some biological activities of hCG beta-subunit (hCGbeta) preparations are caused by th
11 it (L2 beta) can be switched into L2 beta of hCG beta without a loss of receptor binding, yet mutatio
12 f secretable beta, and that the complexes of hCG-beta with chaperones involve the formation of interm
13 or extent of folding, that the complexes of hCG-beta with ER chaperones lead to the formation of sec
14 ave been detected in slow folding mutants of hCG-beta subunit that lack both of the N-linked oligosac
15 he absence of carbohydrate or to the rate of hCG-beta subunit folding, 2) whether such complexes are
16 lation differences, we generated a series of hCG-beta-mCG-beta chimeras and identified domains that c
18 e human chorionic gonadotropin beta-subunit (hCG-beta) reveals the presence of a disulfide between Cy
20 either native or dimeric hTSH containing the hCG beta-subunit-carboxyl-terminal peptide, suggesting t
21 s using the carboxyl-terminal peptide of the hCG beta-subunit as a linker created unimolecular hTSH w
25 in, stable association of ER chaperones with hCG-beta have been difficult to detect probably because
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