ライフサイエンスコーパス: hCG-beta

1 logical assay that showed that the hCG-alpha-hCG-beta heterodimer facilitated human CG receptor-media

2 e tested for hCG, hCG free beta subunit, and hCG beta-core fragment.

3 and that a conformational difference between hCG-beta and mCG-beta was recapitulated in the context o

4 important tumor markers: AFP, ferritin, CEA, hCG-beta, CA 15-3, CA 125, and CA 19-9.

5 Like its human counterpart hCG-beta with which it shares 81% identity, macaque (m)C

6 ained indicate that the amount of detectable hCG-beta-chaperone complexes correlates with the rate or

7 eta-subunit of human chorionic gonadotropin (hCG-beta).

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 lation of syncytin 1 and syncytin 2, but not hCG beta, in primary human cytotrophoblasts.

11 about whether some biological activities of hCG beta-subunit (hCGbeta) preparations are caused by th

12 it (L2 beta) can be switched into L2 beta of hCG beta without a loss of receptor binding, yet mutatio

13 PFF increased the mRNA and protein levels of hCG beta, syncytin 1, syncytin 2, and GCM1; and knockdow

14 PFF acts via NPFFR2 to enhance production of hCG beta and promote GCM1-dependent expression of syncyt

15 f secretable beta, and that the complexes of hCG-beta with chaperones involve the formation of interm

16 or extent of folding, that the complexes of hCG-beta with ER chaperones lead to the formation of sec

17 ave been detected in slow folding mutants of hCG-beta subunit that lack both of the N-linked oligosac

18 he absence of carbohydrate or to the rate of hCG-beta subunit folding, 2) whether such complexes are

19 lation differences, we generated a series of hCG-beta-mCG-beta chimeras and identified domains that c

20 s not detected by X-ray analysis of secreted hCG-beta.

21 e human chorionic gonadotropin beta-subunit (hCG-beta) reveals the presence of a disulfide between Cy

22 e human chorionic gonadotropin beta-subunit (hCG-beta).

23 either native or dimeric hTSH containing the hCG beta-subunit-carboxyl-terminal peptide, suggesting t

24 s using the carboxyl-terminal peptide of the hCG beta-subunit as a linker created unimolecular hTSH w

25 2) terminus, cystine knot, and loop 2 of the hCG beta-subunit.

26 hCG-beta form, and 3) what the nature of the hCG-beta-chaperone binding is.

27 Because folding of wild type hCG-beta subunit occurs in the ER with a t1/2 = 4-5 min,

28 in, stable association of ER chaperones with hCG-beta have been difficult to detect probably because

29 re preferentially secreted and combined with hCG-beta.

30 eted, and its ability to heterodimerize with hCG-beta.