Zobrazeno 1 - 10
of 414
pro vyhledávání: '"I Boime"'
Publikováno v:
Journal of Biological Chemistry. 269:10574-10580
There are six intramolecular disulfide (S-S) bonds that form during intracellular folding of the human chorionic gonadotropin (hCG)-beta subunit. Site-directed mutagenesis of every pair of Cys residues involved in the formation of each S-S bond was u
Publikováno v:
Endocrinology. 141(12)
The crystal structure of human CG reveals that each subunit is a member of the superfamily of cystine-knot growth factors. Although the distribution of the cysteine residues in all the beta-subunits is conserved, the conformation of the human FSH dim
Publikováno v:
European journal of immunology. 28(11)
During mammalian pregnancy, one or more semiallogeneic fetuses gestate in direct contact with the maternal circulation and uterine tissue. However, a damaging maternal immune response is not normally provoked. We studied two possible mechanisms for t
Autor:
T, Moriwaki, N, Suganuma, M, Furuhashi, F, Kikkawa, Y, Tomoda, I, Boime, M, Nakata, T, Mizuochi
Publikováno v:
Glycoconjugate journal. 14(2)
The human chorionic gonadotropin beta-subunit (hCGbeta) is a glycoprotein in which 12 cysteine residues pair to form six intramolecular disulfide bonds. In order to elucidate the effect of each disulfide bond on glycosylation of the molecule, we anal
Publikováno v:
The Journal of biological chemistry. 271(18)
The gonadotropin/thyrotropin hormone family is characterized by a heterodimeric structure composed of a common alpha subunit noncovalently linked to a hormone-specific beta subunit. The conformation of the heterodimer is essential for controlling sec
Autor:
D, Ben-Menahem, I, Boime
Publikováno v:
Trends in endocrinology and metabolism: TEM. 7(3)
One of the distinguishing features of the gonadotropin and thyrotropin hormone family is their heterodimeric structure; the subunits combine early in the secretory pathway and only the dimers are capable of binding to receptors. Therefore, assembly i
Publikováno v:
The Journal of biological chemistry. 269(41)
Human chorionic gonadotropin (hCG) is a member of a family of heterodimeric glycoprotein hormones that contain a common alpha subunit but differ in their hormone-specific beta subunits. Site-directed mutagenesis was used to examine the role of the fi
Publikováno v:
The Journal of biological chemistry. 269(14)
There are six intramolecular disulfide (S-S) bonds that form during intracellular folding of the human chorionic gonadotropin (hCG)-beta subunit. Site-directed mutagenesis of every pair of Cys residues involved in the formation of each S-S bond was u
Publikováno v:
The Journal of biological chemistry. 269(7)
Transcriptional activation of the chorionic gonadotropin (CG) genes is linked to trophoblast differentiation. In a multistep process, cytotrophoblasts expressing only the alpha subunit differentiate into intermediates that coexpress the CG beta subun