Result Number | Material Type | Add to My Shelf Action | Record Details and Options |
---|---|---|---|
1 |
Material Type: Artigo
|
Pituitary FSH is released by a heterodimer of the β -subunits from the two forms of inhibinLing, Nicholas ; Ying, Shao-Yao ; Ueno, Naoto ; Shimasaki, Shunichi ; Esch, Frederick ; Hotta, Mari ; Guillemin, RogerNature (London), 1986-06, Vol.321 (6072), p.779-782 [Periódico revisado por pares]EnglandTexto completo disponível |
|
2 |
Material Type: Artigo
|
Complementary DNA sequences of ovarian follicular fluid inhibin show precursor structure and homology with transforming growth factor- βSeeburg, Peter H ; Ying, Shao-Yao ; Hayflick, Joel S ; Ueno, Naoto ; Mason, Anthony J ; Esch, Frederick ; Guillemin, Roger ; Ling, Nicholas ; Niall, HughNature (London), 1985-12, Vol.318 (6047), p.659-663 [Periódico revisado por pares]London: Nature PublishingTexto completo disponível |
|
3 |
Material Type: Artigo
|
Inhibins, activins and follistatinsYing, S YJournal of steroid biochemistry, 1989, Vol.33 (4), p.705-713 [Periódico revisado por pares]England: Elsevier B.VTexto completo disponível |
|
4 |
Material Type: Artigo
|
Inhibin and beta type transforming growth factor (TGF β) have opposite modulating effects on the follicle stimulating hormone (FSH)-induced aromatase activity of cultured rat granulosa cellsYing, Shao-Yao ; Becker, Ann ; Ling, Nicholas ; Ueno, Naoto ; Guillemin, RogerBiochemical and biophysical research communications, 1986-05, Vol.136 (3), p.969-975 [Periódico revisado por pares]San Diego, CA: Elsevier IncTexto completo disponível |
|
5 |
Material Type: Artigo
|
A homodimer of the β-subunits of inhibin a stimulates the secretion of pituitary follicle stimulating hormoneLing, Nicholas ; Ying, Shao-Yao ; Ueno, Naoto ; Shimasaki, Shunichi ; Hotta, Frederick Esch Mari ; Guillemin, RogerBiochemical and biophysical research communications, 1986-08, Vol.138 (3), p.1129-1137 [Periódico revisado por pares]San Diego, CA: Elsevier IncTexto completo disponível |
|
6 |
Material Type: Artigo
|
Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormoneUeno, N ; Ling, N ; Ying, S.Y ; Esch, F ; Shimasaki, S ; Guillemin, RProceedings of the National Academy of Sciences - PNAS, 1987-12, Vol.84 (23), p.8282-8286 [Periódico revisado por pares]Washington, DC: National Academy of Sciences of the United States of AmericaTexto completo disponível |
|
7 |
Material Type: Artigo
|
(DTrp 6 -Pro 9 -NEt)-luteinising hormone-releasing factor inhibits follicular development in hypophysectomised ratsYING, SHAO-YAO ; GUILLEMIN, ROGERNature (London), 1979-08, Vol.280 (5723), p.593-595 [Periódico revisado por pares]Texto completo disponível |
|
8 |
Material Type: Artigo
|
Immunohistochemical detection of inhibin in the gonadCuevas, Pedro ; Ying, Shao-Yao ; Ling, Nicholas ; Ueno, Naoto ; Esch, Frederick ; Guillemin, RogerBiochemical and biophysical research communications, 1987-01, Vol.142 (1), p.23-30 [Periódico revisado por pares]San Diego, CA: Elsevier IncTexto completo disponível |
|
9 |
Material Type: Artigo
|
Primary Structure of the Human Follistatin Precursor and Its Genomic OrganizationShimasaki, Shunichi ; Koga, Makoto ; Esch, Frederick ; Cooksey, Karen ; Mercado, Maluz ; Koba, Ann ; Ueno, Naoto ; Ying, Shao-Yao ; Ling, Nicholas ; Guillemin, RogerProceedings of the National Academy of Sciences - PNAS, 1988-06, Vol.85 (12), p.4218-4222 [Periódico revisado por pares]Washington, DC: National Academy of Sciences of the United States of AmericaTexto completo disponível |
|
10 |
Material Type: Artigo
|
Type beta transforming growth factor (TGF-β) is a potent stimulator of the basal secretion of follicle stimulating hormone (FSH) in a pituitary monolayer systemYing, Shao-Yao ; Becker, Ann ; Baird, Andrew ; Ling, Nicholas ; Ueno, Naoto ; Esch, Frederick ; Guillemin, RogerBiochemical and biophysical research communications, 1986-03, Vol.135 (3), p.950-956 [Periódico revisado por pares]San Diego, CA: Elsevier IncTexto completo disponível |