Anthony J. Mason

TL;DR: The entire 1,370-amino-acid sequence of the human insulin receptor precursor is deduced from a single complementary DNA clone, finding sequence homologies to human epidermal growth factor receptor and the members of the src family of oncogene products.

TL;DR: The N-terminal amino-acid sequence data on the subunits of each inhibin are used to identify cloned complementary DNAs encoding the biosynthetic precursors and report that inhibins are the product of a gene family that also includes transforming growth factor-β (TGF-β) and whose structural organization is similar to that of pituitary and placental glycoprotein hormones.

TL;DR: The partially deleted gene for the common biosynthetic precursor of gonadotropin-releasing hormone and GnRH-associated peptide is transcriptionally active as revealed by in situ hybridization histochemistry of hpg hypothalamic tissue sections, but immunocytochemical analysis failed to show the presence of antigen corresponding to any part of the precursor protein.

TL;DR: Immunocytochemistry and in situ hybridization showed that GnRH expression was restored in the appropriate hypothalamic neurons of the transgenic hpg animals, an indication of neural-specific expression of the introduced gene.

TL;DR: Cloned cDNAs encoding the precursor protein for gonadotropin-releasing hormone and prolactin release-inhibiting factor were isolated from libraries derived from human and rat hypothalamic mRNA and showed identity between the human placental and human hypothalamic precursor proteins.