Wylie Vale
Salk Institute for Biological Studies
877 Papers
19.7K Citations
Wylie Vale is an academic researcher from Salk Institute for Biological Studies. The author has contributed to research in topics: Receptor & Somatostatin. The author has an hindex of 163, co-authored 876 publications. Previous affiliations of Wylie Vale include Texas Tech University Health Sciences Center & Hammersmith Hospital.
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Papers
Plasma growth hormone responses to constant infusions of human pancreatic growth hormone releasing factor. Intermittent secretion or response attenuation.
C B Webb,Mary Lee Vance,Michael O. Thorner,Gladys Perisutti,Jennifer L. Thominet,Jean Rivier,Wylie Vale,Lawrence A. Frohman +7 more
TL;DR: The results indicate that GH secretion is dose responsive to hpGRF(1-40) infusions, though the response is complex, and the absence of impaired TSH secretion provides evidence against a mediating role of somatostatin.
Corticotropin-releasing factor receptor type 2 messenger ribonucleic acid in rat pituitary: localization and regulation by immune challenge, restraint stress, and glucocorticoids.
TL;DR: It is demonstrated that the expression of CRF R2 in the pituitary is sensitive to alterations to the hypothalamic-pituitary-adrenal axis as CRf R2 mRNA levels in the anterior pituitaries of male rats were significantly decreased 6 h after bacterial endotoxin lipopolysaccharide injection or restraint stress.
Pituitary binding sites for [3H]-labelled luteinizing hormone releasing factor (LRF)
TL;DR: Normal rat anterior pituitary cells in culture possess two binding sites for LRF, one of which corresponds to the half-maximal biological potency of LRF and the other has low affinity and an enormously higher capacity to bind LRF.
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Photo-cross-linkers incorporated into G-protein-coupled receptors in mammalian cells: a ligand comparison.
TL;DR: It is shown that a well-balanced system for non-natural amino acid mutagenesis allows the ligand binding sites of a class II G-protein coupled receptor to be mapped and distinct binding domains to be identified for different ligands in the native environment of mammalian cells.
Constitutive activation of tethered-peptide/ corticotropin-releasing factor receptor chimeras
TL;DR: Results support a propinquity effect in CRF receptor activation, in which the amino-terminal portion of the CRF peptide is presented to the body of the receptor in the proper proximity for activation, and may prove useful in analyzing mechanisms of receptor regulation and in the structural analysis of ligand activated receptors.
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