ArticleCharacterization of growth hormone-releasing hormone (GHRH) binding to cloned porcine GHRH receptor
References (22)
- et al.
Characterization of [125I-Tyr10]-human growth hormone-releasing factor (1–44) amide binding to rat pituitary: evidence for high and low affinity classes of sites
Brain Res.
(1990) - et al.
Proteolytic degradation of rat growth hormone-releasing factor (1–29) amide in rat pituitary and hypothalamus
Brain Res.
(1993) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
Anal. Biochem.
(1976)- et al.
Human growth hormone-releasing hormone analogues with much improved in vitro growth hormone-releasing potencies in rat pituitary cells
Eur. J. Pharmacol.
(1991) - et al.
Structure and functional expression of a complementary DNA for porcine growth hormone-releasing hormone receptor
Neuropeptides
(1993) - et al.
Ligand: A versatile computerized approach for characterization of ligand-binding systems
Anal. Biochem.
(1980) - et al.
Degradation of aspartic acid and asparagine residues in human growth hormone-releasing factor
Int. J. Pept. Protein Res.
(1992) Reconstitution of receptor/GTP-binding protein interactions
Biochim. Biophys. Acta
(1991)- et al.
Differential effect of N-terminal modifications on the biological potencies of growth hormone releasing factor analogues with varying lengths
J. Med. Chem.
(1986) - et al.
Simultaneous analysis of families of sigmoidal curves: Application to bioassay, radioligand assay and physiological dose-response curves
Am. J. Physiol.
(1978)
Degradation of growth hormone releasing factor analogs in neutral aqueous solution is related to deamidation of asparagine residues
Int. J. Pept. Protein Res.
(1991)
Cited by (6)
Chapter 3 Diseases Associated with Growth Hormone-Releasing Hormone Receptor (GHRHR) Mutations
2009, Progress in Molecular Biology and Translational ScienceCitation Excerpt :The C‐terminal domain exhibits numerous phosphorylation sites likely meant to interact with GRK/beta arrestin. Several highly conserved sequences have been identified in all the mammalian GHRHRs (human, mouse, rat, bovine, and porcine) cloned to date54,62–68 and in the teleost fish.69 Figure 3 compares the primary structures of the GHRHR from different species and highlights the consensus areas.
Biological activities of two porcine growth hormone-releasing hormone receptor isoforms
2001, Archives of Biochemistry and BiophysicsStructure and function of the growth-hormone-releasing hormone receptor
2000, Vitamins and HormonesHypothalamic Hormones
2015, Drug Discovery and Evaluation: Pharmacological Assay, Fourth EditionInternational Union of Pharmacology. XXXV. The glucagon receptor family
2003, Pharmacological Reviews
Copyright © 1995 Published by Elsevier Inc.