
1. The cloning of the mammalian gonadotropin-releasing hormone receptor sets the stage for rapid progress in understanding the structure of the receptor, its interaction with ligand, and its mechanisms of activation. 2. The receptor is a 327 to 328-amino acid seven-transmembrane domain G protein-coupled receptor. 3. Recent site-direct mutagenesis studies have provided considerable insight into glycosylation of the receptor, the arrangement of the helices, and the ligand binding domains.
Mammals, Sheep, Sequence Homology, Amino Acid, Protein Conformation, Molecular Sequence Data, Recombinant Proteins, Rats, Mice, Animals, Humans, Cattle, Amino Acid Sequence, Cloning, Molecular, Receptors, LHRH
Mammals, Sheep, Sequence Homology, Amino Acid, Protein Conformation, Molecular Sequence Data, Recombinant Proteins, Rats, Mice, Animals, Humans, Cattle, Amino Acid Sequence, Cloning, Molecular, Receptors, LHRH
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 41 | |
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| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
