Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P01178 (oxytocin)
 15,767 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Studies to discover novel, potent and selective oxytocin antagonists are reported. Combinatorial libraries designed to find novel replacements of fragments of oxytocin antagonist L-371,257, identified pyrimidine, thiazole, indole and benzofuran as potential alternatives to the benzoic acid moiety of L-371,257. Additional investigations identified indole and benzofuran derivatives with potent oxytocin antagonist activity.
 ...
PMID:Identification of potent and selective oxytocin antagonists. Part 1: indole and benzofuran derivatives. 1199 86

Leucine aminopeptidases (LAPs) are metallopeptidases that cleave N-terminal residues from proteins and peptides. While hydrolyzing Leu substrates, LAPs often have a broader specificity. LAPs are members of the M1 or M17 peptidase families, and therefore the LAP nomenclature is complex. LAPs are often viewed as cell maintenance enzymes with critical roles in turnover of peptides. In mammals, the M17 and M1 enzymes with LAP activity contribute to processing peptides for MHC I antigen presentation, processing of bioactive peptides (oxytocin, vasopressin, enkephalins), and vesicle trafficking to the plasma membrane. In microbes, the M17 LAPs have a role in proteolysis and have also acquired the ability to bind DNA. This property enables LAPs to serve as transcriptional repressors to control pyrimidine, alginate and cholera toxin biosynthesis, as well as mediate site-specific recombination events in plasmids and phages. In plants the roles of the M17 LAPs and the peptidases related to M1 LAPs are being elucidated. Roles in defense, membrane transport of auxin receptors, and meiosis have been implicated.
 ...
PMID:Leucine aminopeptidases: diversity in structure and function. 1713 98

cDNA clones corresponding to the vasotocin precursor polypeptide were isolated from a chicken hypothalamic library and sequenced. The derived amino-acid sequence indicates a precursor of comparable structural organization to that described for members of the vasotocin/vasopressin gene family from other species. Unlike in mammals the C-terminal glycopeptide moiety appears not be cleaved off from the neurophysin. Subsequent screening of a chicken genomic library permitted an analysis also of the vasotocin gene structure and exonic composition. The 5'region upstream of the first exon was sequenced and revealed an unusual pattern of 49 repetitive -YYCYCYAAAYY- motifs, together with a polyadenyl region supporting a bend in the DNA, and a long pyrimidine-rich sequence. Three AP2-like elements, identified in the mammalian vasopressin gene, were also observed in the immediate upstream region. There was no obvious homology to the promoter regions of the known oxytocin genes, nor to any other sequence deposited in available databases, nor to other known cis-elements.
 ...
PMID:The chicken vasotocin gene. 2155 35