Structural and functional studies of the metalloendopeptidase (EC 3.4.24.15) involved in degrading gonadotropin releasing hormone

This publication has 11 references indexed in Scilit:

• Inhibition of endopeptidase-24.15 decreases blood pressure in normotensive rats.
  Hypertension, 1991
• Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
  Biochemistry, 1990
• Endopeptidase 24.15 from rat testes. Isolation of the enzyme and its specificity toward synthetic and natural peptides, including enkephalin-containing peptides
  Biochemical Journal, 1989
• Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning.
  Proceedings of the National Academy of Sciences, 1988
• Primary structure homologies between two zinc metallopeptidases, the neutral endopeptidase 24.11 ("enkephalinase") and thermolysin, through clustering analysis
  Biochemistry, 1988
• Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
  FEBS Letters, 1987
• Knowledge-based prediction of protein structures and the design of novel molecules
  Nature, 1987
• Structure of thermolysin refined at 1.6 Å resolution
  Journal of Molecular Biology, 1982
• Comparative model-building of the mammalian serine proteases
  Journal of Molecular Biology, 1981
• Prediction of protein conformation
  Biochemistry, 1974