References
- Jacob H J, Lindpaintner K, Lincoln S E, et al. Genetic mapping of a gene causing hypertension in the stroke-prone spontaneously hypertensive rat. Cell 1991; 67: 213–24
- Hubert P, Lindpaintner K, Beckmann J S, et al. Chromosomal mapping of two genetic loci associated with blood-pressure regulation in hereditary hypertensive rats. Nature 1991; 353: 521–9
- Wilkes B M. Molecular actions of angiotensin in the kidney. Contemporary Issues in nephrology, S Goldfarb, F N Ziyadeh, J H Stein. Churchill Livingstone, New York 1991; Vol 23: 141–60
- Tigerstedt R, Bergman P G. Niere und Kreislauf. Scand Arch Physiol 1898; 8: 223
- Goldblatt H, Lynch J, Hanzal R F, Summerville W W. Studies on experimental hypertension. I. The production of persistent elevation of systolic blood pressure by means of renal ischemia. J Exp Med 1934; 59: 347–80
- Page I H, Helmer O M. A crystalline pressor substance (angiotonin) resulting from the reaction between renin and renin activator. J Exp Med 1940; 71: 29–42
- Bumpus F M, Green A A, Page I H. Purification of angiotonin. J Biol Chem 1954; 210: 287–94
- Skeggs L T, Marsh W H, Kahn J R, Shumway N P. The existence of two forms of hypertension. J Exp Med 1954; 99: 275–82
- Dzau V J. Cardiac renin-angiotensin system: molecular and functional aspects. Am J Med 1988; 84(3A)22–7
- Ondetti M A, Rubin B, Cushman D W. Design of specific inhibitors of angiotensin-converting enzyme. New class of orally active antihypertensive agents. Science 1977; 196: 441–4
- Patchett A A, Cordes E H. The design and properties of N-carboxyalkyldipeptide inhibitors of angiotensin converting enzyme. Adv Enzymol 1985; 57: 1–84
- Case D B, Wallace J M, Keim H J, et al. Estimating renin participation in hypertension. Superiority of converting enzyme inhibitor over saralasin. Am J Med 1976; 61: 790–6
- Bernstein K E, Martin B M, Striker L, Striker G. Partial protein sequence of mouse and bovine kidney angiotensin converting enzyme. Kidney Int 1988; 33: 652–5
- Bernstein K E, Martin B M, Edwards A S, Bernstein E A. Mouse angiotensin-converting enzyme is a protein composed of two homologous domains. J Biol Chem 1989; 264: 11945–51
- Wei L, Alhenc-Gelas F, Corvol P, Clauser E. The two homologous domains of human angiotensin 1-converting enzyme are both catalytic active. J Biol Chem 1991; 266: 9002–8
- Soubrier F, Alhenc-Gelas F, Hubert C, et al. Two putative active centers in human angiotensin 1-converting enzyme revealed by molecular cloning. Proc Natl Acad Sci USA 1988; 85: 9386–90
- Shai S-Y, Langford K G, Martin B M, Bernstein K E. Genomic DNA 5′ to the mouse and human angiotensin-converting enzyme genes contains two distinct regions of conserved sequence. Biochem Biophys Res Commun 1990; 167: 1128–33
- Howard T E, Shai S-Y, Langford K G, Martin B M, Bernstein K E. Transcription of testicular angiotensin-converting enzyme (ACE) is initiated within the 12th intron of somatic ACE gene. Mol Cell Biol 1990; 10: 4294–4302
- Langford K G, Shai S-Y, Howard T E, Kovac M J, Overbeek P A, Bernstein K E. Transgenic mice demonstrate a testis specific promoter for angiotensin converting enzyme (ACE). J Biol Chem 1991; 266: 15559–62
- Timmermans P BMWM, Wong P C, Chiu A T, Herblin W F. Nonpeptide angiotensin II receptor antagonists. TIPS 1991; 12: 55–62
- Blankley C J, Hodges J C, Kely J S, Klutchko S R, European Patent No. 0 245 637, 1988
- Wong P C, Hart S D, Zaspel A M, et al. Functional studies of nonpeptidic angiotensin II receptor subtype-specific ligands: DuP753 (AII-1) and PD123177 (AII-2). J Pharmacol Exp Ther 1990; 255: 584–92
- Dudley D T, Panek R L, Major T C, et al. Subclasses of angiotensin II binding sites and their functional significance. Mol Pharmacol 1990; 38: 370–7
- Murphy T J, Alexander R W, Griedling K K, Runge M S, Bernstein K E. Isolation of a cDNA encoding the vasculartype-1 angiotensin II receptor. Nature 1991; 351: 233–6
- Seed B, Aruffo A. Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure. Proc Natl Acad Sci USA 1987; 84: 3365–9