Year |
Citation |
Score |
1999 |
Cushman DW, Ondetti MA. Design of angiotensin converting enzyme inhibitors. Nature Medicine. 5: 1110-3. PMID 10502801 DOI: 10.1038/13423 |
0.788 |
|
1991 |
Cushman DW, Ondetti MA. History of the design of captopril and related inhibitors of angiotensin converting enzyme. Hypertension. 17: 589-92. PMID 2013486 |
0.772 |
|
1991 |
Ondetti MA. Angiotensin converting enzyme inhibitors. An overview. Hypertension. 18: III134-5. PMID 1937676 |
0.566 |
|
1988 |
Ondetti MA. Structural relationships of angiotensin converting-enzyme inhibitors to pharmacologic activity. Circulation. 77: I74-8. PMID 2836111 |
0.501 |
|
1987 |
Petrillo EW, Powell JR, Cushman DW, Ondetti MA. Angiotensin-converting enzyme inhibitors: accomplishments and challenges. Clinical and Experimental Hypertension. Part a, Theory and Practice. 9: 235-41. PMID 3038385 DOI: 10.3109/10641968709164183 |
0.785 |
|
1987 |
Cushman DW, Ondetti MA, Gordon EM, Natarajan S, Karanewsky DS, Krapcho J, Petrillo EW. Rational design and biochemical utility of specific inhibitors of angiotensin-converting enzyme. Journal of Cardiovascular Pharmacology. 10: S17-30. PMID 2485059 |
0.766 |
|
1984 |
Ondetti MA, Cushman DW. Angiotensin-converting enzyme inhibitors: biochemical properties and biological actions. Crc Critical Reviews in Biochemistry. 16: 381-411. PMID 6094098 |
0.761 |
|
1983 |
Ondetti MA. Biochemistry of the renin-angiotensin system. Introduction. Federation Proceedings. 42: 2722-3. PMID 6305730 |
0.348 |
|
1982 |
Ondetti MA, Cushman DW. Enzymes of the renin-angiotensin system and their inhibitors. Annual Review of Biochemistry. 51: 283-308. PMID 6287916 DOI: 10.1146/Annurev.Bi.51.070182.001435 |
0.795 |
|
1982 |
Petrillo EW, Ondetti MA. Angiotensin-converting enzyme inhibitors: medicinal chemistry and biological actions. Medicinal Research Reviews. 2: 1-41. PMID 6287131 DOI: 10.1002/Med.2610020103 |
0.587 |
|
1982 |
Condon ME, Petrillo EW, Ryono DE, Reid JA, Neubeck R, Puar M, Heikes JE, Sabo EF, Losee KA, Cushman DW, Ondetti MA. Angiotensin-converting enzyme inhibitors: importance of the amide carbonyl of mercaptoacyl amino acids for hydrogen bonding to the enzyme. Journal of Medicinal Chemistry. 25: 250-8. PMID 6279843 DOI: 10.1002/Chin.198233150 |
0.731 |
|
1982 |
Cushman DW, Cheung HS, Sabo EF, Ondetti MA. Development and design of specific inhibitors of angiotensin-converting enzyme. The American Journal of Cardiology. 49: 1390-4. PMID 6176105 DOI: 10.1016/0002-9149(82)90348-4 |
0.801 |
|
1981 |
Georgopapadakou NH, Liu FY, Ryono DE, Neubeck R, Ondetti MA. Chemical modifications of the active site of Streptomyces R61 DD-carboxypeptidase. European Journal of Biochemistry / Febs. 115: 53-7. PMID 7227371 DOI: 10.1111/J.1432-1033.1981.Tb06196.X |
0.429 |
|
1981 |
Ondetti MA, Cushman DW. Design of protease inhibitors. Biopolymers. 20: 2001-10. PMID 6272900 DOI: 10.1002/Bip.1981.360200922 |
0.715 |
|
1981 |
Ondetti MA, Cushman DW. Inhibition of the renin-angiotensin system. A new approach to the therapy of hypertension. Journal of Medicinal Chemistry. 24: 355-61. PMID 6267277 DOI: 10.1002/Chin.198134344 |
0.679 |
|
1981 |
Gordon EM, Pluščec J, Ondetti MA. Carbacyclic isosteres of penicillanic and carbapenemic acids. Synthesis of bicyclo[3.2.0]Heptan-6-ones as potential enzyme inhibitors. Tetrahedron Letters. 22: 1871-1874. DOI: 10.1016/S0040-4039(01)90464-2 |
0.501 |
|
1980 |
Cushman DW, Ondetti MA. Inhibitors of angiotensin-converting enzyme. Progress in Medicinal Chemistry. 17: 41-104. PMID 6273970 DOI: 10.1016/S0079-6468(08)70157-7 |
0.78 |
|
1980 |
Cushman DW, Ondetti MA, Cheung HS, Antonaccio MJ, Murthy VS, Rubin B. Inhibitors of angiotensin-converting enzyme. Advances in Experimental Medicine and Biology. 130: 199-225. PMID 6250340 DOI: 10.1007/978-1-4615-9173-3_8 |
0.787 |
|
1980 |
Cushman DW, Ondetti MA. Inhibitors of angiotensin-converting enzyme for treatment of hypertension. Biochemical Pharmacology. 29: 1871-7. PMID 6249323 DOI: 10.1016/0006-2952(80)90096-9 |
0.774 |
|
1980 |
Cheung HS, Wang FL, Ondetti MA, Sabo EF, Cushman DW. Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence. The Journal of Biological Chemistry. 255: 401-7. PMID 6243277 |
0.743 |
|
1980 |
Cushman DW, Ondetti MA. Control of blood pressure by angiotensin blockade Trends in Pharmacological Sciences. 1: 260-263. DOI: 10.1016/0165-6147(80)90015-2 |
0.635 |
|
1979 |
Ondetti MA, Condon ME, Reid J, Sabo EF, Cheung HS, Cushman DW. Design of potent and specific inhibitors of carboxypeptidases A and B. Biochemistry. 18: 1427-30. PMID 427123 DOI: 10.1021/Bi00575A006 |
0.713 |
|
1979 |
Cushman DW, Cheung HS, Sabo EF, Rubin B, Ondetti MA. Development of specific inhibitors of angiotensin I converting enzyme (kininase II). Federation Proceedings. 38: 2778-82. PMID 228989 |
0.77 |
|
1978 |
Cushman DW, Cheung HS, Sabo EF, Ondetti MA. Design of new antihypertensive drugs: potent and specific inhibitors of angiotensin-converting enzyme. Progress in Cardiovascular Diseases. 21: 176-82. PMID 214817 DOI: 10.1016/0033-0620(78)90023-3 |
0.788 |
|
1978 |
Ondetti MA, Cushman DW. Chapter 9. Inhibitors of the Renin-Angiotensin System Annual Reports in Medicinal Chemistry. 13: 82-91. DOI: 10.1016/S0065-7743(08)60612-0 |
0.742 |
|
1978 |
Cushman DW, Ondetti MA, Cheung HS. Substrate and inhibitor binding to angiotensin-converting enzyme (ACE): role of the C-terminal dipeptide sequence Federation Proceedings. 37: No. 2340. |
0.752 |
|
1977 |
Cushman DW, Cheung HS, Sabo EF, Ondetti MA. Design of potent competitive inhibitors of angiotensin-converting enzyme. Carboxyalkanoyl and mercaptoalkanoyl amino acids. Biochemistry. 16: 5484-91. PMID 200262 DOI: 10.1021/Bi00644A014 |
0.765 |
|
1977 |
Ondetti MA, Rubin B, Cushman DW. Design of specific inhibitors of angiotensin-converting enzyme: new class of orally active antihypertensive agents. Science (New York, N.Y.). 196: 441-4. PMID 191908 DOI: 10.1126/Science.191908 |
0.776 |
|
1977 |
Cushman DW, Cheung HS, Ondetti MA. Design of active site-specific inhibitors of angiotensin-converting enzyme (ACE) Federation Proceedings. 36: No. 4088. |
0.767 |
|
1973 |
Cushman DW, Pluscec J, Williams NJ, Weaver ER, Sabo EF, Kocy O, Cheung HS, Ondetti MA. Inhibition of angiotensin-coverting enzyme by analogs of peptides from Bothrops jararaca venom. Experientia. 29: 1032-5. PMID 4354751 DOI: 10.1007/Bf01930447 |
0.719 |
|
1972 |
Ondetti MA, Pluscec J, Sabo EF, Williams NJ, Weaver ER, Kocy O. Peptidic inhibitors of the angiotensin-converting enzyme. Medicina. 32: Suppl 1:9-14. PMID 4342069 |
0.501 |
|
1971 |
Ondetti MA, Williams NJ, Sabo EF, Pluscec J, Weaver ER, Kocy O. Angiotensin-converting enzyme inhibitors from the venom of Bothrops jararaca. Isolation, elucidation of structure, and synthesis. Biochemistry. 10: 4033-9. PMID 4334402 DOI: 10.1021/Bi00798A004 |
0.571 |
|
1963 |
Bodanszky M, Sheehan JT, Ondetti MA, Lande S. Glycine analogs of bradykinin Journal of the American Chemical Society. 85: 991-997. DOI: 10.1021/Ja00890A036 |
0.362 |
|
1962 |
Gros EG, Ondetti MA, Sproviero JO, Deulofeu V, Deferrari JO. Reaction of ammonia with some acetylated and benzoylated monosaccharides. VII. Migration of different benzoyl groups in the ammonolysis of penta-O-benzoyl-D-glucoses Journal of Organic Chemistry. 27: 924-929. DOI: 10.1021/Jo01050A057 |
0.469 |
|
1961 |
Ondetti MA, Deulofeu V. The structure of olivacine and u-alkaloid C (Guatambuine) Tetrahedron. 15: 160-166. DOI: 10.1016/0040-4020(61)80020-3 |
0.479 |
|
1960 |
Ondetti MA, Deulofeu V. Alkaloids from aspidosperma australe müll. Argov. (note II). The structure of olivacine and U-alkaloid C (guatambuine) Tetrahedron Letters. 1: 18-22. |
0.514 |
|
1959 |
Deferrari JO, Ondetti MA, Deulofeu V. Reaction of ammonia with some acetylated and benzoylated monosaccharides. VI. Derivatives of L-arabinose, D-xylose, and D-ribose Journal of Organic Chemistry. 24: 183-186. DOI: 10.1021/Jo01084A009 |
0.483 |
|
1959 |
Ondetti MA, Deulofeu V. Alkaloids from aspidosperma australe müll. argov. relationship of olivacine to u-alkaloid C Tetrahedron Letters. 1: 1-4. |
0.473 |
|
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