Results 271 to 280 of about 3,459,561 (335)
Lancet, The, 2017 Summary: The magnitude of the clinical benefits produced by inhibitors of the renin-angiotensin system in heart failure has been modest, possibly because of the ability of renin-angiotensin activity to escape from suppression during long-term treatment.
Milton Packer, John J V Mcmurray
exaly +3 more sources
Journal of Molecular Graphics and Modelling, 2010 In this study, an attempt was made to explore a possible correlation between different docking scoring functions (Glide InducedFit docking score and GOLD’s GoldScore and ChemScore) and binding energy values of a set of renin inhibitors, using linear ...
Serdar Durdagi +2 more
exaly +4 more sources
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Lancet, The, 2006
Use of drugs that inhibit the renin-angiotensin system is an effective way to intervene in the pathogenesis of cardiovascular and renal disorders. The idea of blocking the renin system at its origin by inhibition of renin has existed for more than 30 years. Renin inhibition suppresses the generation of the active peptide angiotensin II.
Jan A Staessen, Tom Richart
exaly +3 more sources
Use of drugs that inhibit the renin-angiotensin system is an effective way to intervene in the pathogenesis of cardiovascular and renal disorders. The idea of blocking the renin system at its origin by inhibition of renin has existed for more than 30 years. Renin inhibition suppresses the generation of the active peptide angiotensin II.
Jan A Staessen, Tom Richart
exaly +3 more sources
Application of 3D QSAR CoMFA/CoMSIA and in silico docking studies on novel renin inhibitors against cardiovascular diseases [PDF]
European Journal of Medicinal Chemistry, 2009 For the first time, a set of renin inhibitors were subjected to the 3D QSAR/CoMFA and CoMSIA studies. The utility of renin inhibitors in the treatment of cardiovascular diseases has not been fully explored yet.
Serdar Durdagi +2 more
exaly +3 more sources
Clinical and Experimental Hypertension, 1983
Three experiments are described using new substrate analogue inhibitors of renin. The first experiment shows that introduction of a reduced isostere in the scissile peptide bond of an analogue greatly increases its ability to inhibit renin of a particular species.
B Leckie, M Szelke, A Hallett
exaly +3 more sources
Three experiments are described using new substrate analogue inhibitors of renin. The first experiment shows that introduction of a reduced isostere in the scissile peptide bond of an analogue greatly increases its ability to inhibit renin of a particular species.
B Leckie, M Szelke, A Hallett
exaly +3 more sources
Pharmaceutical Research, 1987
Since the early 1980s, an intensive effort has been focused on the development of orally effective and long-acting inhibitors of renin. During this time, in vitro potency has increased greatly, with several transition-state inhibitor designs yielding inhibitors with subnanomolar IC50 values.
E, Haber +3 more
openaire +5 more sources
Since the early 1980s, an intensive effort has been focused on the development of orally effective and long-acting inhibitors of renin. During this time, in vitro potency has increased greatly, with several transition-state inhibitor designs yielding inhibitors with subnanomolar IC50 values.
E, Haber +3 more
openaire +5 more sources
Design and optimization of new piperidines as renin inhibitors
Bioorganic and Medicinal Chemistry Letters, 2010Olivier Corminboeuf +2 more
exaly +2 more sources
[From the renin gene to renin inhibitors].
Annales d'endocrinologie, 1986The only known action of renin is the hydrolysis of angiotensinogen into angiotensin I. Renin is synthesized as an inactive precursor, preprorenin. The processing of prorenin into active renin occurs after the clivage of a profragment, just after a dibasic pair of amino-acids.
P, Corvol, J, Ménard
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Is Angiotensinogen a Renin Inhibitor and Not the Substrate for Renin?
Journal of Hypertension, 1986The cleavage of the angiotensinogen molecule by renin is slow. The rate constant for cleavage of the enzyme-substrate complex, Kcat (turnover number) is lower than usual for enzymes (0.6/s for the homologous human renin reactions and 0.15/s for the homologous mouse renin reaction).
K, Poulsen, J, Jacobsen
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