BIOMAT Database Logo BIOMAT Database Logo

Inhibitors of renin as potential therapeutic agents. 1987

J M Wood, and J L Stanton, and K G Hofbauer
Research Department, CIBA-GEIGY Limited, Basle, Switzerland.

UI MeSH Term Description Entries
D006973 Hypertension Persistently high systemic arterial BLOOD PRESSURE. Based on multiple readings (BLOOD PRESSURE DETERMINATION), hypertension is currently defined as when SYSTOLIC PRESSURE is consistently greater than 140 mm Hg or when DIASTOLIC PRESSURE is consistently 90 mm Hg or more. Blood Pressure, High,Blood Pressures, High,High Blood Pressure,High Blood Pressures
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009842 Oligopeptides Peptides composed of between two and twelve amino acids. Oligopeptide
D012083 Renin A highly specific (Leu-Leu) endopeptidase that generates ANGIOTENSIN I from its precursor ANGIOTENSINOGEN, leading to a cascade of reactions which elevate BLOOD PRESSURE and increase sodium retention by the kidney in the RENIN-ANGIOTENSIN SYSTEM. The enzyme was formerly listed as EC 3.4.99.19. Angiotensin-Forming Enzyme,Angiotensinogenase,Big Renin,Cryorenin,Inactive Renin,Pre-Prorenin,Preprorenin,Prorenin,Angiotensin Forming Enzyme,Pre Prorenin,Renin, Big,Renin, Inactive
D012084 Renin-Angiotensin System A BLOOD PRESSURE regulating system of interacting components that include RENIN; ANGIOTENSINOGEN; ANGIOTENSIN CONVERTING ENZYME; ANGIOTENSIN I; ANGIOTENSIN II; and angiotensinase. Renin, an enzyme produced in the kidney, acts on angiotensinogen, an alpha-2 globulin produced by the liver, forming ANGIOTENSIN I. Angiotensin-converting enzyme, contained in the lung, acts on angiotensin I in the plasma converting it to ANGIOTENSIN II, an extremely powerful vasoconstrictor. Angiotensin II causes contraction of the arteriolar and renal VASCULAR SMOOTH MUSCLE, leading to retention of salt and water in the KIDNEY and increased arterial blood pressure. In addition, angiotensin II stimulates the release of ALDOSTERONE from the ADRENAL CORTEX, which in turn also increases salt and water retention in the kidney. Angiotensin-converting enzyme also breaks down BRADYKININ, a powerful vasodilator and component of the KALLIKREIN-KININ SYSTEM. Renin-Angiotensin-Aldosterone System,Renin Angiotensin Aldosterone System,Renin Angiotensin System,System, Renin-Angiotensin,System, Renin-Angiotensin-Aldosterone
D006333 Heart Failure A heterogeneous condition in which the heart is unable to pump out sufficient blood to meet the metabolic need of the body. Heart failure can be caused by structural defects, functional abnormalities (VENTRICULAR DYSFUNCTION), or a sudden overload beyond its capacity. Chronic heart failure is more common than acute heart failure which results from sudden insult to cardiac function, such as MYOCARDIAL INFARCTION. Cardiac Failure,Heart Decompensation,Congestive Heart Failure,Heart Failure, Congestive,Heart Failure, Left-Sided,Heart Failure, Right-Sided,Left-Sided Heart Failure,Myocardial Failure,Right-Sided Heart Failure,Decompensation, Heart,Heart Failure, Left Sided,Heart Failure, Right Sided,Left Sided Heart Failure,Right Sided Heart Failure
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities

Related Publications

J M Wood, and J L Stanton, and K G Hofbauer
[Oral inhibitors of renin and their potential use as therapeutic agents in treating hypertension].
June 2008, Harefuah,
J M Wood, and J L Stanton, and K G Hofbauer
Telomerase inhibitors--oligonucleotide phosphoramidates as potential therapeutic agents.
January 2001, Nucleosides, nucleotides & nucleic acids,
J M Wood, and J L Stanton, and K G Hofbauer
Protease inhibitors as potential therapeutic agents for AIDS.
September 1991, Annals of Saudi medicine,
J M Wood, and J L Stanton, and K G Hofbauer
Inhibitors of enkephalin-degrading enzymes as potential therapeutic agents.
January 1993, Progress in medicinal chemistry,
J M Wood, and J L Stanton, and K G Hofbauer
Renin inhibitors as possible antihypertensive agents.
September 1988, Klinische Wochenschrift,
J M Wood, and J L Stanton, and K G Hofbauer
Direct renin inhibitors as antihypertensive agents.
January 2010, American journal of therapeutics,
J M Wood, and J L Stanton, and K G Hofbauer
SRC inhibitors as potential therapeutic agents for human cancers.
June 2006, Mini reviews in medicinal chemistry,
J M Wood, and J L Stanton, and K G Hofbauer
Recent advances in ATM inhibitors as potential therapeutic agents.
December 2022, Future medicinal chemistry,
J M Wood, and J L Stanton, and K G Hofbauer
Selective cyclic nucleotide phosphodiesterase inhibitors as potential therapeutic agents.
January 1977, Annual review of pharmacology and toxicology,
J M Wood, and J L Stanton, and K G Hofbauer
Potential of mTOR inhibitors as therapeutic agents in hematological malignancies.
August 2009, Expert review of hematology,
Copied contents to your clipboard!