ArticleThe FEBS journal2018
Crystal structures of sampatrilat and sampatrilat-Asp in complex with human ACE - a molecular basis for domain selectivity.
Article in The FEBS journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 34 citations in OpenAlex.
- Molecular basis of domain-specific angiotensin I-converting enzyme inhibition by the antihypertensive drugs enalaprilat, ramiprilat, trandolaprilat, quinaprilat and perindoprilat.The FEBS journal · 2026Article
- Ciprofloxacin Inhibits Angiotensin I‑Converting Enzyme (ACE) Activity by Binding at the Exosite, Distal to the Catalytic Pocket.ACS bio & med chem Au · 2025Article
- Metabolites Isolated fromInternational journal of molecular sciences · 2025Article
- Molecular Basis of Dipeptide Recognition inBiomolecules · 2025Article
- Design of Novel Mercapto-3-phenylpropanoyl Dipeptides as Dual Angiotensin-Converting Enzyme C-Domain-Selective/Neprilysin Inhibitors.Journal of medicinal chemistry · 2025Article
- Molecular basis of human angiotensin-1 converting enzyme inhibition by a series of diprolyl-derived compounds.The FEBS journal · 2025Article
- Deep learning-based discovery of compounds for blood pressure lowering effects.Scientific reports · 2025Article
- Advances in the structural basis for angiotensin-1 converting enzyme (ACE) inhibitors.Bioscience reports · 2024Review
- Multi-Target In-Silico modeling strategies to discover novel angiotensin converting enzyme and neprilysin dual inhibitors.Scientific reports · 2024Article
- Structural insights into the inhibitory mechanism of angiotensin-I-converting enzyme by the lactotripeptides IPP and VPP.FEBS letters · 2024Article
- Article
- Structural basis for the inhibition of human angiotensin-1 converting enzyme by fosinoprilat.The FEBS journal · 2022Article
- Angiotensin-converting enzyme inhibitory peptides and isoflavonoids from soybean [Frontiers in nutrition · 2022Article
- Small molecule angiotensin converting enzyme inhibitors: A medicinal chemistry perspective.Frontiers in pharmacology · 2022Review
- Angiotensin-converting enzyme open for business: structural insights into the subdomain dynamics.The FEBS journal · 2021Article
- ACE2 and ACE: structure-based insights into mechanism, regulation and receptor recognition by SARS-CoV.Clinical science (London, England : 1979) · 2020Review
- Molecular Basis for Omapatrilat and Sampatrilat Binding to Neprilysin-Implications for Dual Inhibitor Design with Angiotensin-Converting Enzyme.Journal of medicinal chemistry · 2020Article
- ACE-domain selectivity extends beyond direct interacting residues at the active site.The Biochemical journal · 2020Article
- Whey-Derived Peptides Interactions with ACE by Molecular Docking as a Potential Predictive Tool of Natural ACE Inhibitors.International journal of molecular sciences · 2020Article
- Structural characterization and in-silico analysis of Momordica charantia 7S globulin for stability and ACE inhibition.Scientific reports · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Angiotensin-1-converting enzyme (ACE) is a zinc metallopeptidase that consists of two homologous catalytic domains (known as nACE and cACE) with different substrate specificities. Based on kinetic studies it was previously reported that sampatrilat, a tight-binding inhibitor of ACE, K DATABASE: The atomic coordinates and structure factors for N- and C-domains of ACE bound to sampatrilat and sampatrilat-Asp complexes (6F9V, 6F9R, 6F9T and 6F9U respectively) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.