ArticleScientific reports2017
The Rational Design of Therapeutic Peptides for Aminopeptidase N using a Substrate-Based Approach.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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.
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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.
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Who cites it
20 citing papers in PubMed, 47 citations in OpenAlex.
- Oral peptide drug delivery: design of SEDDS providing a protective effect against intestinal membrane-bound enzymes.Drug delivery and translational research · 2026Article
- Quantum Mechanics/Molecular Mechanics Simulations Distinguish Insulin-Regulated Aminopeptidase Substrate (Oxytocin) and Inhibitor (Angiotensin IV) and Reveal Determinants of Activity and Inhibition.Journal of chemical information and modeling · 2025Article
- A Novel Workflow for In Silico Prediction of Bioactive Peptides: An Exploration ofBiomolecules · 2024Article
- Peptide discovery across the spectrum of neuroinflammation; microglia and astrocyte phenotypical targeting, mediation, and mechanistic understanding.Frontiers in molecular neuroscience · 2024Review
- Multiplex substrate profiling by mass spectrometry for proteases.Methods in enzymology · 2023Article
- Aminopeptidase N Inhibitors as Pointers for Overcoming Antitumor Treatment Resistance.International journal of molecular sciences · 2022Article
- ERAP1 binds peptide C-termini of different sequences and/or lengths by a common recognition mechanism.Immunobiology · 2021Article
- Investigating the phosphinic acid tripeptide mimetic DG013A as a tool compound inhibitor of the M1-aminopeptidase ERAP1.Bioorganic & medicinal chemistry letters · 2021Article
- Gut Digestive Function and Microbiome after Correction of Experimental Dysbiosis in Rats by Indigenous Bifidobacteria.Microorganisms · 2021Article
- Article
- New insights into application of nanoparticles in the diagnosis and screening of novel coronavirus (SARS-CoV-2).Emergent materials · 2021Review
- IRAP Inhibitors: M1-Aminopeptidase Family Inspiration.Frontiers in pharmacology · 2020Review
- Quantitative Multiplex Substrate Profiling of Peptidases by Mass Spectrometry.Molecular & cellular proteomics : MCP · 2019Article
- Peptides as Therapeutic Agents for Inflammatory-Related Diseases.International journal of molecular sciences · 2018Review
- Neutral metalloaminopeptidases APN and MetAP2 as newly discovered anticancer molecular targets of actinomycin D and its simple analogs.Oncotarget · 2018Article
- Current state of in vivo panning technologies: Designing specificity and affinity into the future of drug targeting.Advanced drug delivery reviews · 2018Review
- Global substrate specificity profiling of post-translational modifying enzymes.Protein science : a publication of the Protein Society · 2018Review
- Molecular Imaging of Aminopeptidase N in Cancer and Angiogenesis.Contrast media & molecular imaging · 2018Review
- Distinct Epitopes on CD13 Mediate Opposite Consequences for Cell Adhesion.BioMed research international · 2018Article
- In vitro methods for testing antiviral drugs.Biotechnology advancesReview
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
The M1 family of metalloproteases represents a large number of exopeptidases that cleave single amino acid residues from the N-terminus of peptide substrates. One member of this family that has been well studied is aminopeptidase N (APN), a multifunctional protease known to cleave biologically active peptides and aide in coronavirus entry. The proteolytic activity of APN promotes cancer angiogenesis and metastasis making it an important target for cancer therapy. To understand the substrate specificity of APN for the development of targeted inhibitors, we used a global substrate profiling method to determine the P1-P4' amino acid preferences. The key structural features of the APN pharmacophore required for substrate recognition were elucidated by x-ray crystallography. By combining these substrate profiling and structural data, we were able to design a selective peptide inhibitor of APN that was an effective therapeutic both in vitro and in vivo against APN-expressing prostate cancer models.
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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.