ArticleScientific reports2017
Allosteric inhibition of aminopeptidase N functions related to tumor growth and virus infection.
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 21 papers.
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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.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Structure and receptor recognition of type-II feline infectious peritonitis virus spike glycoprotein.The EMBO journal · 2026Article
- Chemodiversity and Biotechnological Potential of Microginins.International journal of molecular sciences · 2025Review
- Identification ofMolecules (Basel, Switzerland) · 2025Article
- Cross-species recognition of two porcine coronaviruses to their cellular receptor aminopeptidase N of dogs and seven other species.PLoS pathogens · 2025Article
- A novel aminopeptidase N/CD13 inhibitor selectively targets an endothelial form of CD13 after coupling to proteins.Cellular and molecular life sciences : CMLS · 2024Article
- Virus-Receptor Interactions and Receptor-Mediated Virus Entry into Host Cells.Sub-cellular biochemistry · 2024Review
- Structures of a deltacoronavirus spike protein bound to porcine and human receptors.Nature communications · 2022Article
- Effect of Type 2 Diabetes and Impaired Glucose Tolerance on Digestive Enzymes and Glucose Absorption in the Small Intestine of Young Rats.Nutrients · 2022Article
- Discovery of Novel Tetrahydro-β-carboline Containing Aminopeptidase N Inhibitors as Cancer Chemosensitizers.Frontiers in oncology · 2022Article
- Fluorescent probes for visualizing ROS-associated proteins in disease.Chemical science · 2021Review
- Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021Review
- X-ray crystal structure and specificity of the Toxoplasma gondii ME49 TgAPN2.The Biochemical journal · 2020Article
- Inhibition of Porcine Aminopeptidase M (pAMP) by the Pentapeptide Microginins.Molecules (Basel, Switzerland) · 2019Article
- Phosphonic Acid Analogues of Phenylglycine as Inhibitors of Aminopeptidases: Comparison of Porcine Aminopeptidase N, Bovine Leucine Aminopeptidase, Tomato Acidic Leucine Aminopeptidase and Aminopeptidase from Barley Seeds.Pharmaceuticals (Basel, Switzerland) · 2019Article
- Aminobenzosuberone Scaffold as a Modular Chemical Tool for the Inhibition of Therapeutically Relevant M1 Aminopeptidases.Molecules (Basel, Switzerland) · 2018Article
- Characterization of the interaction between recombinant porcine aminopeptidase N and spike glycoprotein of porcine epidemic diarrhea virus.International journal of biological macromolecules · 2018Article
- Neutral metalloaminopeptidases APN and MetAP2 as newly discovered anticancer molecular targets of actinomycin D and its simple analogs.Oncotarget · 2018Article
- Broad receptor engagement of an emerging global coronavirus may potentiate its diverse cross-species transmissibility.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Molecular Imaging of Aminopeptidase N in Cancer and Angiogenesis.Contrast media & molecular imaging · 2018Review
- Receptor-binding loops in alphacoronavirus adaptation and evolution.Nature communications · 2017Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Cell surface aminopeptidase N (APN) is a membrane-bound ectoenzyme that hydrolyzes proteins and peptides and regulates numerous cell functions. APN participates in tumor cell expansion and motility, and is a target for cancer therapies. Small drugs that bind to the APN active site inhibit catalysis and suppress tumor growth. APN is also a major cell entry receptor for coronavirus, which binds to a region distant from the active site. Three crystal structures that we determined of human and pig APN ectodomains defined the dynamic conformation of the protein. These structures offered snapshots of closed, intermediate and open APN, which represent distinct functional states. Coronavirus envelope proteins specifically recognized the open APN form, prevented ectodomain progression to the closed form and substrate hydrolysis. In addition, drugs that bind the active site inhibited both coronavirus binding to cell surface APN and infection; the drugs probably hindered APN transition to the virus-specific open form. We conclude that allosteric inhibition of APN functions occurs by ligand suppression of ectodomain motions necessary for catalysis and virus cell entry, as validated by locking APN with disulfides. Blocking APN dynamics can thus be a valuable approach to development of drugs that target this ectoenzyme.
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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.