ArticleJournal of neural transmission (Vienna, Austria : 1996)2013
Structural comparison of the active site channels in rodent and primate vascular adhesion protein-1.
Article in Journal of neural transmission (Vienna, Austria : 1996), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
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
6 citing papers in PubMed.
- Exploring the Binding Specificity of Siglec-Derived Peptides to Human Primary Amine Oxidase Using an Integrative Approach to Ligand Epitope Mapping.Computational and structural biotechnology journal · 2026Article
- The role of VAP-1 in cardiovascular disease: a review.Frontiers in cardiovascular medicine · 2025Review
- Human Copper-Containing Amine Oxidases in Drug Design and Development.Molecules (Basel, Switzerland) · 2020Review
- Comparison of Inhibitor and Substrate Selectivity between Rodent and Human Vascular Adhesion Protein-1.Mediators of inflammation · 2020Article
- Mapping the interaction site and effect of the Siglec-9 inflammatory biomarker on human primary amine oxidase.Scientific reports · 2018Article
- Novel pyridazinone inhibitors for vascular adhesion protein-1 (VAP-1): old target-new inhibition mode.Journal of medicinal chemistry · 2013Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, we have made homology models of mouse, rat, and monkey vascular adhesion protein-1 (VAP-1) to reveal basis for the species-specific ligand recognition of VAP-1. Based on the structural comparisons, rodent VAP-1s have a narrower active site channel than primate VAP-1s. The variable residues in mouse and rat VAP-1, Phe447 from arm I and the polar residues from the first α-helix of the D3 domain together with C-terminal residues are likely to affect ligand recognition and binding.
Indexed as
Identifiers
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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.