ArticleThe Journal of biological chemistry2020
Identification and analyses of inhibitors targeting apolipoprotein(a) kringle domains KIV-7, KIV-10, and KV provide insight into kringle domain function.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Lipopotrein(a): from the complex metabolism to the optimal lowering drug.Internal and emergency medicine · 2026Review
- Lipoprotein(a) and cardiovascular disease.The Biochemical journal · 2024Review
- The implications of measuring lipoprotein(a) in clinical practice.Global cardiology science & practice · 2024Article
- Fragment-based drug design of novel inhibitors targeting lipoprotein (a) kringle domain KIV-10-mediated cardiovascular disease.Journal of bioenergetics and biomembranes · 2024Article
- Article
- Optimization of plasma-based BioID identifies plasminogen as a ligand of ADAMTS13.Scientific reports · 2024Article
- Crystal structure of the kringle domain of human receptor tyrosine kinase-like orphan receptor 1 (hROR1).Acta crystallographica. Section F, Structural biology communications · 2022Article
- Elevated Lipoprotein(a): Background, Current Insights and Future Potential Therapies.Vascular health and risk management · 2021Review
Corrections and comments
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Authors and funding
34 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Increased plasma concentrations of lipoprotein(a) (Lp(a)) are associated with an increased risk for cardiovascular disease. Lp(a) is composed of apolipoprotein(a) (apo(a)) covalently bound to apolipoprotein B of low-density lipoprotein (LDL). Many of apo(a)'s potential pathological properties, such as inhibition of plasmin generation, have been attributed to its main structural domains, the kringles, and have been proposed to be mediated by their lysine-binding sites. However, available small-molecule inhibitors, such as lysine analogs, bind unselectively to kringle domains and are therefore unsuitable for functional characterization of specific kringle domains. Here, we discovered small molecules that specifically bind to the apo(a) kringle domains KIV-7, KIV-10, and KV. Chemical synthesis yielded compound AZ-05, which bound to KIV-10 with a
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