ArticleJournal of structural biology2019
Solution structural model of the complex of the binding regions of human plasminogen with its M-protein receptor from Streptococcus pyogenes.
Article in Journal of structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 6 citations in OpenAlex.
- Structural basis for collagen recognition by theeLife · 2025Article
- Hydrophobic residues in the D-domain of a plasminogen-binding M-protein modulate α-helicity, oligomerization, and surface anchoring in Streptococcus pyogenes.Protein science : a publication of the Protein Society · 2025Article
- Inactivation of the lysine binding sites of human plasminogen (hPg) reveals novel structural requirements for the tight hPg conformation, M-protein binding, and rapid activation.Frontiers in molecular biosciences · 2023Article
- Crystal structure of the kringle domain of human receptor tyrosine kinase-like orphan receptor 1 (hROR1).Acta crystallographica. Section F, Structural biology communications · 2022Article
- Binding of the kringle-2 domain of human plasminogen to streptococcal PAM-type M-protein causes dissociation of PAM dimers.MicrobiologyOpen · 2021Article
- A local α-helix drives structural evolution of streptococcal M-protein affinity for host human plasminogen.The Biochemical journal · 2020Article
- The M Protein of Streptococcus pyogenes Strain AP53 Retains Cell Surface Functional Plasminogen Binding after Inactivation of the Sortase A Gene.Journal of bacteriology · 2020Article
- Streptococcus co-opts a conformational lock in human plasminogen to facilitate streptokinase cleavage and bacterial virulence.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
Abstract
VEK50 is a truncated peptide from a Streptococcal pyogenes surface human plasminogen (hPg) binding M-protein (PAM). VEK50 contains the full A-domain of PAM, which is responsible for its low nanomolar binding to hPg. The interaction of VEK50 with kringle 2, the PAM-binding domain in hPg (K2
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Registered trials
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