ArticleACS omega2025
Production of a Recombinant Fibrinolytic Protease from an Isolate of Serratia marcescens from the Amazon Basin.
Article in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intravenous fibrinolytic agents are essential for the treatment of cardiovascular diseases, acting through plasminogen activation to dissolve thrombi. However, current therapies are often limited by low fibrin specificity, high production costs, and side effects such as bleeding and allergic reactions. In this study, we describe a novel fibrinolytic protease, rSM519, derived from Serratia marcescens CBAM 519 and recombinantly expressed in Escherichia coli. The enzyme was purified via affinity chromatography and exhibited a molecular mass of 56 kDa. Biochemical assays revealed that rSM519 is a metalloprotease with optimal activity at pH 9.0 and 37 °C, significantly enhanced by Mn
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Registered trials
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