ArticleAdvances in hematology2010
Asn and asn: critical residues for in vitro biological activity of reteplase.
Article in Advances in hematology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Study on the activity of recombinant mutant tissue-type plasminogen activator fused with the C-terminal fragment of hirudin.Journal of thrombosis and thrombolysis · 2021Article
- Reteplase Fc-fusions produced in N. benthamiana are able to dissolve blood clots ex vivo.PloS one · 2021Article
- Improving the solubility, activity, and stability of reteplase usingResearch in pharmaceutical sciences · 2019Article
- Reteplase: Structure, Function, and Production.Advanced biomedical research · 2019Review
- Improvement of Soluble Production of Reteplase inAdvanced biomedical research · 2019Article
- Evaluation of efficacy and safety of Reteplase and Alteplase in the treatment of hyper-acute cerebral infarction.Bioscience reports · 2018Article
- Molecular cloning of Reteplase and its expression in E. coli using tac promoter.Advanced biomedical research · 2014Article
- Optimization of the expression of reteplase in Escherichia coli.Research in pharmaceutical sciences · 2011Article
- Comparison of Three Escherichia coli Strains in Recombinant Production of Reteplase.Avicenna journal of medical biotechnologyArticle
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reteplase (rPA) is a thrombolytic agent used for the treatment of acute myocardial infarction. We studied the expression of rPA and its selected asparagine mutants after integration into the Pichia genome. Though methanol induction of the native and the rPA mutants showed similar expression levels (~200-250 mg/L), the mutants displayed significant loss of protease activity. Strikingly, the clot lysis activities of these mutants were considerably different. While mutation of Asn(12) (N12P) of the Kringle 2 domain showed delayed clot lysis activity (t(1/2) = 38 min) compared to the native rPA (t(1/2) = 33 min), a faster rate of clot lysis (t(1/2) = 27 min) was observed when the Asn(278) (N278S) of the serine protease domain was mutated. Interestingly, the slowest clot lysis activity (t(1/2) = 49 min) demonstrated by the double mutant (N12P, N278S) suggests the dominant role of Asn(12) in regulating the fibrinolytic activity of rPA. The results presented in this paper indicate that the fibrinolytic and the proteolytic activities of rPA are independent of each other.
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.