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Hijacking of plasminogen by dengue virus: The kringle-4 and -5 domains of plasminogen binds synergistically to the domain I of envelope protein.
Protein Sci
February 2025
Department of Biological Sciences, National University of Singapore, Singapore.
Dengue fever is a serious health issue, particularly in tropical countries like Singapore. We have previously found that dengue virus (DENV) recruits human plasmin in blood meal to enhance the permeability of the mosquito midgut for infection. Here, using biolayer interferometry, we found that neither kringle-4 nor kringle-5 plasmin domains alone binds well to dengue virus.
View Article and Find Full Text PDFStreptolysin O accelerates the conversion of plasminogen to plasmin.
Nat Commun
November 2024
Division of Infection Medicine, Department of Clinical Sciences Lund, Faculty of Medicine, Lund University, Lund, Sweden.
Group A Streptococcus (GAS) is a human-specific bacterial pathogen that can exploit the plasminogen-plasmin fibrinolysis system to dismantle blood clots and facilitate its spread and survival within the human host. In this study, we use affinity-enrichment mass spectrometry to decipher the host-pathogen protein-protein interaction between plasminogen and streptolysin O, a key cytolytic toxin produced by GAS. This interaction accelerates the conversion of plasminogen to plasmin by both the host tissue-type plasminogen activator and streptokinase, a bacterial plasminogen activator secreted by GAS.
View Article and Find Full Text PDFLeast hemolytic, 12.6 kDa, plasmin-like fibrinolytic protease from marine Penicillium steckii KU1.
Int J Biol Macromol
December 2024
Department of Biotechnology and Microbiology, Kannur University, Dr. Janaki Ammal Campus, Palayad, Thalassery, Kannur 670661, Kerala, India. Electronic address:
A novel fibrinolytic enzyme, from the marine fungus Penicillium steckii KU1, was purified to electrophoretic homogeneity. The fibrinolytic protease was purified to 13.56 times with a specific activity of 57.
View Article and Find Full Text PDFMosquito salivary apyrase regulates blood meal hemostasis and facilitates malaria parasite transmission.
Nat Commun
September 2024
Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, MD, 20852, USA.
Article Synopsis
- The evolution of blood-feeding insects, like mosquitoes, involves adaptations that help them consume blood while avoiding the host's immune responses.
- Anopheles gambiae salivary apyrase (AgApyrase) plays a key role in blood meal hemostasis by inhibiting platelet aggregation and facilitating the conversion of plasminogen to plasmin, which helps in degrading fibrin and promotes Plasmodium transmission.
- Immunizing against AgApyrase can inhibit Plasmodium infection and transmission, suggesting potential strategies for preventing malaria spread.
Lack of Interactions Between Alteplase/Tenecteplase and the Adenosine A1R/A3R Agonist AST-004.
Stroke
July 2024
Department of Cell Systems and Anatomy, University of Texas Health San Antonio (D.H., D.L., J.D.L.).
Article Synopsis
- AST-004 is a small molecule being researched as a cerebroprotectant for acute stroke, requiring evaluation of its interactions with the only current stroke treatment, tPA (alteplase).
- The study tested AST-004's stability and its effects on tPA's ability to break down clots using various in vitro methods, including assessing its performance in human blood.
- Results showed that AST-004 does not interact negatively with alteplase or tenecteplase, suggesting it can be safely administered alongside these treatments for stroke patients.
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