Therapeutic SERPINs: Improving on Nature [PDF]
Frontiers in Cardiovascular Medicine, 2021 Serine proteases drive important physiological processes such as coagulation, fibrinolysis, inflammation and angiogenesis. These proteases are controlled by serine protease inhibitors (SERPINs) that neutralize their activity.
Coen Maas, Steven de Maat
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Identification and analysis of serpin-family genes by homology and synteny across the 12 sequenced Drosophilid genomes [PDF]
BMC Genomics, 2009 Background The Drosophila melanogaster genome contains 29 serpin genes, 12 as single transcripts and 17 within 6 gene clusters. Many of these serpins have a conserved "hinge" motif characteristic of active proteinase inhibitors.
Micklem Gos +4 more
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Bayesian phylogeny analysis of vertebrate serpins illustrates evolutionary conservation of the intron and indels based six groups classification system from lampreys for ∼500 MY [PDF]
PeerJ, 2015 The serpin superfamily is characterized by proteins that fold into a conserved tertiary structure and exploits a sophisticated and irreversible suicide-mechanism of inhibition.
Abhishek Kumar
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SERPINs—From Trap to Treatment [PDF]
Frontiers in Medicine, 2019 Excessive enzyme activity often has pathological consequences. This for example is the case in thrombosis and hereditary angioedema, where serine proteases of the coagulation system and kallikrein-kinin system are excessively active. Serine proteases are
Wariya Sanrattana +2 more
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Anticoagulant SERPINs: Endogenous Regulators of Hemostasis and Thrombosis
Frontiers in Cardiovascular Medicine, 2022 Appropriate activation of coagulation requires a balance between procoagulant and anticoagulant proteins in blood. Loss in this balance leads to hemorrhage and thrombosis.
Steven P. Grover, Nigel Mackman
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Analysis of AlphaFold and molecular dynamics structure predictions of mutations in serpins. [PDF]
PLoS ONE, 2023 Serine protease inhibitors (serpins) include thousands of structurally conserved proteins playing key roles in many organisms. Mutations affecting serpins may disturb their conformation, leading to inactive forms.
Pedro Garrido-Rodríguez +8 more
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“Super” SERPINs—A stabilizing force against fibrinolysis in thromboinflammatory conditions
Frontiers in Cardiovascular Medicine, 2023 The superfamily of serine protease inhibitors (SERPINs) are a class of inhibitors that utilise a dynamic conformational change to trap and inhibit their target enzymes.
Steven J. Humphreys +2 more
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Viral SERPINS—A Family of Highly Potent Immune-Modulating Therapeutic Proteins
Biomolecules, 2023 Serine protease inhibitors, SERPINS, are a highly conserved family of proteins that regulate serine proteases in the central coagulation and immune pathways, representing 2–10% of circulating proteins in the blood.
Kyle Varkoly +5 more
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Plant Serpins: Potential Inhibitors of Serine and Cysteine Proteases with Multiple Functions
Plants, 2023 Plant serpins are a superfamily of protein inhibitors that have been continuously studied in different species and have great biotechnological potential.
Monaliza Macêdo Ferreira +4 more
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In vivo anti-HIV activity of the heparin-activated serine protease inhibitor antithrombin III encapsulated in lymph-targeting immunoliposomes. [PDF]
PLoS ONE, 2012 Endogenous serine protease inhibitors (serpins) are anti-inflammatory mediators with multiple biologic functions. Several serpins have been reported to modulate HIV pathogenesis, or exhibit potent anti-HIV activity in vitro, but the efficacy of serpins ...
Mohammed Asmal +6 more
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