A versatile inhibitor of digestive enzymes in Aedes aegypti larvae selected from a pacifastin (TiPI) phage display library.
暂无分享,去创建一个
A. Tanaka | A. Tashima | Francisco Jose Alves Lemos | Ricardo Jose Soares Torquato | Veronica Moraes Manzato | Erika Sayuri Nishiduka Costa de Almeida
[1] Pedro M S Tabosa,et al. Trypsin inhibitor from Enterolobium contortisiliquum seeds impairs Aedes aegypti development and enhances the activity of Bacillus thuringiensis toxins. , 2020, Pest management science.
[2] G. Ebel,et al. Arbovirus coinfection and co-transmission: A neglected public health concern? , 2019, PLoS biology.
[3] S. Pletnev,et al. Crystal structure of a novel Kunitz type inhibitor, alocasin with anti-Aedes aegypti activity targeting midgut proteases. , 2018, Pest management science.
[4] D. Ferreira,et al. History, epidemiology and diagnostics of dengue in the American and Brazilian contexts: a review , 2018, Parasites & Vectors.
[5] P. Young. Arboviruses: A Family on the Move. , 2018, Advances in experimental medicine and biology.
[6] T. S. Lim,et al. Phage Display , 2018, Methods in Molecular Biology.
[7] J. Ramos-Castañeda,et al. Dengue in Latin America: Systematic Review of Molecular Epidemiological Trends , 2017, PLoS neglected tropical diseases.
[8] M. Russel,et al. Filamentous Phage: Structure and Biology. , 2017, Advances in experimental medicine and biology.
[9] S. Lindsay,et al. Personal Protection of Permethrin-Treated Clothing against Aedes aegypti, the Vector of Dengue and Zika Virus, in the Laboratory , 2016, PloS one.
[10] T. Soares,et al. Production of serine protease inhibitors by mutagenesis and their effects on the mortality of Aedes aegypti L. larvae , 2015, Parasites & Vectors.
[11] G. Áñez,et al. Epidemiological Scenario of Dengue in Brazil , 2015, BioMed research international.
[12] L. Coelho,et al. Trypsin inhibitor from Moringa oleifera flowers interferes with survival and development of Aedes aegypti larvae and kills bacteria inhabitant of larvae midgut , 2014, Parasitology Research.
[13] A. Tanaka,et al. Selective inhibitors of digestive enzymes from Aedes aegypti larvae identified by phage display. , 2013, Insect biochemistry and molecular biology.
[14] R. Torquato,et al. The Kazal-type inhibitors infestins 1 and 4 differ in specificity but are similar in three-dimensional structure. , 2012, Acta crystallographica. Section D, Biological crystallography.
[15] T. Soares,et al. Molecular characterization of genes encoding trypsin-like enzymes from Aedes aegypti larvae and identification of digestive enzymes. , 2011, Gene.
[16] R. Torquato,et al. The first pacifastin elastase inhibitor characterized from a blood sucking animal , 2010, Peptides.
[17] J. Broeck,et al. Pacifastin-related peptides: Structural and functional characteristics of a family of serine peptidase inhibitors , 2009, Peptides.
[18] M. L. Macedo,et al. Regulatory effects of an inhibitor from Plathymenia foliolosa seeds on the larval development of Anagasta kuehniella (Lepidoptera). , 2009, Comparative biochemistry and physiology. Part A, Molecular & integrative physiology.
[19] M. Juliano,et al. The role of HiTI, a serine protease inhibitor from Haematobia irritans irritans (Diptera: Muscidae) in the control of fly and bacterial proteases. , 2005, Experimental parasitology.
[20] G. Katona,et al. Extended intermolecular interactions in a serine protease-canonical inhibitor complex account for strong and highly specific inhibition. , 2005, Journal of molecular biology.
[21] L. Hedstrom. An Overview of Serine Proteases , 2001, Current protocols in protein science.
[22] E. Auerswald,et al. Functional phage display of leech‐derived tryptase inhibitor (LDTI): construction of a library and selection of thrombin inhibitors , 1999, FEBS letters.
[23] J F Morrison,et al. Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors. , 1969, Biochimica et biophysica acta.
[24] A. Berger,et al. On the size of the active site in proteases. I. Papain. , 1967, Biochemical and biophysical research communications.