Výsledky vyhledávání

Cationic lipid/pDNA complex formation as potential generic method to generate specific IRF pathway stimulators

Autor: Iris Heep, Elisabeth Feldhues, Alf Lamprecht, Thomas Ilg, Simone Putzke

Publikováno v: European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V. 155

Cationic liposome - CpG DNA complexes (lipoplexes) are known as stimulators of innate immunity via Toll-like receptor 9 (TLR9)-triggered activation of the nuclear factor kappa B (NF-κB) pathway. More recent reports suggest that DNA lipoplexes also e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f806884efda3a0a46633501c7c525b72
https://pubmed.ncbi.nlm.nih.gov/32798666

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The immunostimulator Victrio activates chicken toll-like receptor 21

Autor: Thomas Ilg

Publikováno v: Veterinary immunology and immunopathology. 220

The immunostimulator Victrio consists of bacterial plasmid DNA encased in cationic liposomes and protects embryonated chicken eggs and newly hatched chickens against Escherichia coli induced mortality. It is demonstrated that Victrio specifically and

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https://pubmed.ncbi.nlm.nih.gov/31760146

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Investigations on the molecular mode of action of the novel immunostimulator ZelNate: Activation of the cGAS-STING pathway in mammalian cells

Autor: Thomas Ilg

Publikováno v: Molecular immunology. 90

Bovine respiratory disease (BRD) is usually prevented or treated with vaccines and/or antibiotics. The use of antibiotics is, however, of concern due to the potential promotion of microbial resistance and the occurrence of residues. Recently an alter

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dcdb27e508fd47982ee919de816aa798
https://pubmed.ncbi.nlm.nih.gov/28802127

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Glutamate decarboxylase of the parasitic arthropods Ctenocephalides felis and Rhipicephalus microplus: Gene identification, cloning, expression, assay development, identification of inhibitors by high throughput screening and comparison with the orthologs from Drosophila melanogaster and mouse

Autor: Andreas Rohwer, Michael Gaßel, Michael Berger, Thomas Ilg, Sandra Noack

Publikováno v: Insect Biochemistry and Molecular Biology. 43:162-177

Glutamate decarboxylase (l-glutamate 1-carboxylyase, E.C. 4.1.1.15, GAD) is the rate-limiting enzyme for the production of γ-aminobutyric acid (GABA), the major inhibitory neurotransmitter in vertebrates and invertebrates. We report the identificati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0dd297f51a056a1e1d1e009a9e7f287
https://doi.org/10.1016/j.ibmb.2012.11.001

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Structure-activity relationships of acetylcholine derivatives withLucilia cuprinanicotinic acetylcholine receptor α1 and α2 subunits in chicken β2 subunit hybrid receptors in comparison with chicken nicotinic acetylcholine receptor α4/β2

Autor: M. Berger, H. Dederer, Thomas Ilg, T. Meyer, M. Werr

Publikováno v: Insect Molecular Biology. 22:183-198

Insect nicotinic acetylcholine (ACh) receptors (nAChRs) are the targets of several insecticide classes. In the present study, we report the gene identification and cloning of nAChR α1 and α2 subunits (Lcα1 and Lcα2) from the sheep blowfly Lucilia

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cef560bd5d9e8c7ac7e3a586e6281d5f
https://doi.org/10.1111/imb.12014

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Trehalose-6-phosphate synthase from the cat flea Ctenocephalides felis and Drosophila melanogaster: gene identification, cloning, heterologous functional expression and identification of inhibitors by high throughput screening

Autor: F. Bender, C. Wolf, S. Schmalz, Thomas Ilg, C. Kern, M. Berger, Sandra Noack

Publikováno v: Insect Molecular Biology. 21:456-471

Trehalose phosphate synthase (EC 2.4.1.15; TPS) is the crucial enzyme for the biosynthesis of trehalose, the main haemolymph sugar of insects, and therefore a potential insecticidal molecular target. In this study, we report the functional heterologo

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https://doi.org/10.1111/j.1365-2583.2012.01151.x

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Arginine kinase of the sheep blowfly Lucilia cuprina: Gene identification and characterization of the native and recombinant enzyme

Autor: Margaret Werr, Thomas Ilg

Publikováno v: Pesticide Biochemistry and Physiology. 102:115-123

Arginine kinase (ATP: l -arginine ω- N -phosphotransferase, EC2.7.3.3.; AK) is an enzyme with crucial functions in the energy metabolism of insects and other invertebrates as well as some protozoa and has been proposed as a parasiticidal and pestici

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8065aa089aea962f67f9730c00a8d730
https://doi.org/10.1016/j.pestbp.2011.12.001

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Differential sensitivity of Ctenocephalides felis and Drosophila melanogaster nicotinic acetylcholine receptor α1 and α2 subunits in recombinant hybrid receptors to nicotinoids and neonicotinoid insecticides

Autor: Helene Dederer, Thomas Ilg, Margaret Werr

Publikováno v: Insect Biochemistry and Molecular Biology. 41:51-61

Nicotinic acetylcholine receptors (nAChRs) are the binding sites for nicotinoid drugs, such as nicotine and epibatidine, and are the molecular targets of the selectively insecticidal neonicotinoids. In this study we report the full length cDNA clonin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d29440ebc6d4addfe54bf1cff60dde67
https://doi.org/10.1016/j.ibmb.2010.09.012

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Identification and characterization of two arginine kinases from the parasitic insect Ctenocephalides felis

Autor: Jörg Cramer, Margaret Werr, Thomas Ilg

Publikováno v: Insect Biochemistry and Molecular Biology. 39:634-645

Arginine kinase (ATP:l-arginine omega-N-phosphotransferase, EC2.7.3.3.; AK) is an enzyme crucial for the energy metabolism of insects and other invertebrates, that has known allergenic potential in humans and that has been proposed as a pesticidal dr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad2e3353460905de93ff3500b9ecc342
https://doi.org/10.1016/j.ibmb.2009.07.001

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