Relevant bibliographies by topics / Trehalase inhibitors

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  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Trehalase inhibitors'

Author: Grafiati
Published: 9 March 2023
Last updated: 31 July 2025

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Journal articles on the topic "Trehalase inhibitors"

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Marten, Andrew D., Douglas P. Haslitt, Chad A. Martin, et al. "Trehalose supports the growth of Aedes aegypti cells and modifies gene expression and dengue virus type 2 replication." PLOS Pathogens 21, no. 5 (2025): e1012795. https://doi.org/10.1371/journal.ppat.1012795.

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Trehalose is a non-reducing disaccharide that is the major sugar found in insect hemolymph fluid. Trehalose provides energy, and promotes growth, metamorphosis, stress recovery, chitin synthesis, and insect flight. Trehalase is the only enzyme responsible for the hydrolysis of trehalose, which makes it an attractive molecular target. Here we show that Aedes aegypti (Aag2) cells express trehalase and that they can grow on trehalose-containing cell culture media. Trehalase activity was confirmed by treating Aag2 cells with trehalase inhibitors, which inhibited conversion of trehalose to glucose
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White, Christopher, Deborah B. Lee, and Stephen J. Free. "NEUROSPORA TREHALASE AND ITS STRUCTURAL GENE." Genetics 110, no. 2 (1985): 217–27. http://dx.doi.org/10.1093/genetics/110.2.217.

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ABSTRACT We have isolated Neurospora trehalaseless mutants and mapped the trehalase structural gene to linkage group I. The structural gene mutations not only affect thermostability and other characteristics of the enzyme but also affect the production of an inhibitor of the wild-type trehalase. The inhibitor appears to be the mutant trehalase. We suggest that the mutant subunits act as inhibitors by entering into the multimeric forms of the enzyme and altering the ability of the normal wild-type subunits to catalyze the cleavage of trehalose.—Wild type trehalase has been purified to near homo
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Matassini, Camilla, Camilla Parmeggiani, and Francesca Cardona. "New Frontiers on Human Safe Insecticides and Fungicides: An Opinion on Trehalase Inhibitors." Molecules 25, no. 13 (2020): 3013. http://dx.doi.org/10.3390/molecules25133013.

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In the era of green economy, trehalase inhibitors represent a valuable chance to develop non-toxic pesticides, being hydrophilic compounds that do not persist in the environment. The lesson on this topic that we learned from the past can be of great help in the research on new specific green pesticides. This review aims to describe the efforts made in the last 50 years in the evaluation of natural compounds and their analogues as trehalase inhibitors, in view of their potential use as insecticides and fungicides. Specifically, we analyzed trehalase inhibitors based on sugars and sugar mimics,
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Marten, Andrew D., Alicyn I. Stothard, Karishma Kalera, Benjamin M. Swarts, and Michael J. Conway. "Validamycin A Delays Development and Prevents Flight in Aedes aegypti (Diptera: Culicidae)." Journal of Medical Entomology 57, no. 4 (2020): 1096–103. http://dx.doi.org/10.1093/jme/tjaa004.

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Abstract Trehalose is a disaccharide that is the major sugar found in insect hemolymph fluid. Trehalose provides energy, and promotes growth, metamorphosis, stress recovery, chitin synthesis, and insect flight. The hydrolysis of trehalose is under the enzymatic control of the enzyme trehalase. Trehalase is critical to the role of trehalose in insect physiology, and is required for the regulation of metabolism and glucose generation. Trehalase inhibitors represent a novel class of insecticides that have not been fully developed. Here, we tested the ability of trehalose analogues to function as
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Streeter, J. G., and M. L. Gomez. "Three Enzymes for Trehalose Synthesis in Bradyrhizobium Cultured Bacteria and in Bacteroids from Soybean Nodules." Applied and Environmental Microbiology 72, no. 6 (2006): 4250–55. http://dx.doi.org/10.1128/aem.00256-06.

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ABSTRACT α,α-Trehalose is a disaccharide accumulated by many microorganisms, including rhizobia, and a common role for trehalose is protection of membrane and protein structure during periods of stress, such as desiccation. Cultured Bradyrhizobium japonicum and B. elkanii were found to have three enzymes for trehalose synthesis: trehalose synthase (TS), maltooligosyltrehalose synthase (MOTS), and trehalose-6-phosphate synthetase. The activity level of the latter enzyme was much higher than those of the other two in cultured bacteria, but the reverse was true in bacteroids from nodules. Althoug
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Yu, Liuhe, Fan Zhong, Xinyi Jiang, et al. "Effect of Three Novel Thiazolidiones on the Development, Reproduction, and Trehalase Activity of Spodoptera frugiperda (Lepidoptera: Noctuidae)." Agronomy 14, no. 6 (2024): 1315. http://dx.doi.org/10.3390/agronomy14061315.

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Spodoptera frugiperda was used to investigate its role as a trehalase inhibitor of three new thiothiazolidone compounds—6d, 6e, and 6f. The development and reproduction of S. frugiperda were investigated to evaluate the potential of these compounds as a novel pesticide for pest control. Compounds 6d, 6e, and 6f were injected into larvae and female pupae. Molecular changes in trehalose and chitin metabolism genes were monitored. Pupal trehalase activity, the female pupal emergence rate, ovarian development, and SfVg and SfVgR gene expression levels were assessed. The results revealed that all t
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Bini, Davide, Francesca Cardona, Matilde Forcella, et al. "Synthesis and biological evaluation of nojirimycin- and pyrrolidine-based trehalase inhibitors." Beilstein Journal of Organic Chemistry 8 (April 5, 2012): 514–21. http://dx.doi.org/10.3762/bjoc.8.58.

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A small set of nojirimycin- and pyrrolidine-based iminosugar derivatives has been synthesized and evaluated as potential inhibitors of porcine and insect trehalases. Compounds 12, 13 and 20 proved to be active against both insect and porcine trehalases with selectivity towards the insect glycosidase, while compounds 10, 14 and 16 behaved as inhibitors only of insect trehalase. Despite the fact that the activity was found in the micromolar range, these findings may help in elucidating the structural features of this class of enzymes of different origin, which are still scarcely characterised.
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KAMEDA, YUKIHIKO, NAOKI ASANO, TAKUJI YAMAGUCHI, and KATSUHIKO MATSUI. "Validoxylamines as trehalase inhibitors." Journal of Antibiotics 40, no. 4 (1987): 563–65. http://dx.doi.org/10.7164/antibiotics.40.563.

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Kyosseva, S. V., Z. N. Kyossev, and A. D. Elbein. "Inhibitors of Pig Kidney Trehalase." Archives of Biochemistry and Biophysics 316, no. 2 (1995): 821–26. http://dx.doi.org/10.1006/abbi.1995.1110.

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QIAN, XUHONG, ZHIBIN LI, ZHI LIU, GONGHUA SONG, and ZHONG LI. "Syntheses of 2-Aryliminooxazolidine Derivatives as Trehalase Inhibitors." Journal of Antibiotics 54, no. 12 (2001): 1108–10. http://dx.doi.org/10.7164/antibiotics.54.1108.

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Dissertations / Theses on the topic "Trehalase inhibitors"

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BINI, DAVIDE. "Synthesis of Glycoconjugates and their Analogs for the Study of Biological Systems." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2016. http://hdl.handle.net/10281/103143.

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ABSTRACT The project was focussed on the development of three main topics: a) trehalose mimics as trehalase inhibitors, b) synthesis of multivalent glycoconjugates and c) synthesis of glycosylated Pluronic block copolymers. a) Trehalose mimics as trehalase inhibitors Trehalase (α-glucoside-1-glucohydrolase, EC 3.2.1.28) is a specific glycosidase that catalyzes the hydrolysis of trehalose (α-D-glucopyranosyl-α-D-glucopyranoside) to the two constituent glucose units. This disaccharide is found in many organisms, but is absent in mammals. In insects, trehalose hydrolysis by trehalase is fundam
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Thanna, Sandeep. "Design and Synthesis of Novel Inhibitors for Enzymatic Targets in Trehalose Utilization Pathways of Mycobacterium tuberculosis." University of Toledo / OhioLINK, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=toledo1501627900249048.

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Huang, Yin-Jung, and 黃胤榮. "Functional expression of human trehalase in Escherichia coli and identification of novel trehalase inhibitors." Thesis, 2013. http://ndltd.ncl.edu.tw/handle/95603406888333667888.

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碩士<br>國立臺灣師範大學<br>生命科學研究所<br>101<br>In mammals, trehalase, sucrase-isomaltase and maltase-glucoamylase are the major α-glycosidases of the intestinal brush border membranes. These enzymes are responsible for the degradation of di- and oligosaccharides into monosaccharides, and are crucial for the energy-intake. Trehalase (EC 3.2.1.28) hydrolyses α,α-trehalose (1-α-D-glucopyranosyl α-D-glucopyranoside) to two glucose molecules. The intestinal trehalase is involved in the hydrolysis of ingested trehalose which is found mainly in many nutrient foods. The dual protective properties of trehalose (a
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Miao, Yi. "Structural and Biochemical Dissection of the Trehalose Biosynthetic Complex in Pathogenic Fungi." Diss., 2016. http://hdl.handle.net/10161/12130.

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<p>Trehalose is a non-reducing disaccharide essential for pathogenic fungal survival and virulence. The biosynthesis of trehalose requires the trehalose-6-phosphate synthase, Tps1, and trehalose-6-phosphate phosphatase, Tps2. More importantly, the trehalose biosynthetic pathway is absent in mammals, conferring this pathway as an ideal target for antifungal drug design. However, lack of germane biochemical and structural information hinders antifungal drug design against these targets. </p><p>In this dissertation, macromolecular X-ray crystallography and biochemical assays were employed to und
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Book chapters on the topic "Trehalase inhibitors"

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El Nemr, Ahmed, and El Sayed H. El Ashry. "Potential trehalase inhibitors." In Advances in Carbohydrate Chemistry and Biochemistry. Elsevier, 2011. http://dx.doi.org/10.1016/b978-0-12-385520-6.00003-0.

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