Letteratura scientifica selezionata sul tema "Glyoxylate shunt"
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Articoli di riviste sul tema "Glyoxylate shunt":
Long, Bui Hoang Dang, Masahiro Nishiyama, Rintaro Sato, Tomonari Tanaka, Hitomi Ohara e Yuji Aso. "Production of Glyoxylate from Glucose in Engineered Escherichia coli". Fermentation 9, n. 6 (31 maggio 2023): 534. http://dx.doi.org/10.3390/fermentation9060534.
Dolan, Stephen K., e Martin Welch. "The Glyoxylate Shunt, 60 Years On". Annual Review of Microbiology 72, n. 1 (8 settembre 2018): 309–30. http://dx.doi.org/10.1146/annurev-micro-090817-062257.
Puckett, Susan, Carolina Trujillo, Zhe Wang, Hyungjin Eoh, Thomas R. Ioerger, Inna Krieger, James Sacchettini, Dirk Schnappinger, Kyu Y. Rhee e Sabine Ehrt. "Glyoxylate detoxification is an essential function of malate synthase required for carbon assimilation inMycobacterium tuberculosis". Proceedings of the National Academy of Sciences 114, n. 11 (6 marzo 2017): E2225—E2232. http://dx.doi.org/10.1073/pnas.1617655114.
Schink, Bernhard. "An alternative to the glyoxylate shunt". Molecular Microbiology 73, n. 6 (settembre 2009): 975–77. http://dx.doi.org/10.1111/j.1365-2958.2009.06835.x.
Ahn, Sungeun, Jaejoon Jung, In-Ae Jang, Eugene L. Madsen e Woojun Park. "Role of Glyoxylate Shunt in Oxidative Stress Response". Journal of Biological Chemistry 291, n. 22 (1 aprile 2016): 11928–38. http://dx.doi.org/10.1074/jbc.m115.708149.
McVey, Alyssa C., Sean Bartlett, Mahmud Kajbaf, Annalisa Pellacani, Viviana Gatta, Päivi Tammela, David R. Spring e Martin Welch. "2-Aminopyridine Analogs Inhibit Both Enzymes of the Glyoxylate Shunt in Pseudomonas aeruginosa". International Journal of Molecular Sciences 21, n. 7 (3 aprile 2020): 2490. http://dx.doi.org/10.3390/ijms21072490.
Ritson, Dougal J. "A cyanosulfidic origin of the Krebs cycle". Science Advances 7, n. 33 (agosto 2021): eabh3981. http://dx.doi.org/10.1126/sciadv.abh3981.
Nanchen, Annik, Alexander Schicker e Uwe Sauer. "Nonlinear Dependency of Intracellular Fluxes on Growth Rate in Miniaturized Continuous Cultures of Escherichia coli". Applied and Environmental Microbiology 72, n. 2 (febbraio 2006): 1164–72. http://dx.doi.org/10.1128/aem.72.2.1164-1172.2006.
Davis, W. L., R. G. Jones e D. B. Goodman. "Cytochemical localization of malate synthase in amphibian fat body adipocytes: possible glyoxylate cycle in a vertebrate." Journal of Histochemistry & Cytochemistry 34, n. 5 (maggio 1986): 689–92. http://dx.doi.org/10.1177/34.5.3701032.
Sarao, Renu, Howard D. McCurdy e Luciano Passador. "Enzymes of the intermediary carbohydrate metabolism of Polyangium cellulosum". Canadian Journal of Microbiology 31, n. 12 (1 dicembre 1985): 1142–46. http://dx.doi.org/10.1139/m85-215.
Tesi sul tema "Glyoxylate shunt":
Reumerman, Richard A. "Functional and mathematical analysis of the glyoxylate shunt in Streptomyces coelicolor". Thesis, University of Strathclyde, 2015. http://oleg.lib.strath.ac.uk:80/R/?func=dbin-jump-full&object_id=26435.
Dean, Jason Thaddeus. "A synthetic glyoxylate shunt for increased fatty acid degradation in hepatocytes". Diss., Restricted to subscribing institutions, 2009. http://proquest.umi.com/pqdweb?did=1971757751&sid=1&Fmt=2&clientId=1564&RQT=309&VName=PQD.
Koedooder, Coco. "The interplay between Fe-limitation, carbon and light in a (photo)heterotrophic bacterium". Electronic Thesis or Diss., Sorbonne université, 2019. http://www.theses.fr/2019SORUS170.
Iron (Fe) is an essential element for marine microbial growth but is present in trace amounts in the surface waters of the ocean. In heterotrophic bacteria, Fe-limitation particularly impacts ATP production and have been shown to implement various strategies to cope in the presence of Fe-limitation. Genetic tools enabled us to test two potential strategies within the model organism Photobacterium angustum S14. The glyoxylate shunt, a metabolic pathway found in aerobic bacteria bypassing several steps within the classic tricarboxylic acid (TCA) was shown to be upregulated under Fe-limitation and we propose that the glyoxylate shunt was able to redirect a cell’s metabolism away from Fe-limiting steps within the electron transport, thereby increasing the metabolic efficiency of the cell under Fe-limitation. Proteorhodopsin, a light activated proton pump found in several heterotrophic bacteria, could alleviate Fe-stress if the produced proton gradient is coupled to ATP synthase. Our results showed that proteorhodopsin is upregulated as cells approached the stationary phase under both Fe-replete and Fe-limiting conditions but was absent during the exponential phase. Future work in elucidating the role of proteorhodopsin, and particularly under Fe-limitation, should therefore focus on the stationary phase of a bacterial cell. The results from this thesis manuscript contributed to a culminating body of work surrounding the versatility of marine heterotrophic bacteria in coping with Fe-limitation and is an appropriate addition to the literature surrounding the role of proteorhodopsin and the glyoxylate shunt within the marine environment
Capitoli di libri sul tema "Glyoxylate shunt":
Bott, Michael, e Bernhard J. Eikmanns. "TCA Cycle and Glyoxylate Shunt of Corynebacterium glutamicum". In Corynebacterium glutamicum, 281–313. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-29857-8_10.
Peña Mattozzi, M., Yisheng Kang e Jay D. Keasling. "Feast: Choking on Acetyl-CoA, the Glyoxylate Shunt, and Acetyl-CoA-Driven Metabolism". In Cellular Ecophysiology of Microbe, 1–12. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-20796-4_52-1.
de la Peña Mattozzi, M., Y. Kang e J. D. Keasling. "Feast: Choking on Acetyl-CoA, the Glyoxylate Shunt, and Acetyl-CoA-Driven Metabolism". In Handbook of Hydrocarbon and Lipid Microbiology, 1649–60. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-77587-4_116.
Peña Mattozzi, M., Yisheng Kang e Jay D. Keasling. "Feast: Choking on Acetyl-CoA, the Glyoxylate Shunt, and Acetyl-CoA-Driven Metabolism". In Cellular Ecophysiology of Microbe: Hydrocarbon and Lipid Interactions, 463–74. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-50542-8_52.