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Analysis of the Toxicological Profile of <i>Heracleum sosnowskyi</i> Manden. Metabolites Using <i>In Silico</i> Methods. [PDF]
Plants (Basel)Rassabina AE, Fedorov MV.
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Impact of protein prenylation inhibition on Mycobacterium leprae viability and IL-1β production in infected macrophages. [PDF]
J Bacteriolda Silva Rocha M +11 more
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Reconstitution of the Mevalonate Pathway for Improvement of Isoprenoid Production and Industrial Applicability in Escherichia coli. [PDF]
J Microbiol BiotechnolKang MK +7 more
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Editorial: The metabolic pathways of archaea. [PDF]
Front MicrobiolMyllykallio H, Qin W, Berg IA.
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Naturally Occurring PCSK9 Inhibitors: An Updated Review. [PDF]
MoleculesHuh J, Kim H.
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Thermostable Enzyme Variants in the Lower Mevalonate Pathway Improve Isoprenoid Production by Cell-Free Biocatalysis. [PDF]
ACS Sustain Chem EngSarnik SA +5 more
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Opportunistic emissions of volatile isoprenoids
Trends in Plant Science, 2005Isoprene, monoterpenes and sesquiterpenes are synthesized and emitted by some plant species, but not all plant species have this ability. These volatile, nonessential isoprenoid compounds share the same biochemical precursors as larger essential isoprenoids such as gibberellic acids and carotenoids.
Josep Penuelas
exaly +3 more sources
Science, 1997
Living things use isoprenoids as pigments, hormones, molecular signals, and pheromones. The many variations of isoprenoid are generated by versatile enzymes that synthesize multiple products. In their Perspective, Sacchettini and Poulter discuss what the new structures of three of these cyclases, reported on pages 1811, 1815, and 1820 ...
J C, Sacchettini, C D, Poulter
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Living things use isoprenoids as pigments, hormones, molecular signals, and pheromones. The many variations of isoprenoid are generated by versatile enzymes that synthesize multiple products. In their Perspective, Sacchettini and Poulter discuss what the new structures of three of these cyclases, reported on pages 1811, 1815, and 1820 ...
J C, Sacchettini, C D, Poulter
openaire +2 more sources
2010
Up to 2% of the mammalian proteome is post-translationally modified with isoprenes (Gelb 1997). The first prenylated polypeptides reported were secreted pheromone peptides identified in jelly fungi (Sakagami et al. 1978; Tsuchiya et al. 1978). The structure of these peptides resembled the a-factor mating pheromone from S.
Nguyen, Uyen +3 more
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Up to 2% of the mammalian proteome is post-translationally modified with isoprenes (Gelb 1997). The first prenylated polypeptides reported were secreted pheromone peptides identified in jelly fungi (Sakagami et al. 1978; Tsuchiya et al. 1978). The structure of these peptides resembled the a-factor mating pheromone from S.
Nguyen, Uyen +3 more
openaire +2 more sources