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Bioengineering studies and pathway modeling of the heterologous biosynthesis of tetrahydrocannabinolic acid in yeast

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Peroxisome deficiency-induced ER stress and SREBP-2 pathway activation in the liver of newborn PEX2 knock-out mice

Kovacs, W. J., Charles, K. N., Walter, K., Shackelford, J. E., Wikander, T. M., Richards, M. J., Fliesler, S. J., Krisans, S. K., & Faust, P. L. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2012.02.011 · Cited by 37

Enhanced β-carotene production in Yarrowia lipolytica through the metabolic and fermentation engineering

Jing, Y., Wang, J., Gao, H., Jiang, Y., Jiang, W., Jiang, M. H., Xin, F., & Zhang, W. (2023) · Journal of Industrial Microbiology & Biotechnology · doi:10.1093/jimb/kuad009 · Cited by 39

AMPK-regulated glycerol excretion maintains metabolic crosstalk between reductive and energetic stress

Zhai, X., Yang, R., Chu, Q., Guo, Z., Hou, P., Li, X., Bai, C., Lu, Z., Qiao, L., Fu, Y., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-024-01549-x · Cited by 36

Alteration of cholesterol distribution at the plasma membrane of cancer cells: From evidence to pathophysiological implication and promising therapy strategy

Maja, M., & Tyteca, D. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.999883 · Cited by 38

Comparative Transcriptomic Analysis of Subcutaneous Adipose Tissue from Local Pig Breeds

Albuquerque, A., Óvilo, C., Núñez, Y., Benítez, R., López-García, A., García, F., Félix, M. D. R., Laranjo, M., Charneca, R., & Martins, J. M. (2020) · Genes · doi:10.3390/genes11040422 · Cited by 36

Strategies to Better Target Fungal Squalene Monooxygenase

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Hepatic molecular responses to Bifidobacterium pseudocatenulatum CECT 7765 in a mouse model of diet-induced obesity

Moya-Pérez, Á., Romo‐Vaquero, M., Tomás-Barberán, F. A., Sanz, Y., & García‐Conesa, M. (2013) · Nutrition Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2013.04.011 · Cited by 35

Sesquiterpene Synthase–3-Hydroxy-3-Methylglutaryl Coenzyme A Synthase Fusion Protein Responsible for Hirsutene Biosynthesis in Stereum hirsutum

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The E3 ubiquitin ligase MARCHF6 as a metabolic integrator in cholesterol synthesis and beyond

Scott, N. A., Sharpe, L. J., & Brown, A. J. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2020.158837 · Cited by 16

Molecular Modeling of the Reaction Pathway and Hydride Transfer Reactions of HMG-CoA Reductase

Haines, B. E., Steussy, C. N., Stauffacher, C. V., & Wiest, O. (2012) · Biochemistry · doi:10.1021/bi3008593 · Cited by 32

Sterol Regulatory Element-Binding Protein (Sre1) Promotes the Synthesis of Carotenoids and Sterols in Xanthophyllomyces dendrorhous

Gutiérrez, M. S., Campusano, S., González, A. M., Gómez, M., Barahona, S., Sepúlveda, D., Espenshade, P. J., Fernández‐Lobato, M., Baeza, M., Cifuentes, V., et al. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00586 · Cited by 31

The cholesterol synthesis enzyme lanosterol 14α-demethylase is post-translationally regulated by the E3 ubiquitin ligase MARCH6

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Efficient Plant Triterpenoids Synthesis in Saccharomyces cerevisiae : from Mechanisms to Engineering Strategies

Wang, S., Meng, D., Feng, M., Li, C., & Wang, Y. (2024) · ACS Synthetic Biology · doi:10.1021/acssynbio.4c00061 · Cited by 29

Computational study of conformational changes in human 3-hydroxy-3-methylglutaryl coenzyme reductase induced by substrate binding

da Costa, C. H. S., Oliveira, A. R. S., dos Santos, A. M., da Costa, K. S., Lima, A. H., Alves, C. N., & Lameira, J. (2018) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2018.1549508 · Cited by 29

Enhanced bio-synthesis of isoprene via modifying mevalonate and methylerythritol phosphate pathways for industrial application: A review

Kant, G., Pandey, A., Shekhar, H., & Srivastava, S. (2023) · Process Biochemistry · doi:10.1016/j.procbio.2023.04.021 · Cited by 29

S-Carvone Suppresses Cellulase-Induced Capsidiol Production in Nicotiana tabacum by Interfering with Protein Isoprenylation

Huchelmann, A., Gastaldo, C., Veinante, M., Zeng, Y., Heintz, D., Tritsch, D., Schaller, H., Rohmer, M., Bach, T. J., & Hemmerlin, A. (2013) · PLANT PHYSIOLOGY · doi:10.1104/pp.113.232546 · Cited by 29

HCV 3a Core Protein Increases Lipid Droplet Cholesteryl Ester Content via a Mechanism Dependent on Sphingolipid Biosynthesis

Loizides‐Mangold, U., Clément, S., Garcia, A. A., Branche, E., Conzelmann, S., Parisot, C., Potma, E. O., Riezman, H., & Negro, F. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115309 · Cited by 29

Insig Regulates HMG‐CoA Reductase by a Non‐Degradative Mechanism in Fission Yeast

Burg, J. S., Bard, M., Powell, D. W., & Espenshade, P. J. (2007) · The FASEB Journal · doi:10.1096/fasebj.21.5.a609-c

Insig Regulates HMG-CoA Reductase by Controlling Enzyme Phosphorylation in Fission Yeast

Burg, J. S., Powell, D. W., Chai, R. L., Hughes, A. L., Link, A. J., & Espenshade, P. J. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.09.004 · Cited by 53

Regulation and degradation of HMGCo-A reductase

Panda, T., & Devi, V. A. (2004) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-004-1720-5 · Cited by 24

Glucose Controls Phosphoregulation of Hydroxymethylglutaryl Coenzyme A Reductase through the Protein Phosphatase 2A-related Phosphatase Protein, Ppe1, and Insig in Fission Yeast

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The 3-hydroxy-3-methylglutaryl coenzyme-A reductases from fungi: A proposal as a therapeutic target and as a study model

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