Regulation of glucose metabolism from a liver-centric perspective
Open accessAbstract
Glucose homeostasis is tightly regulated to meet the energy requirements of the vital organs and maintain an individual’s health. The liver has a major role in the control of glucose homeostasis by controlling various pathways of glucose metabolism, including glycogenesis, glycogenolysis, glycolysis and gluconeogenesis. Both the acute and chronic regulation of the enzymes involved in the pathways are required for the proper functioning of these complex interwoven systems. Allosteric control by various metabolic intermediates, as well as post-translational modifications of these metabolic enzymes constitute the acute control of these pathways, and the controlled expression of the genes encoding these enzymes is critical in mediating the longer-term regulation of these metabolic pathways. Notably, several key transcription factors are shown to be involved in the control of glucose metabolism including glycolysis and gluconeogenesis in the liver. In this review, we would like to illustrate the current understanding of glucose metabolism, with an emphasis on the transcription factors and their regulators that are involved in the chronic control of glucose homeostasis. Hundreds of liver enzymes are involved in the body's processing of glucose. Together these enzymes help the body to maintain blood glucose levels and convert excessive carbohydrates into fatty acids. Seung-Hoi Koo and colleagues at Korea University. The researchers explain how these different liver enzymes are tightly regulated by several key transcription factors, including sterol regulatory element binding protein 1c (SREBP-1c), carbohydrate response element binding protein (ChREBP), cAMP response element-binding protein (CREB) and forkhead box protein O1 (FoxO1). Specifically, SREBP-1c and ChREBP are responsible for the chronic activation of glycolysis and fatty acid biosynthesis, while CREB and FoxO1 are responsible for the chronic activation of gluconeogenesis—the production of glucose from non-carbohydrate sources.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The increased presence of progesterone in the mid-luteal phase promotes shuttling of glucose into the liver and upregulates GLUT-4 and GLUT-1 translocation to enhance glycogen storage in endometrial tissue for embryonic support.
“the increased presence of progesterone in the mid-luteal phase promotes the shuttling of glucose into the liver, as well as upregulating GLUT-4 and GLUT-1 translocation to enhance glycogen storage in the endometrial tissue for embryonic support [84,157].”
From International society of sports nutrition position stand: nutritional concerns of the female athlete (2023) · cites this paper as [84]
The Concluding remarks state that the liver takes up glucose under feeding conditions and stores excess glucose as glycogen. They attribute hepatic glycogen storage to insulin-related mechanisms, not progesterone. The paper does not support the claim about the mid-luteal phase, GLUT-1 or GLUT-4 translocation, or glycogen storage in endometrial tissue for embryonic support. (LLM, conf=0.84)
Experimental — accuracy not yet measuredProgesterone affects glucose metabolism through upregulation of GLUT1 expression to increase endometrial glycolytic metabolism, attenuating skeletal and hepatic glycolytic pathways.
“affects glucose metabolism through the upregulation of GLUT1 expression to increase endometrial glycolytic metabolism, attenuating skeletal and hepatic glycolytic pathways [82–85]”
From International society of sports nutrition position stand: nutritional concerns of the female athlete (2023) · cites this paper as [84]
The 'Control of hepatic gluconeogenesis' and 'Concluding remarks' sections discuss liver glucose metabolism, but do not address progesterone. Searches for progesterone, GLUT1, endometrial glycolysis, and attenuation of skeletal or hepatic glycolysis found no passage supporting the attributed mechanism. (LLM, conf=0.76)
Experimental — accuracy not yet measuredRobust evidence demonstrates that estrogen and progesterone have important roles in regulating substrate metabolism.
“Robust evidence exists that demonstrates the important roles estrogen and progesterone have in regulating substrate metabolism [20,24,66,70,80,82,84,154–159].”
From International society of sports nutrition position stand: nutritional concerns of the female athlete (2023) · cites this paper as [84]
The ‘Control of hepatic gluconeogenesis’ section discusses estrogen-related receptor gamma (ERRγ), not the hormone estrogen. The passages do not address progesterone or establish that estrogen and progesterone regulate substrate metabolism (searched: progesterone; estrogen and progesterone substrate metabolism). (LLM, conf=0.77)
Experimental — accuracy not yet measuredProgesterone decreases the sensitivity of IGF-1 mediated uptake of glucose into skeletal muscle but upregulates GLUT-4 and GLUT-1 translocation to enhance glycogen storage in endometrial tissue for embryonic support.
“Progesterone decreases the sensitivity of IGF-1 mediated uptake of glucose into skeletal muscle, but upregulates GLUT-4 and GLUT-1 translocation to enhance glycogen storage in the endometrial tissue for embryonic support [84].”
From International society of sports nutrition position stand: nutritional concerns of the female athlete (2023) · cites this paper as [84]
The section on regulation of glycogen metabolism in the liver discusses insulin-driven hepatic glycogen synthesis, not progesterone or endometrial tissue; no page number is provided in our copy. Searches for progesterone and IGF-1-mediated skeletal-muscle glucose uptake, and for endometrial GLUT-1/GLUT-4 translocation, found no passage addressing the claim. (LLM, conf=0.76)
Experimental — accuracy not yet measuredEstrogen, specifically 17β-estradiol, promotes lipolysis and increases fatty acid availability while decreasing the rate of gluconeogenesis with muscle and liver glycogen sparing.
“Estrogen, specifically 17β-estradiol, promotes lipolysis and increases fatty acid availability while decreasing the rate of gluconeogenesis with muscle and liver glycogen sparing.”
From International society of sports nutrition position stand: nutritional concerns of the female athlete (2023) · cites this paper as [84]
The Control of hepatic gluconeogenesis section discusses fasting-related lipolysis and estrogen-related receptor gamma, but does not describe effects of 17β-estradiol. The Overview of glucose metabolism in the liver discusses glycogen depletion during fasting, not muscle or liver glycogen sparing by estrogen. Searches for estradiol, lipolysis, gluconeogenesis, and glycogen sparing found no passage addressing the attributed claim; page numbers were unavailable. (LLM, conf=0.75)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor
Brunet, A., Bonni, A., Zigmond, M. J., Lin, M. Z., Juo, P., Hu, L. S., Anderson, M. J., Arden, K. C., Blenis, J., & Greenberg, M. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80595-4 · Cited by 6,535 · see citing works
SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver
Horton, J. D., Goldstein, J. L., & Brown, M. S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15593 · Cited by 4,285 · see citing works
SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver
Horton, J. D., Goldstein, J. L., & Brown, M. S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215593 · Cited by 4,092 · see citing works
A Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis
Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864 · see citing works
Phosphorylated CREB binds specifically to the nuclear protein CBP
Chrivia, J. C., Kwok, R. P. S., Lamb, N., Hagiwara, M., Montminy, M. R., & Goodman, R. H. (1993) · Nature · doi:10.1038/365855a0 · Cited by 2,052 · see citing works
Control of hepatic gluconeogenesis through the transcriptional coactivator PGC-1
Yoon, J. C., Puigserver, P., Chen, G., Donovan, J., Wu, Z., Rhee, J., Adelmant, G., Stafford, J., Kahn, C. R., Granner, D. K., et al. (2001) · Nature · doi:10.1038/35093050 · Cited by 1,821 · see citing works
Li, Y., Xu, S., Mihaylova, M. M., Zheng, B., Hou, X., Jiang, B., Park, O., Luo, Z., Lefai, É., Shyy, J. Y.-J., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.009 · Cited by 1,788 · see citing works
Repa, J. J., Liang, G., Ou, J., Bashmakov, Y. K., Lobaccaro, J. A., Shimomura, I., Shan, B., Brown, M. S., Goldstein, J. L., & Mangelsdorf, D. J. (2000) · Genes & Development · doi:10.1101/gad.844900 · Cited by 1,693 · see citing works
Insulin-regulated hepatic gluconeogenesis through FOXO1–PGC-1α interaction
Puigserver, P., Rhee, J., Donovan, J., Walkey, C. J., Yoon, J. C., Oriente, F., Kitamura, Y., Altomonte, J., Dong, H., Accili, D., et al. (2003) · Nature · doi:10.1038/nature01667 · Cited by 1,487 · see citing works
CREB regulates hepatic gluconeogenesis through the coactivator PGC-1
Herzig, S., Long, F., Jhala, U. S., Hedrick, S., Quinn, R., Bauer, A., Rudolph, D., Schutz, G., Yoon, C., Puigserver, P., et al. (2001) · Nature · doi:10.1038/35093131 · Cited by 1,440 · see citing works
(2004) · doi:10.1016/s0092-8674(04)00452-0 · Cited by 1,356 · see citing works
Nuclear Receptors, RXR, and the Big Bang
Evans, R. M., & Mangelsdorf, D. J. (2014) · Cell · doi:10.1016/j.cell.2014.03.012 · Cited by 1,200 · see citing works
Defects in Adaptive Energy Metabolism with CNS-Linked Hyperactivity in PGC-1α Null Mice
Lin, J., Wu, P.-H., Tarr, P. T., Lindenberg, K. S., St-Pierre, J., Zhang, C.-Y., Mootha, V. K., Jäger, S., Vianna, C. R., Reznick, R. M., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.013 · Cited by 1,162 · see citing works
Biggs, W., Meisenhelder, J., Hunter, T. R., Cavenee, W. K., & Arden, K. C. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.13.7421 · Cited by 1,116 · see citing works
CREB and the CRTC co-activators: sensors for hormonal and metabolic signals
Altarejos, J. Y., & Montminy, M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3072 · Cited by 1,035 · see citing works
The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism
Koo, S., Flechner, L., Qi, L., Zhang, X., Screaton, R. A., Jeffries, S., Hedrick, S. A., Xu, W., Boussouar, F., Brindle, P. K., et al. (2005) · Nature · doi:10.1038/nature03967 · Cited by 996 · see citing works
Self-citationActivation of cAMP and mitogen responsive genes relies on a common nuclear factor
Arias, J., Alberts, A. S., Brindle, P. K., Claret, F. X., Smeal, T., Karin, M., Feramisco, J. R., & Montminy, M. (1994) · Nature · doi:10.1038/370226a0 · Cited by 726 · see citing works
Shimano, H., Yahagi, N., Amemiya-Kudo, M., Hasty, A. H., Osuga, J.-I., Tamura, Y., Shionoiri, F., Iizuka, Y., Ohashi, K., Harada, K., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.50.35832 · Cited by 691 · see citing works
A glucose-responsive transcription factor that regulates carbohydrate metabolism in the liver
Yamashita, H., Takenoshita, M., Sakurai, M., Bruick, R. K., Henzel, W. J., Shillinglaw, W., Arnot, D., & Uyeda, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.161284298 · Cited by 682 · see citing works
The CREB Coactivator TORC2 Functions as a Calcium- and cAMP-Sensitive Coincidence Detector
Screaton, R. A., Conkright, M. D., Katoh, Y., Best, J. L., Canettieri, G., Jeffries, S., Guzmán, E., Niessen, S., Yates, J. R., Takemori, H., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.015 · Cited by 649 · see citing works
Matsumoto, M., Pocai, A., Rossetti, L., DePinho, R. A., & Accili, D. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.08.006 · Cited by 616 · see citing works
Daitoku, H., Hatta, M., Matsuzaki, H., Aratani, S., Ohshima, T., Miyagishi, M., Nakajima, T., & Fukamizu, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400593101 · Cited by 602 · see citing works
Conkright, M. D., Canettieri, G., Screaton, R. A., Guzmán, E., Miraglia, L. J., Hogenesch, J. B., & Montminy, M. (2003) · Molecular Cell · doi:10.1016/j.molcel.2003.08.013 · Cited by 602 · see citing works
FoxO proteins in insulin action and metabolism
Barthel, A., Schmoll, D., & Unterman, T. G. (2005) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2005.03.010 · Cited by 599 · see citing works
REGULATION OF GLUCOSE PRODUCTION BY THE LIVER
Nordlie, R. C., Foster, J. D., & Lange, A. J. (1999) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.19.1.379 · Cited by 585 · see citing works
PGC-1 promotes insulin resistance in liver through PPAR-α-dependent induction of TRB-3
Koo, S.-H., Satoh, H., Herzig, S., Lee, C.-H., Hedrick, S., Kulkarni, R., Evans, R. M., Olefsky, J., & Montminy, M. (2004) · Nature Medicine · doi:10.1038/nm1044 · Cited by 550 · see citing works
Self-citationSeol, W., Choi, H.-S., & Moore, D. D. (1996) · Science · doi:10.1126/science.272.5266.1336 · Cited by 528 · see citing works
The nuclear receptor LXR is a glucose sensor
Mitro, N., Mak, P. A., Vargas, L., Godio, C., Hampton, E. N., Molteni, V., Kreusch, A., & Sáez, E. (2006) · Nature · doi:10.1038/nature05449 · Cited by 525 · see citing works
SREBPs: metabolic integrators in physiology and metabolism
Jeon, T.-I., & Osborne, T. F. (2011) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2011.10.004 · Cited by 513 · see citing works
The glucose-6-phosphatase system
SCHAFTINGEN, E. V., & Gerin, I. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3620513 · Cited by 495 · see citing works
Nakae, J., Park, B., & Accili, D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.23.15982 · Cited by 474 · see citing works
Roach, P. (2002) · Current Molecular Medicine · doi:10.2174/1566524024605761 · Cited by 468 · see citing works
Arginine Methylation of FOXO Transcription Factors Inhibits Their Phosphorylation by Akt
Yamagata, K., Daitoku, H., Takahashi, Y., Namiki, K., Hisatake, K., Kako, K., Mukai, H., Kasuya, Y., & Fukamizu, A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.09.013 · Cited by 436 · see citing works
Liver-Specific Inhibition of ChREBP Improves Hepatic Steatosis and Insulin Resistance in ob/ob Mice
Dentin, R., Benhamed, F., Hainault, I., Fauveau, V., Foufelle, F., Dyck, J. R. B., Girard, J. R., & Postic, C. (2006) · Diabetes · doi:10.2337/db06-0200 · Cited by 429 · see citing works
Mechanism for Fatty Acid “Sparing” Effect on Glucose-induced Transcription
Kawaguchi, T., Osatomi, K., Yamashita, H., Kabashima, T., & Uyeda, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107895200 · Cited by 424 · see citing works
Kim, Y. D., Park, K.-G., Lee, Y.-S., Park, Y.-Y., Kim, D.-K., Nedumaran, B., Jang, W. G., Cho, W.-J., Ha, J., Lee, I.-K., et al. (2008) · Diabetes · doi:10.2337/db07-0381 · Cited by 422 · see citing works
HORMONAL REGULATION OF HEPATIC GLUCONEOGENESIS AND GLYCOLYSIS
Pilkis, S. J., El‐Maghrabi, M. R., & Claus, T. H. (1988) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.57.070188.003543 · Cited by 404 · see citing works
The glucose-6-phosphatase system
SCHAFTINGEN, E. V., & Gerin, I. (2002) · Biochemical Journal · doi:10.1042/bj3620513 · Cited by 374 · see citing works
Kawaguchi, T., Takenoshita, M., Kabashima, T., & Uyeda, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.231370798 · Cited by 373 · see citing works
Im, S., Yousef, L., Blaschitz, C., Liu, J. Z., Edwards, R. A., Young, S. G., Raffatellu, M., & Osborne, T. F. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.04.001 · Cited by 357 · see citing works
Dentin, R., Girard, J. R., & Postic, C. (2004) · Biochimie · doi:10.1016/j.biochi.2004.11.008 · Cited by 328 · see citing works
Hepatic Glucose Sensing via the CREB Coactivator CRTC2
Dentin, R., Hedrick, S. A., Xie, J., Yates, J. R., & Montminy, M. (2008) · Science · doi:10.1126/science.1151363 · Cited by 319 · see citing works
REGULATION OF THE EXPRESSION OF LIPOGENIC ENZYME GENES BY CARBOHYDRATE
Towle, H. C., Kaytor, E. N., & Shih, H. (1997) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.17.1.405 · Cited by 302 · see citing works
The CREB coactivator CRTC2 links hepatic ER stress and fasting gluconeogenesis
Wang, Y., Vera, L. I., Fischer, W. H., et al. (2009) · Nature · doi:10.1038/nature08111 · Cited by 297 · see citing works
ChREBP: A Glucose-activated Transcription Factor Involved in the Development of Metabolic Syndrome
Iizuka, K., & Horikawa, Y. (2008) · Endocrine Journal · doi:10.1507/endocrj.k07e-110 · Cited by 222 · see citing works
CREB and FoxO1: two transcription factors for the regulation of hepatic gluconeogenesis
Oh, K., Han, H.-S., Kim, M.-J., & Koo, S. (2013) · BMB Reports · doi:10.5483/bmbrep.2013.46.12.248 · Cited by 221 · see citing works
Self-citationInositol-1,4,5-trisphosphate receptor regulates hepatic gluconeogenesis in fasting and diabetes
Wang, Y., Li, G., Goode, J., Paz, J. C., Ouyang, K., Screaton, R. A., Fischer, W. H., Chen, J., Tabas, I. A., & Montminy, M. (2012) · Nature · doi:10.1038/nature10988 · Cited by 211 · see citing works
ChREBP, but not LXRs, is required for the induction of glucose-regulated genes in mouse liver
Denechaud, P., Bossard, P., Lobaccaro, J. A., Millatt, L. J., Staels, B., Girard, J. R., & Postic, C. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34314 · Cited by 205 · see citing works
Regulation of Hepatic Gluconeogenesis by an ER-Bound Transcription Factor, CREBH
Lee, M., Chanda, D., Yang, J., Oh, H., Kim, S. S., Yoon, Y.-S., Hong, S., Park, K., Lee, I., Choi, C. S., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.02.016 · Cited by 194 · see citing works
Self-citationMolecular mechanisms of DAX1 action
Iyer, A. K., & McCabe, E. R. B. (2004) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2004.07.018 · Cited by 193 · see citing works
Direct Role of ChREBP·Mlx in Regulating Hepatic Glucose-responsive Genes
Ma, L., Tsatsos, N. G., & Towle, H. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413063200 · Cited by 190 · see citing works
FoxOs Function Synergistically to Promote Glucose Production
Haeusler, R. A., Kaestner, K. H., & Accili, D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.c110.175851 · Cited by 186 · see citing works
Pilkis, S. J., & Claus, T. H. (1991) · Annual Review of Nutrition · doi:10.1146/annurev.nu.11.070191.002341 · Cited by 177 · see citing works
Role of glycogen phosphorylase in liver glycogen metabolism
Agius, L. (2015) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2015.09.002 · Cited by 172 · see citing works
Targeted disruption of the CREB coactivator Crtc2 increases insulin sensitivity
Wang, Y., Inoue, H., Ravnskjær, K., Viste, K., Miller, N., Liu, Y., Hedrick, S. A., Vera, L. I., & Montminy, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914897107 · Cited by 167 · see citing works
Lee, J.-M., Seo, W., Song, K. H., Chanda, D., Kim, Y. D., Kim, D., Lee, M., Ryu, D., Kim, Y., Noh, J., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.134890 · Cited by 163 · see citing works
Self-citationA Phosphorylation Cascade Controls the Degradation of Active SREBP1*
Bengoechea-Alonso, M., & Ericsson, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807906200 · Cited by 144 · see citing works
Kim, D., Ryu, D., Koh, M., Lee, M., Lim, D., Kim, M. J., Kim, Y., Cho, W., Lee, C., Park, S. B., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.315168 · Cited by 136 · see citing works
Self-citationErion, D. M., Ignatova, I. D., Yonemitsu, S., Nagai, Y., Chatterjee, P., Weismann, D., Hsiao, J. J., Zhang, D., Iwasaki, T., Stark, R., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.10.007 · Cited by 108 · see citing works
Sterol regulatory element-binding protein 1 is negatively modulated by PKA phosphorylation
Lu, M. M., & Shyy, J. Y.-J. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00374.2005 · Cited by 89 · see citing works
Choi, D., Oh, K., Han, H.-S., Yoon, Y.-S., Jung, C.-Y., Kim, S., & Koo, S. (2012) · Hepatology · doi:10.1002/hep.25809 · Cited by 81 · see citing works
Self-citationModulation of Glucokinase Regulatory Protein: A Double-Edged Sword?
Brouwers, M. C. G. J., Jacobs, C., Bast, A., Stehouwer, C. D. A., & Schaper, N. C. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.08.004 · Cited by 78 · see citing works
Yoon, Y.-S., Lee, M., Ryu, D., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012665107 · Cited by 78 · see citing works
Glucose activation of ChREBP in hepatocytes occurs via a two-step mechanism
Tsatsos, N. G., & Towle, H. C. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.12.029 · Cited by 77 · see citing works
Kim, D., Gang, G.-T., Ryu, D., et al. (2013) · Diabetes · doi:10.2337/db12-0946 · Cited by 74 · see citing works
Salt-inducible Kinase Regulates Hepatic Lipogenesis by Controlling SREBP-1c Phosphorylation
Yoon, Y.-S., Seo, W., Lee, M., Kim, S., & Koo, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900096200 · Cited by 64 · see citing works
Self-citationLiver glycogen metabolism: An overview
van de Werve, G., & Jeanrenaud, B. (1987) · Diabetes/Metabolism Reviews · doi:10.1002/dmr.5610030104 · Cited by 62 · see citing works
Control of Liver Glycogen Synthase Activity and Intracellular Distribution by Phosphorylation
R�os, S., Garcı́a-Rocha, M., Domínguez, J. E., Ferrer, J. C., & Guinovart, J. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808576200 · Cited by 58 · see citing works
Zinker, B. A., Mika, A. K., Nguyen, P., Wilcox, D. M., Öhman, L., von Geldern, T. W., Opgenorth, T. J., & Jacobson, P. B. (2007) · Metabolism · doi:10.1016/j.metabol.2006.10.021 · Cited by 48 · see citing works
Xie, Y., Lee, O., Nedumaran, B., et al. (2008) · Biochemical Journal · doi:10.1042/bj20080782 · Cited by 48 · see citing works
Bedford, D. C., Kasper, L. H., Wang, R., Chang, Y., Green, D. R., & Brindle, P. K. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.06.010 · Cited by 43 · see citing works
The role of cyclic AMP in rapid and long-term regulation of gluconeogenesis and glycolysis.
Pilkis, S. J., Claus, T. H., & El‐Maghrabi, M. R. (1988) · PubMed · Cited by 43 · see citing works
Nedumaran, B., Hong, S.-P., Xie, Y., Kim, Y., Seo, W., Lee, M., Lee, C. H., Koo, S., & Choi, H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.034660 · Cited by 42 · see citing works
Self-citationIdentification and function of phosphorylation in the glucose-regulated transcription factor ChREBP
Tsatsos, N. G., Davies, M. N., O’Callaghan, B. L., et al. (2008) · Biochemical Journal · doi:10.1042/bj20071156 · Cited by 39 · see citing works
Han, H.-S., Jung, C.-Y., Yoon, Y.-S., Choi, S., Choi, D., Kang, G. W., Park, K., Kim, S., & Koo, S. (2014) · Science Signaling · doi:10.1126/scisignal.2004479 · Cited by 37 · see citing works
Self-citationInsulin-Inducible SMILE Inhibits Hepatic Gluconeogenesis
Lee, J.-M., Seo, W., Han, H.-S., et al. (2015) · Diabetes · doi:10.2337/db15-0249 · Cited by 25 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Glucose transporters in adipose tissue, liver, and skeletal muscle in metabolic health and disease
Chadt, A., & Al-Hasani, H. (2020) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-020-02417-x · Cited by 510 · see citing works
Hepatokines and metabolism: Deciphering communication from the liver
Jensen-Cody, S. O., & Potthoff, M. J. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101138 · Cited by 252 · see citing works
Regulation of Skeletal Muscle Glucose Transport and Glucose Metabolism by Exercise Training
Evans, P. L., McMillin, S. L., Weyrauch, L. A., & Witczak, C. A. (2019) · Nutrients · doi:10.3390/nu11102432 · Cited by 190 · see citing works
Tao, T., Deng, P., Wang, Y., Zhang, X., Guo, Y., Chen, W., & Qin, J. (2022) · Advanced Science · doi:10.1002/advs.202103495 · Cited by 178 · see citing works
Mitochondrial Dysfunction and Neurodegeneration in Lysosomal Storage Disorders
Plotegher, N., & Duchen, M. R. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.12.003 · Cited by 161 · see citing works
International society of sports nutrition position stand: nutritional concerns of the female athlete
Sims, S. T., Kerksick, C. M., Smith-Ryan, A. E., Janse de Jonge, X. A. K., Hirsch, K. R., Arent, S. M., Hewlings, S. J., Kleiner, S. M., Bustillo, E., Tartar, J. L., et al. (2023) · Journal of the International Society of Sports Nutrition · doi:10.1080/15502783.2023.2204066 · Cited by 91 · see citing works
Distinct hepatocyte identities in liver homeostasis and regeneration
Chen, F., Schönberger, K., & Tchorz, J. S. (2023) · JHEP Reports · doi:10.1016/j.jhepr.2023.100779 · Cited by 30 · see citing works
Exercise as a Therapeutic Strategy for Obesity: Central and Peripheral Mechanisms
Zhang, Y., Wang, R., Liu, T., & Wang, R. (2024) · Metabolites · doi:10.3390/metabo14110589 · Cited by 27 · see citing works
Liver organoids: Current advances and future applications for hepatology
Kim, Y., Kang, M., Mamo, M. G., Adisasmita, M., Huch, M., & Choi, D. (2025) · Clinical and Molecular Hepatology · doi:10.3350/cmh.2024.1040 · Cited by 26 · see citing works
Obesity and Exercise: New Insights and Perspectives
James, N. M., & Stanford, K. I. (2025) · Endocrine Reviews · doi:10.1210/endrev/bnaf017 · Cited by 20 · see citing works
- Authors
- Han, H.-S., Kang, G., Kim, J. S., Choi, B. H., & Koo, S.-H.
- Affiliations
- Korea University (KR)
- Corresponding author
- Koo, Seung-Hoi
- Venue
- Experimental & Molecular Medicine
- Published
- 2016-03-11
- Volume
- 48
- Issue
- 3
- Pages
- e218-e218
- ISSN
- 1226-3613 (ISSN-L)
- 2092-6413
- PMC
- PMC4892876
- OpenAlex
- W2296585153
- Cited by
- 835
- References
- 76
- Citations by year
- 2026: 96 · 2025: 137 · 2024: 126 · 2023: 118 · 2022: 121 · 2021: 110 · 2020: 64 · 2019: 31 · 2018: 19 · 2017: 12 · 2016: 1
- FWCI
- 1.90
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Experimental & Molecular Medicine (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- National Research Foundation (2015R1A5A1009024)
- Korea University
- National Research Foundation of Korea (2015R1A2A1A01006687, NRF-2015R1A5A1009024, NRF‐2012M3A9B6055345, 2015R1A5A1009024, NRF-2015R1A2A1A01006687)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Rheumatology › Glycogen Storage Diseases and Myoclonus
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diet, Metabolism, and Disease
- Keywords
- glucose homeostasis, hepatic glucose metabolism, glycogen synthesis, glycogenolysis, glycolysis, gluconeogenesis, transcription factors, SREBP-1c, ChREBP, CREB, FOXO1, post-translational regulation, allosteric regulation, fatty acid synthesis, gene expression regulation
- MeSH terms
- Animals, Gluconeogenesis, Glucose, Glycolysis, Homeostasis, Humans, Liver
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review