The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Regulation of mammalian acetyl-CoA carboxylase
Abstract
Acetyl-CoA carboxylase (ACC) plays a critical role in the regulation of fatty acid metabolism and its two isoforms, ACCalpha and ACCbeta, appear to have distinct functions in the control of fatty acid synthesis and fatty acid oxidation, respectively. They are regulated by similar short-term mechanisms of allosteric activation by citrate, and reversible phosphorylation and inactivation, and there is clearly interaction between these mechanisms. AMP-activated protein kinase is the important physiological ACC kinase for both isoforms and yet there is a potential physiological role for cAMP-dependent protein kinase in the hormonally mediated inactivation of ACCalpha, and phosphorylation of ACCbeta in its unique N-terminus.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Acetyl CoA carboxylase (ACC), as the rate-limiting enzyme in de-novo lipogenesis, exists around the mitochondria and controls β-oxidation of fatty acids in the mitochondria [13].”
From Regulatory Efficacy of the Polyunsaturated Fatty Acids from Microalgae Spirulina platensis on Lipid Metabolism and Gut Microbiota in High-Fat Diet Rats (2018) · cites this paper as [13]
In the citing paper
“In low energy conditions, AMP-activated protein kinase (AMPK) phosphorylates and inhibits ACC, decreasing malonyl CoA and increasing CPT1 activity.54”
From The multifaceted contributions of mitochondria to cellular metabolism (2018) · cites this paper as [54]
Citations
Cites
Regulation of fatty acid synthesis and oxidation by the AMP-activated protein kinase
Hardie, D. G., & Pan, D. A. (2002) · Biochemical Society Transactions · doi:10.1042/bst0301064 · Cited by 574
Flagged first, then by citations
Cited by
Sorted by citations
The multifaceted contributions of mitochondria to cellular metabolism
Spinelli, J. B., & Haigis, M. C. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0124-1 · Cited by 1,935
Steinberg, G. R., & Kemp, B. E. (2009) · Physiological Reviews · doi:10.1152/physrev.00011.2008 · Cited by 1,672
AMPK and mTOR in Cellular Energy Homeostasis and Drug Targets
Inoki, K., Kim, J., & Guan, K. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134537 · Cited by 818
Gene networks driving bovine milk fat synthesis during the lactation cycle
Bionaz, M., & Loor, J. J. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-366 · Cited by 786
Recent insights into hepatic lipid metabolism in non-alcoholic fatty liver disease (NAFLD)
Musso, G., Gambino, R. J., & Cassader, M. (2008) · Progress in Lipid Research · doi:10.1016/j.plipres.2008.08.001 · Cited by 691
De novo lipogenesis in the liver in health and disease: more than just a shunting yard for glucose
Sanders, F., & Griffin, J. L. (2015) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12178 · Cited by 585
Acylcarnitines: Nomenclature, Biomarkers, Therapeutic Potential, Drug Targets, and Clinical Trials
Dambrova, M., Makrecka‐Kuka, M., Kuka, J., Vilšķe̅rsts, R., Nordberg, D. O. T., Attwood, M. M., Smesny, S., Şen, Z. D., Guo, A. C., Oler, E., et al. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000408 · Cited by 549
Savage, D. B. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27300 · Cited by 447
Nonalcoholic fatty liver disease: molecular mechanisms for the hepatic steatosis
Koo, S. (2013) · Clinical and Molecular Hepatology · doi:10.3350/cmh.2013.19.3.210 · Cited by 421
Jaswal, J. S., Keung, W., Wang, W., Ussher, J. R., & Lopaschuk, G. D. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.01.015 · Cited by 401
Integrating canonical and metabolic signalling programmes in the regulation of T cell responses
Pollizzi, K. N., & Powell, J. D. (2014) · Nature reviews. Immunology · doi:10.1038/nri3701 · Cited by 395
Lipid metabolic enzymes: emerging drug targets for the treatment of obesity
Shi, Y., & Burn, P. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1469 · Cited by 345
Cheng, S., Fryer, L. G. D., Carling, D., & Shepherd, P. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c300534200 · Cited by 340
Glycerolipid Metabolism and Signaling in Health and Disease
Prentki, M., & Madiraju, S. R. M. (2008) · Endocrine Reviews · doi:10.1210/er.2008-0007 · Cited by 331
Choi, C. S., Savage, D. B., Abu-Elheiga, L., Liu, Z.-X., Kim, S., Kulkarni, A., Distefano, A., Hwang, Y.-J., Reznick, R. M., Codella, R., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706794104 · Cited by 325
AMPK-Mediated Regulation of Lipid Metabolism by Phosphorylation
Wang, Q., Liu, S., Zhai, A., Zhang, B., & Tian, G. (2018) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b17-00724 · Cited by 324
Tan, B., Yin, Y., Liu, Z., Xin-guo, L., Xu, H.-J., Kong, X., Huang, R., Tang, W., Shinzato, I., Smith, S. B., et al. (2008) · Amino Acids · doi:10.1007/s00726-008-0148-0 · Cited by 315
Malonyl-CoA, a Key Signaling Molecule in Mammalian Cells
Saggerson, D. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155434 · Cited by 301
Targeting protein modifications in metabolic diseases: molecular mechanisms and targeted therapies
Wu, X., Xu, M., Geng, M., Chen, S., Little, P. J., Xu, S., & Weng, J. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01439-y · Cited by 295
AMPK signaling and its targeting in cancer progression and treatment
Hsu, C.-C., Peng, D., Cai, Z., & Lin, H. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.04.006 · Cited by 265
Acetyl-CoA Carboxylases and Diseases
Wang, Y., Yu, W., Li, S., Guo, D., He, J., & Wang, Y. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.836058 · Cited by 238
Tan, B., Yin, Y., Liu, Z., Tang, W., Xu, H.-J., Kong, X., Xin-guo, L., Yao, K., WanTing, G., Smith, S. B., et al. (2010) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2010.03.012 · Cited by 191
Ashino, N. G., Saito, K. N., Souza, F. D., Nakutz, F. S., Roman, E. A., Velloso, L. A., Torsoni, A. S., & Torsoni, M. A. (2011) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2010.12.011 · Cited by 191
Ceddia, R. B. (2005) · International Journal of Obesity · doi:10.1038/sj.ijo.0803025 · Cited by 184
Histological evaluation of AMPK signalling in primary breast cancer
Hadad, S. M., Baker, L., Quinlan, P., Robertson, K. E., Bray, S. E., Thomson, G., Kellock, D., Jordan, L. B., Purdie, C. A., Hardie, D. G., et al. (2009) · BMC Cancer · doi:10.1186/1471-2407-9-307 · Cited by 177
Gómez‐Zorita, S., Fernández‐Quintela, A., Macarulla, M. T., Aguirre, L., Hijona, E., Bujanda, L., Milagro, F. I., Martínez, J. A., & Portillo, M. P. (2011) · British Journal Of Nutrition · doi:10.1017/s0007114511002753 · Cited by 163
Functional and structural properties of mammalian acyl-coenzyme A thioesterases
Kirkby, B., Roman, N., Kobe, B., Kellie, S., & Forwood, J. K. (2010) · Progress in Lipid Research · doi:10.1016/j.plipres.2010.04.001 · Cited by 163
Metabolic regulation of citrate and iron by aconitases: role of iron–sulfur cluster biogenesis
Tong, W.-H., & Rouault, T. A. (2007) · BioMetals · doi:10.1007/s10534-006-9047-6 · Cited by 165
Dependence of Arbuscular-Mycorrhizal Fungi on Their Plant Host for Palmitic Acid Synthesis
Trépanier, M., Bécard, G., Moutoglis, P., WILLEMOT, C., Gagné, S., Avis, T. J., & Rioux, J.-A. (2005) · Applied and Environmental Microbiology · doi:10.1128/aem.71.9.5341-5347.2005 · Cited by 157
Assifi, M. M., Suchánková, G., Constant, S., Prentki, M., Saha, A. K., & Ruderman, N. B. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00144.2005 · Cited by 159
Qu, Y.-Y., Zhao, R., Zhang, H., Zhou, Q., Xu, F., Zhang, X., Xu, W., Shao, N., Zhou, S.-X., Dai, B., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-1023 · Cited by 139
Ginsenoside Rb1 reduces fatty liver by activating AMP-activated protein kinase in obese rats
Shen, L., Xiong, Y., Wang, D. Q. ‐., Howles, P. N., Basford, J. E., Wang, J., Xiong, Y., Hui, D. Y., Woods, S. C., & Liu, M. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m035907 · Cited by 126
Treating the metabolic syndrome: acetyl-CoA carboxylase inhibition
Harwood, H. J., Jr. (2005) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.9.2.267 · Cited by 129
Desoyé, G., & Herrera, E. (2020) · Progress in Lipid Research · doi:10.1016/j.plipres.2020.101082 · Cited by 133
Spencer, C. M., Schafer, X., Moorman, N. J., & Munger, J. C. (2011) · Journal of Virology · doi:10.1128/jvi.02630-10 · Cited by 125
Fediuc, S., Gaidhu, M. P., & Ceddia, R. B. (2005) · Journal of Lipid Research · doi:10.1194/jlr.m500438-jlr200 · Cited by 121
Changes in white adipose tissue metabolism induced by resveratrol in rats
Alberdi, G., Rodríguez, V. M., Miranda, J., Macarulla, M. T., Arias, N., Andrés‐Lacueva, C., & Portillo, M. P. (2011) · Nutrition & Metabolism · doi:10.1186/1743-7075-8-29 · Cited by 117
Naidu, P. B., Uddandrao, V. V. S., Naik, R. R., Suresh, P., Meriga, B., Begum, M. S., Pandiyan, R., & Saravanan, G. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.10.007 · Cited by 116
Jones, J. E. C., Esler, W. P., Patel, R. S., Lanba, A., Vera, N. B., Pfefferkorn, J. A., & Vernochet, C. (2017) · PLoS ONE · doi:10.1371/journal.pone.0169566 · Cited by 113
Regulation of fatty acid uptake and metabolism in L6 skeletal muscle cells by resistin
Palanivel, R., & Sweeney, G. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.08.011 · Cited by 111
Aguer, C., Mercier, J. G., Man, C. Y. W., Metz, L., Bordenave, S., Lambert, K., Jean, E., Lantier, L., Bounoua, L., Brun, J. ‐., et al. (2010) · Diabetologia · doi:10.1007/s00125-010-1708-x · Cited by 113
STK11/LKB1 Modulation of the Immune Response in Lung Cancer: From Biology to Therapeutic Impact
Tostivint, E. P., Lugat, A., Fontenau, J.-F., Denis, M. G., & Bennouna, J. (2021) · Cells · doi:10.3390/cells10113129 · Cited by 107
Gaidhu, M. P., Fediuc, S., & Ceddia, R. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602992200 · Cited by 111
Park, S. Y., Lee, S. W., Lee, S. Y., Hong, K. W., Bae, S. S., Kim, K., & Kim, C. D. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01135 · Cited by 111
Hepatic lipid metabolic pathways modified by resveratrol in rats fed an obesogenic diet
Alberdi, G., Rodríguez, V. M., Macarulla, M. T., Miranda, J., Churruca, I., & Portillo, M. P. (2012) · Nutrition · doi:10.1016/j.nut.2012.09.011 · Cited by 107
The role of AMP-activated protein kinase in regulating white adipose tissue metabolism
Ceddia, R. B. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.06.014 · Cited by 105
Mukai, T., Egawa, M., Takeuchi, T., Yamashita, H., & Kusudo, T. (2017) · FEBS Open Bio · doi:10.1002/2211-5463.12240 · Cited by 105
High Fat Activates O-GlcNAcylation and Affects AMPK/ACC Pathway to Regulate Lipid Metabolism
Pang, Y., Xu, X., Xiang, X., Li, Y., Zhao, Z., Li, J., Gao, S., Liu, Q., Mai, K., & Ai, Q. (2021) · Nutrients · doi:10.3390/nu13061740 · Cited by 109
Inoue, T., Inoguchi, T., Sonoda, N., Hendarto, H., Makimura, H., Sasaki, S., Yokomizo, H., Fujimura, Y., Miura, D., & Takayanagi, R. (2015) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2015.03.026 · Cited by 103
Li, T.-T., Liu, Y.-Y., Wan, X.-Z., Huang, Z.-R., Liu, B., & Zhao, C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103075 · Cited by 103
Regulatory roles for L-arginine in reducing white adipose tissue
Tan, B. (2012) · Frontiers in bioscience · doi:10.2741/4047 · Cited by 106
Hutchinson, D. S., Chernogubova, E., Dallner, O. S., Cannon, B., & Bengtsson, T. (2005) · Diabetologia · doi:10.1007/s00125-005-1936-7 · Cited by 101
Stahmann, N., Woods, A., Spengler, K., Heslegrave, A., Bauer, R., Krause, S., Viollet, B., Carling, D., & Heller, R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.108688 · Cited by 100
Parim, B., Nemani, H., Meriga, B., Mehar, S. K., Potana, S., & Ramgopalrao, S. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.07.008 · Cited by 101
Mizuarai, S., Miki, S., Araki, H., Takahashi, K., & Kotani, H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503152200 · Cited by 96
Role of malonyl-CoA in heart disease and the hypothalamic control of obesity
Folmes, C. D. L., & LOPASCHUK, G. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.10.008 · Cited by 98
Kamel, W., Sugihara, E., Nobusue, H., Yamaguchi‐Iwai, S., Onishi, N., Maki, K., Fukuchi, Y., Matsuo, K., Muto, A., Saya, H., et al. (2016) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-16-0499 · Cited by 94
Hulea, L., Gravel, S., Morita, M., Cargnello, M., Uchenunu, O., Im, Y. K., Lehuédé, C., Ma, E. H., Leibovitch, M., McLaughlan, S., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.09.001 · Cited by 91
Li, H., Ge, Y., Zheng, X., & Zhang, L. (2008) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.04.036 · Cited by 96
Hall, D. T., Griss, T., Ma, J. F., Sanchez, B. J., Sadek, J., Tremblay, A. M. K., Mubaid, S., Omer, A., Ford, R. J., Bedard, N., et al. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708307 · Cited by 88
Obestatin as a regulator of adipocyte metabolism and adipogenesis
Gurriarán‐Rodríguez, U., Al–Massadi, O., Roca-Rivada, A., Crujeiras, A. B., Gallego, R., Pardo, M., Seoane, L. M., Pazos, Y., Casanueva, F. F., & Camiña, J. P. (2010) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2010.01192.x · Cited by 90
AMPK‐dependent hormonal regulation of whole‐body energy metabolism
Dzamko, N. L., & Steinberg, G. R. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01969.x · Cited by 90
The Role of Mitochondrial Fat Oxidation in Cancer Cell Proliferation and Survival
Oliveira, M., & Liesa, M. (2020) · Cells · doi:10.3390/cells9122600 · Cited by 89
Liu, S., Du, M., Tu, Y., You, W., Chen, W., Liu, G., Li, J., Wang, Y., Lu, Z., Wang, T., et al. (2022) · Animal nutrition · doi:10.1016/j.aninu.2022.09.003 · Cited by 90
Singh, S. P., Niemczyk, M., Saini, D., Awasthi, S., Zimniak, L., & Zimniak, P. (2008) · Biochemistry · doi:10.1021/bi702124u · Cited by 82
AMP-Activated Protein Kinase Activation by Adrenoceptors in L6 Skeletal Muscle Cells
Hutchinson, D. S., & Bengtsson, T. (2006) · Diabetes · doi:10.2337/diabetes.55.03.06.db05-0901 · Cited by 79
Steinberg, G. R., Macaulay, S. L., Febbraio, M. A., & Kemp, B. E. (2006) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y06-005 · Cited by 80
Mosaoa, R., Kasprzyk-Pawelec, A., Fernandez, H. R., & Avantaggiati, M. L. (2021) · Biomolecules · doi:10.3390/biom11020141 · Cited by 80
Zhao, Y., Li, J.-Y., Yin, L. W., Feng, L., Liu, Y., Jiang, W., Wu, P., Zhao, J., Chen, D., Zhou, X., et al. (2018) · Aquaculture · doi:10.1016/j.aquaculture.2018.12.050 · Cited by 71
SATHASİVAMPİLLAİ, S. V., Rajamanoharan, P. R. S., Munday, M. R., & Heinrich, M. (2016) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2016.07.053 · Cited by 68
Self-citationNOX4 Pathway as a Source of Selective Insulin Resistance and Responsiveness
Wu, X., & Williams, K. J. (2012) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.111.244525 · Cited by 67
Lorenz, M. W., & Anand, A. N. (2004) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.20002 · Cited by 67
Metformin activation of AMPK suppresses AGE-induced inflammatory response in hNSCs
Chung, M.-M., Nicol, C. J., Cheng, Y.-C., Lin, K.-H., Chen, Y.-L., Pei, D., Lin, C.-H., Shih, Y.-N., Yen, C.-H., Chen, S.-J., et al. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.01.017 · Cited by 66
Yu, M., Li, Z., Rong, T. Z., Wang, G., Liu, Z., Chen, W., Li, J., Li, J., & Ma, X. (2020) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-020-00484-9 · Cited by 66
Citrate, a Ubiquitous Key Metabolite with Regulatory Function in the CNS
Westergaard, N., Waagepetersen, H. S., Belhage, B., & Schousboe, A. (2017) · Neurochemical Research · doi:10.1007/s11064-016-2159-7 · Cited by 68
Murrieta, C. M., Hess, B. W., Scholljegerdes, E. J., Engle, T. E., HOSSNER, K. L., Moss, G. E., & Rule, D. C. (2006) · Journal of Animal Science · doi:10.2527/jas.2005-677 · Cited by 61
Ou, T., Hsu, M., Chan, K., Huang, C., Ho, H.-H., & Wang, C. (2011) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.4489 · Cited by 61
Metabolism Characteristics of Th17 and Regulatory T Cells in Autoimmune Diseases
Qin, Y., Gao, C., & Luo, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.828191 · Cited by 68
Park, J.-Y., Kim, Y.-H., Im, J. A., & Lee, H. (2015) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-015-0709-1 · Cited by 58
Watson, E. V., Yilmaz, L. S., & Walhout, A. J. M. (2015) · Annual Review of Genetics · doi:10.1146/annurev-genet-112414-055257 · Cited by 55
Kampe, K., Sieber, J., Orellana, J. M., Mundel, P. H., & Jehle, A. W. (2013) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00454.2013 · Cited by 56
Han, J. D. J., Li, L., Wang, D., & Ma, H. (2016) · Lipids in Health and Disease · doi:10.1186/s12944-016-0208-5 · Cited by 55
Recent Development in Acetyl-CoA Carboxylase Inhibitors and their Potential as Novel Drugs
Wu, X., & Huang, T. (2020) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0312 · Cited by 55
Shi, L., Shi, L., Song, G., Zhang, H.-F., Hu, Z., Wang, C., & Zhang, D. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.06.013 · Cited by 56
The dynamic organization of fungal acetyl-CoA carboxylase
Hunkeler, M., Stuttfeld, E., Hagmann, A., Imseng, S., & Maier, T. (2016) · Nature Communications · doi:10.1038/ncomms11196 · Cited by 56
Chemical Genetics of Acetyl-CoA Carboxylases
Zu, X., Zhong, J., Luo, D., Tan, J., Zhang, Q., Wu, Y., Liu, J., Cao, R., Wen, G., & Cao, D. (2013) · Molecules · doi:10.3390/molecules18021704 · Cited by 54
Steenberg, D. E., Jørgensen, N. B., Birk, J. B., Sjøberg, K. A., Kiens, B., Richter, E. A., & Wojtaszewski, J. F. P. (2018) · The Journal of Physiology · doi:10.1113/jp276735 · Cited by 53
The molecular associations between the SnRK1 complex and carbon/nitrogen metabolism in plants
Han, C., Wang, H., Shi, W., & Bai, M. (2023) · New Crops · doi:10.1016/j.ncrops.2023.12.003 · Cited by 54
Liu, Y., Li, F., He, L., Tan, B., Deng, J., Kong, X., Li, Y., Geng, M., Yin, Y., & Wu, G. (2015) · British Journal Of Nutrition · doi:10.1017/s0007114514004310 · Cited by 51
Wei, H., Cai, W., Liu, H., Han, D. H., Zhu, X., Yang, Y., Jin, J., & Xie, S.-Q. (2019) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2019.111552 · Cited by 52
Brose, S. A., Marquardt, A. L., & Golovko, M. Y. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12617 · Cited by 53
Chen, D., Banerjee, S., Cui, Q. C., Kong, D., Sarkar, F. H., & Dou, Q. P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047186 · Cited by 50
The regulation of AMPK signaling in a natural state of profound metabolic rate depression
Ramnanan, C. J., McMullen, D. C., Groom, A. G., & Storey, K. B. (2009) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-009-0246-7 · Cited by 48
Pan, M., Yang, G., Li, S., Li, M., Tsai, M., Wu, J.-C., Badmaev, V., Ho, C., & Lai, C. (2017) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201601104 · Cited by 48
Arabolaza, A. L., Shillito, M. E., Lin, T., Diacovich, L., Melgar, M. M., Pham, H., Amick, D. L., Gramajo, H. C., & Tsai, S. (2010) · Biochemistry · doi:10.1021/bi1005305 · Cited by 48
Loussouarn, C., Pers, Y., Bony, C., Jørgensen, C., & Noël, D. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.623973 · Cited by 47
Xiao, X., Li, H., Qi, X., Wang, Y., Xu, C., Liu, G., Wen, G., & Liu, J. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.06.003 · Cited by 47
Weatherly, S. C., Volrath, S., & Elich, T. D. (2004) · Biochemical Journal · doi:10.1042/bj20031960 · Cited by 45
Complex Formation and Regulation of Escherichia coli Acetyl-CoA Carboxylase
Broussard, T. C., Price, A. E., Laborde, S. M., & Waldrop, G. L. (2013) · Biochemistry · doi:10.1021/bi4000707 · Cited by 48
Lipotoxic and inflammatory phenotypes in rats with uncontrolled metabolic syndrome and nephropathy
Dominguez, J. H., Wu, P., Packer, C. S., Temm, C. J., & Kelly, K. J. (2007) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00021.2007 · Cited by 46
Metadata
- Authors
- Munday, M. R.
- Affiliations
- University of London (GB)
- Corresponding author
- Munday, M. R.
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2002-11-01
- Volume
- 30
- Issue
- 6
- Pages
- 1059-1064
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- OpenAlex
- W1978058114
- Cited by
- 301
- References
- 1
- Citations by year
- 2026: 8 · 2025: 13 · 2024: 9 · 2023: 19 · 2022: 18 · 2021: 13 · 2020: 18 · 2019: 13 · 2018: 17 · 2017: 12 · 2016: 17 · 2015: 17 · 2014: 6 · 2013: 14 · 2012: 10
- FWCI
- 2.38
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Transactions (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- acetyl-CoA carboxylase, fatty acid synthesis, fatty acid oxidation, reversible phosphorylation, AMPK, protein kinase A, N-terminal phosphorylation, enzyme regulation, mammalian metabolism
- MeSH terms
- Acetyl-CoA Carboxylase, Animals, Humans, Kinetics, Phosphorylation, Structure-Activity Relationship, Gene Expression Regulation, Enzymologic, Protein Structure, Tertiary, Protein Isoforms
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