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.
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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
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Oral hydroxycitrate supplementation enhances glycogen synthesis in exercised human skeletal muscle
Cheng, I.-S., Huang, S.-W., Lu, H.-C., Wu, C.-L., Chu, Y.-C., Lee, S.-D., Huang, C.-Y., & Kuo, C.-H. (2012) · British Journal of Nutrition · doi:10.1017/s0007114511003862 · Cited by 42
Liu, T., Gou, L., Yan, S., & Huang, T. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.8700 · Cited by 15
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
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