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West Ashley Library
Closed for Staff Day
Phone: (843) 766-6635
Wando Mount Pleasant Library
Closed for Staff Day
Phone: (843) 805-6888
Village Library
Closed for Staff Day
Phone: (843) 884-9741
St. Paul's/Hollywood Library
Closed for Staff Day
Phone: (843) 889-3300
Otranto Road Library
Closed for Staff Day
Phone: (843) 572-4094
Mt. Pleasant Library
Closed for Staff Day
Phone: (843) 849-6161
McClellanville Library
Closed for Staff Day
Phone: (843) 887-3699
Keith Summey North Charleston Library
Closed for Staff Day
Phone: (843) 744-2489
John's Island Library
Closed for Staff Day
Phone: (843) 559-1945
Hurd/St. Andrews Library
Closed for Staff Day
Phone: (843) 766-2546
Folly Beach Library
Closed for Staff Day
Phone: (843) 588-2001
Dorchester Road Library
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Phone: (843) 552-6466
John L. Dart Library
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Phone: (843) 722-7550
Baxter-Patrick James Island
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Phone: (843) 795-6679
Main Library
Closed for Staff Day
Phone: (843) 805-6930
Bees Ferry West Ashley Library
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Miss Jane's Building (Edisto Library Temporary Location)
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Compartmentalization of Mammalian Folate-Mediated One-Carbon Metabolism.
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- Author(s): Tibbetts, Anne S.; Appling, Dean R.
- Source:
Annual Review of Nutrition. 2010, Vol. 30 Issue 1, p57-81. 35p. 4 Diagrams. - Source:
- Additional Information
- Subject Terms:
- Abstract: The recognition that mitochondria participate in folate-mediated one-carbon metabolism grew out of pioneering work beginning in the 1950s from the laboratories of D.M. Greenberg, C.G. Mackenzie, and G. Kikuchi. These studies revealed mitochondria as the site of oxidation of one-carbon donors such as serine, glycine, sarcosine, and dimethylglycine. Subsequent work from these laboratories and others demonstrated the participation of folate coenzymes and folate-dependent enzymes in these mitochondrial processes. Biochemical and molecular genetic approaches in the 1980s and 1990s identified many of the enzymes involved and revealed an interdependence of cytoplasmic and mitochondrial one-carbon metabolism. These studies led to the development of a model of eukaryotic one-carbon metabolism that comprises parallel cytosolic and mitochondrial pathways, connected by one-carbon donors such as serine, glycine, and formate. Sequencing of the human and other mammalian genomes has facilitated identification of the enzymes that participate in this intercompartmental one-carbon metabolism, and animal models are beginning to clarify the roles of the cytoplasmic and mitochondrial isozymes of these enzymes. Identifying the mitochondrial transporters for the one-carbon donors and elucidating how flux through these pathways is controlled are two areas ripe for exploration. [ABSTRACT FROM AUTHOR]
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