Serine Palmitoyltransferase 1, Human

Known as: LCB 1, SPT 1, Long Chain Base Biosynthesis Protein 1 
Serine palmitoyltransferase 1 (473 aa, ~53 kDa) is encoded by the human SPTLC1 gene. This protein plays a role in the biosynthesis of sphingolipids.
National Institutes of Health

Topic mentions per year

Topic mentions per year

1982-2014
01219822014

Papers overview

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2014
2014
Sphingolipids is characterized to be composed of a unique fatty amino alcohol, so-called long-chain base (LCB) or sphingoid base… (More)
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2012
2012
Diagnosed allergic disease (any) 1.26 0.67-2.37 .47 1.34 0.68-2.63 .40 0.956 0.44-2.08 .91 1.07 0.80-1.44 .63 Doctor-diagnosed… (More)
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2010
2010
The present work tested the hypothesis that a short-term dietary deficiency of magnesium (Mg) (21 days) in rats would result in… (More)
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2007
2007
Sphingolipid biosynthesis commences with the condensation of L-serine and palmitoyl-CoA to produce 3-ketodihydrosphingosine (KDS… (More)
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2006
2006
Metformin has been shown to increase fatty acid oxidation, an effect mediated by AMP activated protein kinase (AMPK). We… (More)
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Highly Cited
1998
Highly Cited
1998
Lysenin, a hemolytic protein derived from the earthworm Eisenia foetida, has a high affinity for sphingomyelin. Chinese hamster… (More)
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1996
1996
Synthesis of the ceramide portion of sphingolipids in animals has been hypothesized to be tightly regulated thereby controlling… (More)
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1994
1994
The first and committed step in synthesis of the ceramide moiety of sphingolipids is catalyzed by serine palmitoyltransferase (EC… (More)
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1988
1988
Serine palmitoyltransferase (EC 2.3.1.50) catalyzes the condensation of L-serine and palmitoyl-CoA to yield 3-ketosphinganine in… (More)
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1985
1985
Serine palmitoyltransferase [EC 2.3.1.50] catalyzes the first unique reaction of sphingolipid biosynthesis. To determine whether… (More)
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