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1 pe that was corrected by transformation with serine palmitoyltransferase.
2 hesis of complex sphingolipids downstream of serine palmitoyltransferase.
3 imiting enzyme in sphingolipid biosynthesis, serine palmitoyltransferase.
4 but unlike myriocin FTY720 does not inhibit serine palmitoyltransferase.
5 the activities of both ceramide synthase and serine palmitoyltransferase.
6 we revealed aberrant gene expressions (e.g., serine palmitoyltransferase 1 [SPTLC1] and ceramide synt
7 epsin F (OR = 1.10, p-value = 7.16E-05), and serine palmitoyltransferase 2 (OR = 0.86, p-value = 1.00
8 s and knockdowns affecting either subunit of serine palmitoyltransferase, a key enzyme in ceramide an
10 ntial substrate specificity of virus-encoded serine palmitoyltransferase, a key enzyme of sphingolipi
11 sphingolipids, apparently via modulation of serine palmitoyltransferase, a rate-limiting enzyme in d
12 were protected from diet-induced increase in serine palmitoyltransferase, acid sphingomyelinase, and
13 tion that associates with increased monocyte serine palmitoyltransferase activity and chemotaxis towa
14 are synthesized from alanine via promiscuous serine palmitoyltransferase activity and correlate with
15 These mutations are dominant and decrease serine palmitoyltransferase activity by 50% when the wil
23 n, isolation, and analyses of the Toxoplasma serine palmitoyltransferase, an enzyme catalyzing the fi
26 ion of [(3)H]palmitate, a substrate for both serine palmitoyltransferase and ceramide synthase, into
27 ation of [3H]palmitate, a substrate for both serine palmitoyltransferase and ceramide synthase, into
28 isin B1, specific inhibitors of key enzymes (serine palmitoyltransferase and dihydroceramide synthase
29 thase activity (over 2-fold, p = 0.01); both serine palmitoyltransferase and glucosylceramide synthas
30 ion are the ORMDL proteins that are bound to serine palmitoyltransferase and mediate feedback inhibit
31 hytosphingosine bypasses the requirement for serine palmitoyltransferase and restores proteolysis.
32 generation through the de novo pathway (e.g. serine palmitoyltransferase) and via the hydrolysis of s
33 hingolipid biosynthetic pathway (mediated by serine palmitoyltransferase), and at least regulated, de
34 is due to impaired homeostatic regulation of serine palmitoyltransferase as responsible for defects i
36 o regulate sphingolipid synthesis by binding serine palmitoyltransferase, but its role in inflammatio
37 n SPTSSA impaired the negative regulation of serine palmitoyltransferase by ORMDLs leading to excessi
38 zymes known as the alpha-oxoamine synthases, serine palmitoyltransferase catalyzes the committed step
43 cycloserine, and 4-HPR transiently activated serine palmitoyltransferase, demonstrating that 4-HPR in
45 is work demonstrates that one subunit of the serine palmitoyltransferase enzyme, SPTLC1, but not subu
47 ace of L-serine, the mutant HSAN1-associated serine palmitoyltransferase generates deoxysphingolipids
48 While the putative homologues of giardial serine palmitoyltransferase (gSPT) subunit genes (gspt-1
49 two isoforms of the small subunits of human serine palmitoyltransferase (hssSPTs) that activate the
50 as evolutionarily related to the prokaryotic serine palmitoyltransferase, identified in the Sphingomo
51 A-stimulated RAW264.7 cells (and mutation of serine palmitoyltransferase in CHO-LYB cells); furthermo
52 e for de novo sphingoid base biosynthesis by serine palmitoyltransferase in the transient G0/G1 arres
53 ySLs) are atypical sphingolipids formed when serine palmitoyltransferase incorporates L-alanine inste
54 we1 kinase renders mutant cells sensitive to serine palmitoyltransferase inhibition due to impaired s
55 esis pharmacologically through exposure to a serine palmitoyltransferase inhibitor (myriocin) show st
57 lipid synthesis pathway was tested using the serine palmitoyltransferase inhibitor myriocin, the sphi
60 oamine synthases are soluble homodimers, but serine palmitoyltransferase is a membrane-associated enz
63 ort here that the gene encoding a subunit of serine palmitoyltransferase is located within the HSN1 l
64 This result suggests that the activation of serine palmitoyltransferase is the event responsible for
65 1-100, which harbors a temperature-sensitive serine palmitoyltransferase, lacked increased de novo ge
66 n orthologue to be a functional, homodimeric serine palmitoyltransferase localized to the endoplasmic
67 f ceramide, through the rate-limiting enzyme serine palmitoyltransferase long chain (Sptlc)-2, is req
68 canonically composed of 2 subunits, SPTLC1 (serine palmitoyltransferase long chain base subunit 1) a
69 erase long chain base subunit 1) and SPTLC2 (serine palmitoyltransferase long chain base subunit 2).
70 y a more recently described subunit, SPTLC3 (serine palmitoyltransferase long chain base subunit 3).
71 onstrated that the ER-resident human protein serine palmitoyltransferase long chain-1 (SPTLC1), which
72 olling enzyme of de novo ceramide synthesis, serine palmitoyltransferase long-chain base subunit 1 (S
73 itary neuropathies are dominant mutations in serine palmitoyltransferase, long chain base subunit 1 (
74 the gene was identified as SPTLC1, encoding serine palmitoyltransferase, long chain base subunit-1.
76 ysical interaction between Orm1 and Orm2 and serine palmitoyltransferase, responsible for the first c
77 ynthase, and ISP-1, myriocin an inhibitor of serine palmitoyltransferase, significantly attenuated th
78 AHR bound and activated the gene promoter of serine palmitoyltransferase small subunit A (SPTSSA), wh
80 precursors and intermediates, and increased serine palmitoyltransferase (SPT) and fatty acid (FA) el
81 member of a family that negatively regulates serine palmitoyltransferase (SPT) and thus biosynthesis
82 disrupt the normal homeostatic regulation of serine palmitoyltransferase (SPT) by ORMDL proteins, res
91 teins function as regulatory subunits of the serine palmitoyltransferase (SPT) complex, which is the
92 ted to a few bacterial phyla that encode the serine palmitoyltransferase (SPT) enzyme, which catalyse
94 with the SPOTS complex, which is composed of serine palmitoyltransferase (SPT) enzymes and accessory
100 volved, we utilized two models: heterozygous serine palmitoyltransferase (SPT) subunit 2 (Sptlc2) gen
101 osomucoid-like proteins (ORMs) interact with serine palmitoyltransferase (SPT) to negatively regulate
102 yridoxal-5'-phosphate (PLP)-dependent enzyme serine palmitoyltransferase (SPT) which is a promising t
103 ndensation of alanine with palmitoyl-CoA via serine palmitoyltransferase (SPT), as indicated by incor
104 n SPTLC1 gene, encoding the Lcb1p subunit of serine palmitoyltransferase (SPT), cause hereditary sens
107 s with either L-cycloserine, an inhibitor of serine palmitoyltransferase (SPT), or fumonisin B(1), an
108 -chain base 1 (LCB1), one of two subunits of serine palmitoyltransferase (SPT), the enzyme catalyzing
109 ere labeled with [14C]serine, a substrate of serine palmitoyltransferase (SPT), the enzyme catalyzing
110 not directly alter the in vitro activity of serine palmitoyltransferase (SPT), the enzyme responsibl
111 apid decrease in LCB levels, indicating that serine palmitoyltransferase (SPT), the first and rate-li
112 nesis, the ehv050 gene predicted to encode a serine palmitoyltransferase (SPT), the first and rate-li
113 ot associated with changes in mRNA levels of serine palmitoyltransferase (SPT), the rate-limiting enz
115 osynthesis in Leishmania, we have focused on serine palmitoyltransferase (SPT), which catalyses the f
118 ipid biosynthesis is initiated by the enzyme serine palmitoyltransferase (SPT), which resides in the
131 ion is catalysed by the PLP-dependent enzyme serine palmitoyltransferase (SPT; EC 2.3.1.50), which is
132 of the Lcb1p subunit of yeast and mammalian serine palmitoyltransferases (SPT) were investigated.
136 pressed the expression of SPTLC1 and SPTLC2 (serine palmitoyltransferase [SPT] long-chain base subuni
137 trypanosomatid protozoan Leishmania lacking serine palmitoyltransferase (spt2-) and SLs grow well, a
138 he same prototypical fold found in bacterial serine palmitoyltransferases (Spts), enveloping the PLP
140 e report that HSAN-I-associated mutations in serine palmitoyltransferase subunit SPTLC2 dampened huma
141 t A (SPTSSA), which encodes a subunit of the serine palmitoyltransferase that catalyzes the first and
142 th myriocin (50 nm), a specific inhibitor of serine palmitoyltransferase (the first step in de novo s
143 n of Sptlc1 Sptlc1 is an obligate subunit of serine palmitoyltransferase, the enzyme responsible for
145 synthesis that form a conserved complex with serine palmitoyltransferase, the first and rate-limiting
146 is, increase the activity and mRNA levels of serine palmitoyltransferase, the first committed step in
147 rtially reduced by myriocin, an inhibitor of serine palmitoyltransferase, the first committed step in
149 ngolipids since it is the main substrate for serine palmitoyltransferase, the initial and rate-limiti
150 investigation using a labeled substrate for serine palmitoyltransferase, the rate-limiting enzyme in
151 treated with myriocin, a potent inhibitor of serine palmitoyltransferase, the rate-limiting enzyme in
153 synthase, but not by ISP-1, an inhibitor of serine palmitoyltransferase, the rate-limiting step in t
154 xysphingolipids are produced when the enzyme serine palmitoyltransferase uses l-alanine instead of l-
155 lytic activity and homeostatic regulation of serine palmitoyltransferase was investigated in human em
156 cted a deletion mutant of BF2461, a putative serine palmitoyltransferase whose yeast homolog catalyze
158 t lack Nogo-B, pharmacological inhibition of serine palmitoyltransferase with myriocin reinstates end