A mammalian homolog of the yeast LCB1 encodes a component of serine palmitoyltransferase, the enzyme catalyzing the first step in sphingolipid synthesis
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P1343
The SPTLC3 subunit of serine palmitoyltransferase generates short chain sphingoid basesAnthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent processThe External Aldimine Form of Serine Palmitoyltransferase: STRUCTURAL, KINETIC, AND SPECTROSCOPIC ANALYSIS OF THE WILD-TYPE ENZYME AND HSAN1 MUTANT MIMICSStructural insights into the enzymatic mechanism of serine palmitoyltransferase from Sphingobacterium multivorumYeast cells lacking the ARV1 gene harbor defects in sphingolipid metabolism. Complementation by human ARV1.Serine palmitoyltransferase (SPT) deficient mice absorb less cholesterolDe novo synthesis of sphingolipids is required for cell survival by down-regulating c-Jun N-terminal kinase in Drosophila imaginal discs.Initial steps of Shigella infection depend on the cholesterol/sphingolipid raft-mediated CD44-IpaB interactionDe novo sphingolipid biosynthesis: a necessary, but dangerous, pathway.Hereditary sensory neuropathy type 1 mutations confer dominant negative effects on serine palmitoyltransferase, critical for sphingolipid synthesis.Reducing plasma membrane sphingomyelin increases insulin sensitivity.Rafts can trigger contact-mediated secretion of bacterial effectors via a lipid-based mechanism.The topology of the Lcb1p subunit of yeast serine palmitoyltransferase.Integrative transformation system for the metabolic engineering of the sphingoid base-producing yeast Pichia ciferrii.Molecular characterization of membrane-associated soluble serine palmitoyltransferases from Sphingobacterium multivorum and Bdellovibrio stolpiiOverexpression of the wild-type SPT1 subunit lowers desoxysphingolipid levels and rescues the phenotype of HSAN1Intracellular APP Domain Regulates Serine-Palmitoyl-CoA Transferase Expression and Is Affected in Alzheimer's Disease.Sphingolipid and glycosphingolipid metabolic pathways in the era of sphingolipidomics.Control of phosphatidylserine biosynthesis through phosphatidylserine-mediated inhibition of phosphatidylserine synthase I in Chinese hamster ovary cells.Sphingolipid synthesis and scavenging in the intracellular apicomplexan parasite, Toxoplasma gondiiInhibition of serine palmitoyltransferase reduces Aβ and tau hyperphosphorylation in a murine model: a safe therapeutic strategy for Alzheimer's diseaseRole of Intracellular Lipid Logistics in the Preferential Usage of Very Long Chain-Ceramides in GlucosylceramideLiver-specific deficiency of serine palmitoyltransferase subunit 2 decreases plasma sphingomyelin and increases apolipoprotein E levels.Structural, mechanistic and regulatory studies of serine palmitoyltransferase.Sphingolipid metabolism and interorganellar transport: localization of sphingolipid enzymes and lipid transfer proteins.The role of ORMDL proteins, guardians of cellular sphingolipids, in asthma.Enhanced serine palmitoyltransferase expression in proliferating fibroblasts, transformed cell lines, and human tumors.Involvement of VIP36 in intracellular transport and secretion of glycoproteins in polarized Madin-Darby canine kidney (MDCK) cells.Functional characterization of the promoter for the mouse SPTLC2 gene, which encodes subunit 2 of serine palmitoyltransferase.De novo-synthesized ceramide is involved in cannabinoid-induced apoptosis.Mammalian cell mutants resistant to a sphingomyelin-directed cytolysin. Genetic and biochemical evidence for complex formation of the LCB1 protein with the LCB2 protein for serine palmitoyltransferase.Effects of sphingolipid synthesis inhibition on cholesterol gallstone formation in C57BL/6J mice.A water-soluble homodimeric serine palmitoyltransferase from Sphingomonas paucimobilis EY2395T strain. Purification, characterization, cloning, and overproduction.Mutations in the Lcb2p subunit of serine palmitoyltransferase eliminate the requirement for the TSC3 gene in Saccharomyces cerevisiae.Purification and characterization of Chinese hamster phosphatidylserine synthase 2.Characterization of free endogenous C14 and C16 sphingoid bases from Drosophila melanogaster.Modulation of amyloid precursor protein cleavage by cellular sphingolipids.Structural characterization of suppressor lipids by high-resolution mass spectrometry.Acceleration of the substrate Calpha deprotonation by an analogue of the second substrate palmitoyl-CoA in Serine Palmitoyltransferase.Quantification of 3-ketodihydrosphingosine using HPLC-ESI-MS/MS to study SPT activity in yeast Saccharomyces cerevisiae.
P2860
Q24319169-6BE7BFEF-9DEF-43FA-B3EB-141281071077Q24675885-20B33952-5CA0-4805-A245-49E6245483CBQ27654958-A25C4245-4B07-43CE-B188-213B6B5BE5C5Q27656285-07AC6273-C6AF-4F6F-8EF5-2112CBDC9A5CQ27940092-1C9FCC55-4F2F-413C-AC40-7ED59E8C883AQ28510763-D5DCC7D1-1AB1-4F24-B3F6-43456013320DQ33959886-F54171BF-FF6F-4AFC-BB75-7D829B1E82BBQ34091098-CC7077B0-E138-4126-A264-CE8BF0F7CF5AQ34128457-1C066CCE-477C-4625-9251-2ECCF45E2C67Q34157831-7EE76E45-F38E-42D8-94A2-54B0300AD0C4Q34208250-55ED37F2-BDD6-4B32-AFE0-23A5533F5D47Q34347987-09FD496A-D759-48C9-BD17-D701B71F40E6Q34359002-81B4E6D9-67A3-4939-B0FA-D8E562D5099EQ34540102-FEA48808-4E29-4B72-8398-AA21B40C30A6Q34635803-810B6DCA-065F-424B-84D1-4FC187FFE229Q35013547-66755F68-160B-4491-B997-A508F2E8CB5CQ35030310-3BDBB9E1-5F0D-4280-B0AA-3FAF9B2A1B45Q35324757-C5D3194B-3294-415C-A7E2-AC2CC3A6DF06Q36466022-CF95C969-5C0B-465C-9CE3-5143A0373640Q36775799-9588640A-9CB4-43DB-A43F-B19B18F342CFQ36836935-401FF014-612D-4F7E-9B92-F82F3811FB15Q37377548-77E27118-D808-4AED-A5F6-54CA1EC00207Q37446891-4FAE95F2-64AF-42A4-9368-07F40E775974Q38012195-29C503C3-A9DD-4ADF-86FD-00783346CECBQ38266425-652C4AE2-CAA6-410F-B5E0-1BF67C0724E3Q38771128-D6EE7153-E0FB-4541-A0A3-2F2DF9DFC6F2Q40646901-9B528539-92A5-47FD-BDEF-649121FE6560Q40747672-6D28221D-3D37-4ECE-9C3D-DFD2EBAAA6D2Q41345293-2383392F-F31F-4089-A8C6-D834EFBD85BBQ41775676-901CEADF-FF11-442A-873A-E96D6623293FQ42819525-308365DB-23DD-4D35-A4B7-8EB657AFAA80Q42995625-B70C54CA-4A2D-4E37-8BA3-E9BF6CCDD26BQ43560399-7EADE890-742F-49EA-85A1-EF4D206830D7Q44107796-2808E345-905C-4B0C-9B04-45054374781CQ44545614-324BDA2C-AA3B-44C3-8329-C6E539F9B34CQ44586590-93555D54-4818-4B6A-9DDA-64C5251FE0FFQ44722885-DC7CE55A-B1F2-4319-AF49-E3BF9A40DE25Q46507091-949DE56F-EE5E-4654-8D91-C214438B7991Q46826656-CC603A28-154F-4620-BE78-7B08823E33B9Q47722430-746D0333-4007-4AAD-8834-22EF2ACC63BC
P2860
A mammalian homolog of the yeast LCB1 encodes a component of serine palmitoyltransferase, the enzyme catalyzing the first step in sphingolipid synthesis
description
1997 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1997
@ast
im Dezember 1997 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1997/12/19)
@sk
vědecký článek publikovaný v roce 1997
@cs
wetenschappelijk artikel (gepubliceerd op 1997/12/19)
@nl
наукова стаття, опублікована в грудні 1997
@uk
name
A mammalian homolog of the yea ...... step in sphingolipid synthesis
@ast
A mammalian homolog of the yea ...... step in sphingolipid synthesis
@en
A mammalian homolog of the yea ...... step in sphingolipid synthesis
@nl
type
label
A mammalian homolog of the yea ...... step in sphingolipid synthesis
@ast
A mammalian homolog of the yea ...... step in sphingolipid synthesis
@en
A mammalian homolog of the yea ...... step in sphingolipid synthesis
@nl
prefLabel
A mammalian homolog of the yea ...... step in sphingolipid synthesis
@ast
A mammalian homolog of the yea ...... step in sphingolipid synthesis
@en
A mammalian homolog of the yea ...... step in sphingolipid synthesis
@nl
P2093
P921
P3181
P356
P1476
A mammalian homolog of the yea ...... step in sphingolipid synthesis
@en
P2093
M. M. Nagiec
M. Nishijima
R. C. Dickson
P304
32108–32114
P3181
P356
10.1074/JBC.272.51.32108
P407
P4510
P577
1997-12-19T00:00:00Z