Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells
about
The complex life of simple sphingolipidsInhibition of sphingomyelin synthase (SMS) affects intracellular sphingomyelin accumulation and plasma membrane lipid organizationCasein kinase I{gamma}2 down-regulates trafficking of ceramide in the synthesis of sphingomyelinAll members in the sphingomyelin synthase gene family have ceramide phosphoethanolamine synthase activityThe multigenic sphingomyelin synthase familyCalmodulin is involved in the Ca2+-dependent activation of ceramide kinase as a calcium sensorAdenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 increases the atherogenic potential in miceFunctional characterization of enzymes catalyzing ceramide phosphoethanolamine biosynthesis in miceER residency of the ceramide phosphoethanolamine synthase SMSr relies on homotypic oligomerization mediated by its SAM domainMacrophage sphingomyelin synthase 2 deficiency decreases atherosclerosis in micePharmacologic inhibition of sphingomyelin synthase (SMS) activity reduces apolipoprotein-B secretion from hepatocytes and attenuates endotoxin-mediated macrophage inflammation.Cell-free synthesis and functional characterization of sphingolipid synthases from parasitic trypanosomatid protozoa.Sphingomyelin synthases regulate protein trafficking and secretionReducing plasma membrane sphingomyelin increases insulin sensitivity.Limonoid compounds inhibit sphingomyelin biosynthesis by preventing CERT protein-dependent extraction of ceramides from the endoplasmic reticulum.Ceramide phosphoethanolamine biosynthesis in Drosophila is mediated by a unique ethanolamine phosphotransferase in the Golgi lumenMitochondrial dysfunction and increased reactive oxygen species impair insulin secretion in sphingomyelin synthase 1-null mice.Increased oxidative stress impairs adipose tissue function in sphingomyelin synthase 1 null mice.A method for visualization of "omic" datasets for sphingolipid metabolism to predict potentially interesting differences.Dynamic modification of sphingomyelin in lipid microdomains controls development of obesity, fatty liver, and type 2 diabetesSphingomyelin synthase 1-generated sphingomyelin plays an important role in transferrin trafficking and cell proliferation.Sphingomyelin synthase 2 (SMS2) deficiency attenuates LPS-induced lung injuryCeramide transfer protein function is essential for normal oxidative stress response and lifespan.Integral membrane lipid phosphatases/phosphotransferases: common structure and diverse functions.Attenuated free cholesterol loading-induced apoptosis but preserved phospholipid composition of peritoneal macrophages from mice that do not express group VIA phospholipase A2.Regulation of cell migration by sphingomyelin synthases: sphingomyelin in lipid rafts decreases responsiveness to signaling by the CXCL12/CXCR4 pathway.Impact of sphingomyelin synthase 1 deficiency on sphingolipid metabolism and atherosclerosis in mice.Cellular lipidomicsRole of membrane sphingomyelin and ceramide in platform formation for Fas-mediated apoptosisEpidermal sphingolipids: metabolism, function, and roles in skin disorders.On the effects of topical synthetic pseudoceramides: comparison of possible keratinocyte toxicities provoked by the pseudoceramides, PC104 and BIO391, and natural ceramidesSphingomyelin synthase 1 activity is regulated by the BCR-ABL oncogenePsychosine-triggered endomitosis is modulated by membrane sphingolipids through regulation of phosphoinositide 4,5-bisphosphate production at the cleavage furrow.Developmentally regulated sphingolipid synthesis in African trypanosomesLipid metabolism in Trypanosoma bruceiDifferential regulation of sphingomyelin synthesis and catabolism in oligodendrocytes and neurons.Regulation of ceramide biosynthesis by TOR complex 2.Sphingomyelin synthases regulate production of diacylglycerol at the Golgi.Sphingolipid topology and the dynamic organization and function of membrane proteins.Ceramide signaling in mammalian epidermis.
P2860
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P248
Q24537161-4D3DB902-C1B4-42C2-A1C7-667895AA9D96Q24647417-CBCF9A0F-B49C-4A5E-AE87-0A2D670C530FQ24654811-EAA7A286-E7F9-4452-9F3A-7A0CDC4120C2Q28117543-8E603AF8-F94D-4C4C-82A4-7AB877579C99Q28257423-A3E7EF2D-B8ED-4A78-8059-D0959EA1BC2FQ28275392-10BD3660-87B9-42E6-ABD9-493B9CE01C3EQ28299660-B33BC96B-3F16-41F4-AC6F-823CA6D43EE5Q28506403-36BE0458-3617-4AD3-800E-8E62ADD97085Q28818276-4D0B4B9F-33FC-4634-A3FB-8BBB7058D73BQ30490333-B8A5F4D5-12C2-430B-91BC-E57D1C9BC6FCQ33916433-1BCAB2B0-66DB-4154-B2B3-60EA49BD8694Q33966843-AE3E8D38-28C6-4E87-AC62-AAF33AB39E7FQ34042764-412BE0EC-DAAC-4F22-98FE-2A133A70DFC7Q34208250-E8C63C52-4EA4-4E7E-AE54-580CD81D1844Q34273268-EBDC39A2-EDAA-4B6F-B6BC-58EFF8CE0CD5Q34330339-6C6E7ADA-37C8-4D8D-BEE0-B4B492B1BCA7Q34537129-7794927C-8FF3-4A92-BBE1-0E38B9DC19F0Q34674948-DBE4F925-B10D-4F74-AE9B-89AE45A51C42Q34955765-754500FA-E8A3-453F-9514-AF0778A87EDBQ35150259-75831343-10DE-4306-8D4C-E1C2DC16DDE6Q35371671-A06FF3F4-5CDB-4D6B-A939-96FF714E5513Q35771622-C8EBDEC1-91CA-45D6-A946-DB61C1D74604Q35854971-58263FB0-075F-4569-A79A-7CB7C5F7AFADQ36085014-D0588A89-1691-4B7D-9BA6-E7D366EF9DADQ36097195-9CE12107-54F1-48F9-87C1-99EEAB0C7026Q36211046-FDD1865E-FB07-4526-BACF-0166C754A4F9Q36239748-8038CFA4-8FD9-421C-9463-56204189D4E8Q36247057-A3B70790-4104-4B2C-9BA3-F2D974899B13Q36403166-BBB17D5A-2B7A-4C63-8BE7-64D24D653299Q36589543-89C4E0F3-BFDB-41D5-B965-C1714C2901AFQ36696383-FF897647-26A8-4A07-9AAE-B5A8C376CD65Q36744139-00406CDF-86F1-4FE0-8684-223C09F73363Q37052732-163DA7C8-1F05-4D5A-A535-7654C20AF06FQ37069574-930EA5FC-F564-484B-B090-1AE27A64EF18Q37098733-8CBBDA8A-5293-445D-8F2D-4EBC7F363E4CQ37286940-778EF523-31D9-4391-BAC0-339491399DB9Q37439524-CC3EFD78-DBBC-4034-937E-9D4ABE24A70CQ37444626-06319577-56ED-486C-BAAA-5C2A866D4419Q37616697-467A685E-DF02-4807-92DE-5EA6ECE43C10Q37619251-80F6EA20-15E3-4A97-B246-B8E7BCCD21E4
P2860
Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells
description
2004 nî lūn-bûn
@nan
2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Expression cloning of a human ...... thase-defective lymphoid cells
@ast
Expression cloning of a human ...... thase-defective lymphoid cells
@en
Expression cloning of a human ...... thase-defective lymphoid cells
@en-gb
Expression cloning of a human ...... thase-defective lymphoid cells
@nl
type
label
Expression cloning of a human ...... thase-defective lymphoid cells
@ast
Expression cloning of a human ...... thase-defective lymphoid cells
@en
Expression cloning of a human ...... thase-defective lymphoid cells
@en-gb
Expression cloning of a human ...... thase-defective lymphoid cells
@nl
prefLabel
Expression cloning of a human ...... thase-defective lymphoid cells
@ast
Expression cloning of a human ...... thase-defective lymphoid cells
@en
Expression cloning of a human ...... thase-defective lymphoid cells
@en-gb
Expression cloning of a human ...... thase-defective lymphoid cells
@nl
P2093
P921
P3181
P356
P1476
Expression cloning of a human ...... thase-defective lymphoid cells
@en
P2093
Hisanori Umehara
Michihiko Miyaji
Shohei Yamaoka
Toshiro Okazaki
Toshiyuki Kitano
P304
P3181
P356
10.1074/JBC.M401205200
P407
P577
2004-04-30T00:00:00Z