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Identification of essential residues for the catalytic function of 85-kDa cytosolic phospholipase A2. Probing the role of histidine, aspartic acid, cysteine, and arginineCrystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoformThe Saccharomyces cerevisiae Lipin homolog is a Mg2+-dependent phosphatidate phosphatase enzyme.Analysis of the kinetic mechanism of recombinant human isoprenylcysteine carboxylmethyltransferase (Icmt)A retrospective: use of Escherichia coli as a vehicle to study phospholipid synthesis and functionPhospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic interventionStructure/Function Relationships of Adipose Phospholipase A2 Containing a Cys-His-His Catalytic TriadMechanistic Characterization of the Tetraacyldisaccharide-1-phosphate 4′-Kinase LpxK Involved in Lipid A BiosynthesisSaccharomyces cerevisiae contains a Type II phosphoinositide 4-kinaseThe Saccharomyces cerevisiae PHM8 gene encodes a soluble magnesium-dependent lysophosphatidic acid phosphatase.A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase.YEH2/YLR020c encodes a novel steryl ester hydrolase of the yeast Saccharomyces cerevisiae.Regulation of profilin localization in Saccharomyces cerevisiae by phosphoinositide metabolism.Characterization of the yeast actin patch protein App1p phosphatidate phosphataseCharacterization and function in vivo of two novel phospholipases B/lysophospholipases from Saccharomyces cerevisiae.Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae.The Saccharomyces cerevisiae LSB6 gene encodes phosphatidylinositol 4-kinase activity.Characterization of the yeast DGK1-encoded CTP-dependent diacylglycerol kinase.Cholesterol is superior to 7-ketocholesterol or 7 alpha-hydroxycholesterol as an allosteric activator for acyl-coenzyme A:cholesterol acyltransferase 1Interfacial kinetic analysis of the tumour suppressor phosphatase, PTEN: evidence for activation by anionic phospholipidsMathematical modeling and validation of the ergosterol pathway in Saccharomyces cerevisiaeMembrane Topology and Biochemical Characterization of the Escherichia coli BacA Undecaprenyl-Pyrophosphate PhosphataseMuLK, a eukaryotic multi-substrate lipid kinaseCharacterization of murine sphingosine-1-phosphate phosphohydrolaseAn alternative route for UDP-diacylglucosamine hydrolysis in bacterial lipid A biosynthesis.Lipin 2 binds phosphatidic acid by the electrostatic hydrogen bond switch mechanism independent of phosphorylation.Phosphorylation of lipin 1 and charge on the phosphatidic acid head group control its phosphatidic acid phosphatase activity and membrane association.Molecular characterization of a phosphatidylcholine-hydrolyzing phospholipase C.Development of Potent and Selective Inhibitors for Group VIA Calcium-Independent Phospholipase A2 Guided by Molecular Dynamics and Structure-Activity Relationships.The Escherichia coli gene encoding the UDP-2,3-diacylglucosamine pyrophosphatase of lipid A biosynthesis.Control of phospholipid synthesis by phosphorylation of the yeast lipin Pah1p/Smp2p Mg2+-dependent phosphatidate phosphatase.Incorporation of extracellular fatty acids by a fatty acid kinase-dependent pathway in Staphylococcus aureus.Mechanisms underlying Plk1 polo-box domain-mediated biological processes and their physiological significance.EmrE dimerization depends on membrane environment.Characterization of the human LPIN1-encoded phosphatidate phosphatase isoforms.Phosphatidate degradation: phosphatidate phosphatases (lipins) and lipid phosphate phosphatases.HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly.The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity.Mammalian Mg2+-independent phosphatidate phosphatase (PAP2) displays diacylglycerol pyrophosphate phosphatase activity.
P2860
Q24311432-B4D3FDE2-20A1-4312-9060-FBCB0508C54FQ24321337-E34FDAFB-9CC8-4899-8F90-840268A2C350Q24324045-561AE291-5EFD-4E92-84AF-8CDD7E0DD8A7Q24542354-E15BC2FF-2917-42DE-9A70-EA25EBBE1C2AQ24792001-39A4E88F-C149-43C8-8B2A-E9B0CBF010CBQ26995227-8EEF3013-3D16-4C08-AF2F-127A36B781C6Q26997377-6407CF84-1084-44DD-ACF7-90078B3EC499Q27671706-09F3B375-859B-4685-B6C8-5B1EDCB86285Q27676710-EF3EBFB1-6881-4205-818B-2590E4D47837Q27929859-4F715DE0-2BC4-4177-ABBF-3C972E23D5B5Q27930790-45920218-9D67-443A-9B60-8FB3C94FE2F4Q27930968-90AEEF4C-085F-480C-8733-8A86D782F6FBQ27932534-FFBE21B8-CFED-477C-B11A-EFDEB42E69F6Q27934768-201F8CB0-E207-4285-B3FE-F30191C3FB6FQ27934916-8B92898A-632E-4185-A4E0-34C3E7B8F756Q27936743-B3599ED8-B030-4AF6-97F4-04994A10EA35Q27937888-96808981-20DD-44A8-9461-F0E3CB8AF270Q27938509-1C7697E5-5BEF-46EB-A775-F59469D71CE4Q27940004-AACD8544-0D53-44B3-BF05-9613D01E9AA7Q28203844-ADF39A2C-EF0E-419F-B34C-67B17A905DC6Q28203936-8D297FDC-F1BF-4AB3-A4C9-478DC41B119AQ28478408-ED066692-A479-4523-A637-FF0674B40D53Q28550889-8535FBB9-965A-477D-A6C4-BF3D9FA9AAB5Q28588452-8359BE49-AD63-4194-B096-289B43FFC2D4Q28592202-D8CA2258-275F-4C8D-A253-4515AA445A31Q30090089-AA8D7E36-5C40-402B-BCDF-87286426C2D2Q30384605-69BA147D-27D3-4EE7-A0A5-762A3CBDE9C8Q30413930-11E9981E-DC88-4A63-AAEA-D71E72BE2F31Q30665377-9041409B-78E0-4EE0-8237-170704AE731AQ30785490-86B55DB9-B9C7-4D86-96FE-77848720BEEEQ31051692-27DD53EB-5453-4E51-A90B-4521D2B420C0Q33257316-27DDC15E-160E-4B80-AC3A-600EA0F83208Q33554927-C56EC023-90B4-437E-ADF9-9296FDE1E8D8Q33574269-E8A1BBF7-F32E-4988-9764-41357790A7D5Q33771551-E019326D-25A3-4C67-919C-5AC4BE9423FBQ33825194-F0505D28-5593-4375-A899-88AC8D3428F6Q33871978-2C18F4E9-220E-4023-83C4-4F8CBD3819F9Q33948566-AD6C2DDB-E822-45BA-829E-087B0D7A53A8Q34408937-3A08E96D-8C7E-4105-B6AA-3C4894C83E0FQ34421337-AAEC5110-1287-48DE-90AE-29AE727F9A83
P2860
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Lipid signaling enzymes and surface dilution kinetics.
@en
type
label
Lipid signaling enzymes and surface dilution kinetics.
@en
prefLabel
Lipid signaling enzymes and surface dilution kinetics.
@en
P2093
P2860
P356
P1476
Lipid signaling enzymes and surface dilution kinetics.
@en
P2093
P2860
P304
18711-18714
P356
10.1074/JBC.270.32.18711
P407
P577
1995-08-01T00:00:00Z