about
Golgi localization and functional expression of human uridine diphosphataseA yeast Golgi E-type ATPase with an unusual membrane topology.Human monocyte derived dendritic cells express functional P2X and P2Y receptors as well as ecto-nucleotidasesAutotaxin is an exoenzyme possessing 5'-nucleotide phosphodiesterase/ATP pyrophosphatase and ATPase activitiesDetermination of native oligomeric state and substrate specificity of rat NTPDase1 and NTPDase2 after heterologous expression in Xenopus oocytesPurification, cloning, and expression of an apyrase from the bed bug Cimex lectularius. A new type of nucleotide-binding enzyme.Molecular cloning of the chicken oviduct ecto-ATP-diphosphohydrolase.The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II.Cellular function and molecular structure of ecto-nucleotidases.Requirement of Cys399 for processing of the human ecto-ATPase (NTPDase2) and its implications for determination of the activities of splice variants of the enzyme.Continuous intravenous infusion of ATP in humans yields large expansions of erythrocyte ATP pools but extracellular ATP pools are elevated only at the start followed by rapid declines.Activation of human eosinophils via P2 receptors: novel findings and future perspectives.Ectonucleotidases in solid organ and allogeneic hematopoietic cell transplantationComplementary DNA cloning and sequencing of the chicken muscle ecto-ATPase. Homology with the lymphoid cell activation antigen CD39.Immunolocalization of the ecto-ATPase and ecto-apyrase in chicken gizzard and stomach. Purification and N-terminal sequence of the stomach ecto-apyrase.Adenosine and blood platelets.Neuromodulation: purinergic signaling in respiratory control.Therapeutic potentials of ecto-nucleoside triphosphate diphosphohydrolase, ecto-nucleotide pyrophosphatase/phosphodiesterase, ecto-5'-nucleotidase, and alkaline phosphatase inhibitors.Purinergic receptors and nucleotide processing ectoenzymes: Their roles in regulating mesenchymal stem cell functions.Cholesterol-dependent lipid assemblies regulate the activity of the ecto-nucleotidase CD39.Evidence for coordinated induction and repression of ecto-5'-nucleotidase (CD73) and the A2a adenosine receptor in a human B cell line.Cloning and expression of apyrase gene from Ancylostoma caninum in Escherechia coli.Ecto-ATP diphosphohydrolase/CD39 is overexpressed in differentiated human melanomas.New insights on the regulation of the adenine nucleotide pool of erythrocytes in mouse modelsExtracellular metabolism of nucleotides in the nervous system.Mammalian plasma membrane ecto-nucleoside triphosphate diphosphohydrolase 1, CD39, is not active intracellularly. The N-glycosylation state of CD39 correlates with surface activity and localization.ire-1-dependent transcriptional up-regulation of a lumenal uridine diphosphatase from Caenorhabditis elegans.Various N-glycoforms differentially upregulate E-NTPDase activity of the NTPDase3/CD39L3 ecto-enzymatic domain.Lipopolysaccharide treatment modifies pH- and cation-dependent ecto-ATPase activity of endothelial cells.ATP crossing the cell plasma membrane generates an ionic current in xenopus oocytes.Assignment of ecto-nucleoside triphosphate diphosphohydrolase-1/cd39 expression to microglia and vasculature of the brain.Defective ATP breakdown activity related to an ENTPD1 gene mutation demonstrated using 31P NMR spectroscopy.Functional characterization of rat ecto-ATPase and ecto-ATP diphosphohydrolase after heterologous expression in CHO cells.Magnesium-Dependent Ecto-ATP Diphosphohydrolase Activity in Leishmania donovani.
P2860
Q24309506-34D990A3-897B-4587-BF8F-EC0CACC4C549Q27937264-AB4E6929-DB3C-44A3-A827-CDEE0B664CFFQ28138370-40FDED27-367B-46A9-AD01-42C9EFF1987BQ28301252-691A8C41-554B-4468-91F1-A7288248610FQ28571699-066CAE31-45A3-4680-81C0-3486EFEE8690Q31980341-61A2FB2A-A0DA-4D05-BA4E-829B414B0CA8Q32060630-78774CC3-4AB5-4EC4-8A90-98B93E039E4DQ33867954-55D74F08-E51F-4FF1-8429-A3A98386019DQ34031794-7B3CE4A2-4BDC-4550-B297-96975E4CFD66Q34218222-BF9FDDBD-B465-4284-9F6A-2D9829BC4050Q35587830-D0608B24-4B11-4049-9DAF-A7C8C2F7E2B1Q36294569-8AA94FCC-BFEC-4ADB-B22F-10F969C99315Q36350059-FB0DBACF-E523-4906-87A4-6FAC00F82923Q36842053-015A6BF5-E357-410B-9BAD-99841E45E5D1Q36882348-3B8011BB-4FF9-4DC3-A109-02BD30D60869Q37864112-BBEDE725-29C8-49F2-9881-FD1BA9B4504FQ38110513-5EBB7462-CD6F-41A8-9EC6-A2368E1BE025Q38151635-75E6C0F8-EE17-4B26-95D3-12848D2B176FQ38207600-72631E72-CF4B-451F-96AF-5CAFA7067672Q38326346-3FADB7BB-46B7-485D-B95D-4F56805228CFQ40652135-CC1AA969-F7FC-4EC8-B7E3-60EBFBF9A3D4Q40704278-57ABCF0A-6467-4B47-A0D7-F80E7CC3D016Q41020104-23194FF4-AB9C-4C05-9D70-3D967C16F4B9Q41136916-EDD29B3F-6E64-4FFE-AFD1-4430E5599160Q41456052-686FA0B8-B5B1-4817-B3F9-6AC1D4530049Q43730427-9F1E6D3B-E6BA-4294-8A08-ABC559B21BB8Q44854775-AE33EBE0-C969-4ACE-9D56-8025E5C28219Q47732889-158AE203-D892-4D36-906D-88940C363D11Q48279493-E5EEF812-F845-4F86-B3F0-A07C3D6028A7Q48892875-8DDE82E5-A75C-4AED-B948-E6060049D0C6Q49144649-02CF5919-931F-4BE7-9A1A-5EE56BE22C88Q50516122-6986ED3D-06D3-4B4B-BCC9-51D73E9E61AAQ50519006-CC272BF7-BCDC-42ED-99A0-4F9C019A8079Q51536256-5E58F925-E52B-4A66-AB93-C27E6C233C1F
P2860
description
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
im April 1996 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published in Journal of Biological Chemistry
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована у квітні 1996
@uk
name
CD39 Is an Ecto-(Ca,Mg)-apyrase
@en
CD39 Is an Ecto-(Ca,Mg)-apyrase
@nl
type
label
CD39 Is an Ecto-(Ca,Mg)-apyrase
@en
CD39 Is an Ecto-(Ca,Mg)-apyrase
@nl
prefLabel
CD39 Is an Ecto-(Ca,Mg)-apyrase
@en
CD39 Is an Ecto-(Ca,Mg)-apyrase
@nl
P2860
P356
P1476
CD39 Is an Ecto-(Ca,Mg)-apyrase
@en
P2093
Guido Guidotti
Ting-Fang Wang
P2860
P304
P356
10.1074/JBC.271.17.9898
P407
P577
1996-04-26T00:00:00Z