Zobrazeno 1 - 10
of 24
pro vyhledávání: '"E. F. Roberts"'
Publikováno v:
Journal of Biological Chemistry. 266:5268-5272
Human monoblast U937 cells contain a soluble phospholipase A2 (PLA2) that is activated over the range of 150-600 nM Ca2+ and is stable only at neutral pH. We have purified this PLA2 over 34,000-fold to near homogeneity using sequential ion exchange,
Publikováno v:
Diabetes. 39:619-625
Autor:
E F, Roberts
Publikováno v:
NursingConnections. 12(2)
Publikováno v:
Seminars in oncology. 26(2 Suppl 6)
Prior studies have indicated that MTA requires intracellular polyglutamation for optimal cytotoxic effect and that these polyglutamates potently inhibit several key enzymes of folate metabolism, including thymidylate synthase (TS), dihydrofolate redu
Autor:
E F, Roberts
Publikováno v:
NursingConnections. 10(3)
Publikováno v:
Advances in experimental medicine and biology.
Autor:
R M, Kramer, E F, Roberts, S L, Um, A G, Börsch-Haubold, S P, Watson, M J, Fisher, J A, Jakubowski
Publikováno v:
The Journal of biological chemistry. 271(44)
The Ca2+-sensitive 85-kDa cytosolic phospholipase A2 (cPLA2) is responsible for thrombin-stimulated mobilization of arachidonic acid for the synthesis of thromboxane A2 in human platelets. We have previously shown that thrombin activates p38 kinase,
Publikováno v:
University of Strathclyde
In the present study we examined the activation of Ca(2+)-sensitive cytosolic phospholipase A2 (cPLA2) after aggregation of cell-surface high-affinity Fc receptors for IgE (Fc epsilon RI) on mast cells. MCII mast cells (a factor-dependent bone-marrow
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ded226839a6fc91fd64350a13fff46f5
https://europepmc.org/articles/PMC1137421/
https://europepmc.org/articles/PMC1137421/
Autor:
J D, Sharp, R T, Pickard, X G, Chiou, J V, Manetta, S, Kovacevic, J R, Miller, A D, Varshavsky, E F, Roberts, B A, Strifler, D N, Brems
Publikováno v:
The Journal of biological chemistry. 269(37)
The Ca(2+)-sensitive cytosolic phospholipase A2 (cPLA2) displays both a phospholipase A2 and a lysophospholipase activity. Numerous hydrolases, including lipases, catalyze the hydrolysis of ester bonds by means of an active site triad of amino acids
Publikováno v:
The Journal of biological chemistry. 268(35)
Receptor-mediated activation of human platelets by thrombin initiates a series of rapid biochemical events that include activation of phospholipase A2 to liberate arachidonic acid for further conversion to thromboxane A2. The identity of the phosphol