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1.
Phys Rev Lett ; 117(6): 062501, 2016 Aug 05.
Article in English | MEDLINE | ID: mdl-27541463

ABSTRACT

Shape parameters of a weakly deformed ground-state band and highly deformed slightly triaxial sideband in ^{42}Ca were determined from E2 matrix elements measured in the first low-energy Coulomb excitation experiment performed with AGATA. The picture of two coexisting structures is well reproduced by new state-of-the-art large-scale shell model and beyond-mean-field calculations. Experimental evidence for superdeformation of the band built on 0_{2}^{+} has been obtained and the role of triaxiality in the A∼40 mass region is discussed. Furthermore, the potential of Coulomb excitation as a tool to study superdeformation has been demonstrated for the first time.

2.
Phys Rev Lett ; 113(1): 012501, 2014 Jul 04.
Article in English | MEDLINE | ID: mdl-25032921

ABSTRACT

The properties of pygmy dipole states in 208Pb were investigated using the 208Pb(17O, 17O'γ) reaction at 340 MeV and measuring the γ decay with high resolution with the AGATA demonstrator array. Cross sections and angular distributions of the emitted γ rays and of the scattered particles were measured. The results are compared with (γ, γ') and (p, p') data. The data analysis with the distorted wave Born approximation approach gives a good description of the elastic scattering and of the inelastic excitation of the 2+ and 3- states. For the dipole transitions a form factor obtained by folding a microscopically calculated transition density was used for the first time. This has allowed us to extract the isoscalar component of the 1- excited states from 4 to 8 MeV.

3.
Biochem Biophys Res Commun ; 195(2): 723-9, 1993 Sep 15.
Article in English | MEDLINE | ID: mdl-8396924

ABSTRACT

Okadaic acid, penetrating the human erythrocytes, almost completely inhibits P-Ser-protein phosphatase activity, whereas it unaffects Ser/Thr-protein kinase activity (casein kinases CKI and CKII), thus promoting a marked increase of the endogenous Ser-phosphorylation level of membrane proteins, such as cytoskeletal spectrin beta-subunit (band 2) and transmembrane band 3 protein. By contrast, the Tyr-phosphorylation state of band 3 protein is practically unaffected by okadaic acid, being unaffected both Tyr-protein kinase and P-Tyr-protein phosphatase activities.


Subject(s)
Erythrocyte Membrane/metabolism , Ethers, Cyclic/pharmacology , Membrane Proteins/blood , Casein Kinases , Cytosol/enzymology , Erythrocyte Membrane/drug effects , Erythrocytes/enzymology , Humans , Kinetics , Okadaic Acid , Phosphoprotein Phosphatases/antagonists & inhibitors , Phosphoprotein Phosphatases/blood , Phosphorylation , Protein Kinases/blood
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