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Sökning: WFRF:(Leeb Lundberg F)

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1.
  • Aad, G., et al. (författare)
  • Observation and measurement of Higgs boson decays to WW* with the ATLAS detector
  • 2015
  • Ingår i: Physical Review D (Particles, Fields, Gravitation and Cosmology). - : American Physical Society. - 1550-2368 .- 1550-7998. ; 92:1
  • Tidskriftsartikel (refereegranskat)abstract
    • We report the observation of Higgs boson decays to WW* based on an excess over background of 6.1 standard deviations in the dilepton final state, where the Standard Model expectation is 5.8 standard deviations. Evidence for the vector-boson fusion (VBF) production process is obtained with a significance of 3.2 standard deviations. The results are obtained from a data sample corresponding to an integrated luminosity of 25 fb(-1) from root s = 7 and 8 TeV pp collisions recorded by the ATLAS detector at the LHC. For a Higgs boson mass of 125.36 GeV, the ratio of the measured value to the expected value of the total production cross section times branching fraction is 1.09(-0.15)(+0.16)(stat)(-0.14)(+0.17)(syst). The corresponding ratios for the gluon fusion and vector-boson fusion production mechanisms are 1.02 +/- 0.19(stat)(-0.18)(+0.22)(syst) and 1.27(-0.40)(+0.44)(stat)(-0.21)(+0.30)(syst), respectively. At root s = 8 TeV, the total production cross sections are measured to be sigma(gg -> H -> WW*) = 4.6 +/- 0.9(stat)(-0.7)(+0.8)(syst) pb and sigma(VBF H -> WW*) = 0.51(-0.15)(+0.17)(stat)(-0.08)(+0.13)(syst) pb. The fiducial cross section is determined for the gluon-fusion process in exclusive final states with zero or one associated jet.
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2.
  • Aad, G., et al. (författare)
  • Measurement of charged-particle spectra in Pb plus Pb collisions at root s(NN)=2.76 TeV with the ATLAS detector at the LHC
  • 2015
  • Ingår i: Journal of High Energy Physics. - : Springer. - 1029-8479 .- 1126-6708. ; :9
  • Tidskriftsartikel (refereegranskat)abstract
    • Charged-particle spectra obtained in Pb+Pb interactions at root s(NN) = 2.76TeV and pp interactions at root s(NN) = 2.76TeV with the ATLAS detector at the LHC are presented, using data with integrated luminosities of 0.15 nb(-1) and 4.2 pb(-1), respectively, in a wide transverse momentum (0.5 < p(T) < 150 GeV) and pseudorapidity (vertical bar eta vertical bar < 2) range. For Pb+Pb collisions, the spectra are presented as a function of collision centrality, which is determined by the response of the forward calorimeters located on both sides of the interaction point. The nuclear modification factors R-AA and R-CP are presented in detail as a function of centrality, p(T) and eta. They show a distinct p(T)-dependence with a pronounced minimum at about 7 GeV. Above 60 GeV, R-AA is consistent with a plateau at a centrality-dependent value, within the uncertainties. The value is 0.55 +/- 0.01(stat.) +/- 0.04(syst.) in the most central collisions. The R-AA distribution is consistent with flat vertical bar eta vertical bar dependence over the whole transverse momentum range in all centrality classes.
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3.
  • Windahl, Sara H, 1971, et al. (författare)
  • The role of the G protein-coupled receptor GPR30 in the effects of estrogen in ovariectomized mice.
  • 2009
  • Ingår i: American journal of physiology. Endocrinology and metabolism. - : American Physiological Society. - 0193-1849 .- 1522-1555. ; 296:3, s. E490-6
  • Tidskriftsartikel (refereegranskat)abstract
    • In vitro studies suggest that the membrane G protein-coupled receptor GPR30 is a functional estrogen receptor (ER). The aim of the present study was to determine the possible in vivo role of GPR30 as a functional ER primarily for the regulation of skeletal parameters, including bone mass and longitudinal bone growth, but also for some other well-known estrogen-regulated parameters, including uterine weight, thymus weight, and fat mass. Three-month-old ovariectomized (OVX) GPR30-deficient mice (GPR30(-/-)) and wild-type (WT) mice were treated with either vehicle or increasing doses of estradiol (E(2); 0, 30, 70, 160, or 830 ng.mouse(-1).day(-1)). Body composition [bone mineral density (BMD), fat mass, and lean mass] was analyzed by dual-energy-X ray absorptiometry, while the cortical and trabecular bone compartments were analyzed by peripheral quantitative computerized tomography. Quantitative histological analyses were performed in the distal femur growth plate. Bone marrow cellularity and distribution were analyzed using a fluorescence-activated cell sorter. The estrogenic responses on most of the investigated parameters, including increase in bone mass (total body BMD, spine BMD, trabecular BMD, and cortical bone thickness), increase in uterine weight, thymic atrophy, fat mass reduction, and increase in bone marrow cellularity, were similar for all of the investigated E(2) doses in WT and GPR30(-/-) mice. On the other hand, E(2) treatment reduced longitudinal bone growth, reflected by decreased femur length and distal femur growth plate height, in the WT mice but not in the GPR30(-/-) mice compared with vehicle-treated mice. These in vivo findings demonstrate that GPR30 is not required for normal estrogenic responses on several major well-known estrogen-regulated parameters. In contrast, GPR30 is required for a normal estrogenic response in the growth plate.
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4.
  • Maurer, M, et al. (författare)
  • New topics in bradykinin research
  • 2011
  • Ingår i: Allergy. - : Wiley-Blackwell. - 1398-9995. ; 66:11, s. 1397-1406
  • Tidskriftsartikel (refereegranskat)abstract
    • Bradykinin has been implicated to contribute to allergic inflammation and the pathogenesis of allergic conditions. It binds to endothelial B(1) and B(2) receptors and exerts potent pharmacological and physiological effects, notably, decreased blood pressure, increased vascular permeability and the promotion of classical symptoms of inflammation such as vasodilation, hyperthermia, oedema and pain. Towards potential clinical benefit, bradykinin has also been shown to exert potent antithrombogenic, antiproliferative and antifibrogenic effects. The development of pharmacologically active substances, such as bradykinin receptor blockers, opens up new therapeutic options that require further research into bradykinin. This review presents current understanding surrounding the role of bradykinin in nonallergic angioedema and other conditions seen by allergists and emergency physicians, and its potential role as a therapeutic target.
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5.
  • Benovic, J. L., et al. (författare)
  • Agonist-dependent phosphorylation of the α2-adrenergic receptor by the β-adrenergic receptor kinase
  • Ingår i: Journal of Biological Chemistry. - : ASBMB. - 0021-9258. ; 262:36, s. 17251-17253
  • Tidskriftsartikel (refereegranskat)abstract
    • Desensitization of the β-adrenergic receptor, a receptor which is coupled to the stimulation of adenylate cyclase, may be regulated via phosphorylation by a unique protein kinase. This recently discovered enzyme, known as the β-adrenergic receptor kinase, only phosphorylates the agonist-occupied form of the β-adrenergic receptor. To assess whether receptors coupled to the inhibition of adenylate cyclase might also be substrates, we examined the effects of β-adrenergic receptor kinase on the partially purified human platelet α2-adrenergic receptor. Phosphorylation of the reconstituted α2-adrenergic receptor was dependent on agonist occupancy and was completely blocked by co-incubation with α2-antagonists. The time course of phosphorylation of the α2-adrenergic receptor was virtually identical to that observed with the β-adrenergic receptor with maximum stoichiometries of 7-8 mol of phosphate/mol of receptor in each case. In contrast, the α1-adrenergic receptor, which is coupled to stimulation of phosphatidylinositol hydrolysis, is not a substrate for the β-adrenergic receptor kinase. These results suggest that receptors coupled to either stimulation or inhibition of adenylate cyclase may be regulated by an agonist-dependent phosphorylation mediated by the β-adrenergic receptor kinase.
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6.
  • De Weerd, W. F C, et al. (författare)
  • Bradykinin sequesters B2 bradykinin receptors and the receptor-coupled Ga SUBUNITS Gaq and Gai in caveolae
  • Ingår i: FASEB Journal. - : The Federation of American Societies for Experimental Biology. - 0892-6638. ; 11:9
  • Tidskriftsartikel (refereegranskat)abstract
    • Caveolae are small flask-like invaginations on the plasma membrane that contain both G-proteins aim G-protein coupled receptors. Consequently, these structures have been implicated to serve a role in transmembrane signaling. Bradykinin (BK) is a potent vasoactive peptide that acts through B2 BK receptors to stimulate both Gaq and Gai. DDT1 MF2 smooth muscle cells were used to show that eaveolae contain both Gaq, Gai and B2 receptors. Ga subunits and caveolin, a marker protein for eaveolae, were monitored by iminunoblotting, while B2 receptors were monitored as receptor radioligand complexes which were formed prior to cell disruption and caveolae enrichment. At 4°C, both agonist and antagonist receptor complexes were detected in eaveolae, and both types of complexes were acid-sensitive. Elevation of the temperature to 37°C resulted in a recruitment of agonist receptor complexes to caveotae and an increased acid-resistance of these complexes. Furthermore, these con ditions also promoted the recruitment of Gaq and Gci subunits. In contrast, antagonist receptor complexes were not recruited and remained acid-sensitive, and antagonists did not recruit Ga subunits. These results show that agonists for some G-protein-coupled receptors sequester their receptors and receptorcoupled Ga subunits in caveolae.
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7.
  • Dickinson, K. E.J., et al. (författare)
  • Photoaffinity cross-linking of a radioiodinated probe, 125I-A55453, into alpha1-adrenergic receptors
  • Ingår i: Molecular Pharmacology. - : American Society for Pharmacology and Experimental Therapeutics. - 0026-895X. ; 26:2, s. 187-195
  • Tidskriftsartikel (refereegranskat)abstract
    • We have synthesized and characterized a high-affinity alpha1-adrenergic receptor probe, 4-amino-6,7-dimethoxy-2[4'-[5''-(3-125I-iodo-4-aminophenyl)pentan oyl]-1'-piperazinyl]quinazoline (125I-A55453). This ligand binds reversibly to rat hepatic plasma membranes with high affinity (K(D) = 77 ± 6 pM), and it labels the same number of 'specific' prazosin-competable sites as the alpha1-adrenergic receptor-selective radioligand [125I] iodo-2-[β-(4-hydroxyphenyl)-ethylaminomethyl]tetralone. Specific binding is stereoselective and competed for by alpha-adrenergic agents with an alpha1-adrenergic receptor specificity. 125I-A55453 can be covalently photoincorporated into peptides of rat hepatic and splenic membranes using the bifunctional photoactive cross-linker, N-succinimidyl-6-(4'-azido-2'-nitrophenylamino)hexanoate. Following photolysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis of labeled hepatic membranes reveals a major 'specifically' labeled peptide of M(r) = 82,000 (± 1,000) with minor peptides at M(r) = 50,000 (± 500), and 40,000 (± 300). Covalent incorporation of 125I-A55453 into the M(r) = 82,000 peptide is inhibited by adrenergic drugs with an alpha1-adrenergic receptor specificity. Labeled splenic membranes demonstrate a broad band of photoincorporated radioactivity centered at M(r) = 82,000, and covalent incorporation into this peptide is also attenuated with an alpha1-adrenergic receptor specificity. This new high-affinity radioiodinated probe has features which should make it useful for the molecular characterization of alpha1-adrenergic receptors in tissues.
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8.
  • Fathy, Dana B., et al. (författare)
  • A single position in the third transmembrane domains of the human B1 and B2 bradykinin receptors is adjacent to and discriminates between the C- terminal residues of subtype-selective ligands
  • Ingår i: Journal of Biological Chemistry. - : ASBMB. - 0021-9258. ; 273:20, s. 12210-12218
  • Tidskriftsartikel (refereegranskat)abstract
    • In order to identify agonist- and antagonist-binding epitopes in the human B1 and B2 bradykinin (BK) receptors, we exploited the ability of these receptors to discriminate between peptide ligands that differ only by the absence (B1) grid presence (B2) of a C-terminal Arg. This was done by constructing chimeric proteins in which specific domains were exchanged between these receptors as recently described by us (Leeb, T., Mathis, S. A, and Leeb-Lundberg, L. M. F. (1997) J. Biol. Chem. 272, 311-317). The constructs were then expressed in HEK293 and A10 cells and assayed by radioligand binding and by agonist-stimulated inositol phospholipid hydrolysis and intracellular Ca2+ mobilization. Substitution of the third transmembrane domain (TM-III) of the B1 receptor in the B2 receptor (B2(B1III)) dramatically reduced the affinities of B2-selective peptide ligands including both the agonist BK and the antagonist NPC17731. High affinity binding of both ligands to B2(B1III) was fully regain when one residue, Lys111, in TM-III of this chimera was replaced with the corresponding wild-type (WT) B2 receptor residue, Ser (B2(B1IIIS111)). Replacement of Ser111 with Lys in the WT B2 receptor decreased the affinities of BK and NPC17731 and increased the affinity of the B1-selective des-Arg10 analog of NPC17731, NPC18565. The results show that the C- terminal residue of peptide agonists and antagonists when bound to the B2 receptor is adjacent to Ser111 in the receptor. A Lys at this position, as is the case in the WT B1 receptor, provides a positive charge that repels the C-terminal Arg in B2-selective peptides and attracts the negative charge of the C terminus of B1-selective peptides, which lack the C-terminal Arg. Therefore, the residues at this one single position are crucial in determining the peptide selectivity of B1 and B2 BK receptors.
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9.
  • Fathy, D. B., et al. (författare)
  • The third transmembrane domains of the human B1 and B2 bradykinin receptor subtypes are involved in discriminating between subtype-selective ligands
  • Ingår i: FASEB Journal. - : The Federation of American Societies for Experimental Biology. - 0892-6638. ; 11:9, s. 1327-1327
  • Tidskriftsartikel (refereegranskat)abstract
    • The B1 and B2 bradykinin (BK) receptor subtypes belong to the GPCR faro ily, and they discriminate between peptides that differ only by the absence and presence of a C-terminal Arg, To identify receptor residues conferring tigand spe.cificity, chimeric constructs in which TM-III were exchanged between the receptors were expressed and assayed by radioligand binding and fluorescence Ca2+ imaging in t1EK293 and A10 cells, respectively. Substitution of B1 TMIII into the B2 receptor (B2(B1III) decreased the affinity for the B2-selective agonist BK and antagonist NPC17731, while substitution of B2 TM-III into the Bt receptor decreased the affinity for the Bl-selective agonist des-Argm-Lys BK. High affinity binding to B2(B1III) was fully restored when one residue, Lys-11, in TMdlI was replaced with the corresponding residue, Serltl, in the wild-type B2 receptor. Binding was also restored by replacement with Ala, tlis, and Met, but not by' Arg. These results show that TM-III contributes significantly to the ability of these receptors to diseriminate between subtype selective ligands. We believe that the low affinity of B2-selective peptides for the B1 receptor is due in part to the positive charge of Lys-1. facing the ligand binding pocket which repels the positive charge of the C terminal Arg in these peptides.
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10.
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