484 research outputs found

    Urotensin receptor in GtoPdb v.2021.3

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    The urotensin-II (U-II) receptor (UT, nomenclature as agreed by the NC-IUPHAR Subcommittee on the Urotensin receptor [26, 36, 93]) is activated by the endogenous dodecapeptide urotensin-II, originally isolated from the urophysis, the endocrine organ of the caudal neurosecretory system of teleost fish [7, 92]. Several structural forms of U-II exist in fish and amphibians [93]. The goby orthologue was used to identify U-II as the cognate ligand for the predicted receptor encoded by the rat gene gpr14 [2, 20, 63, 69, 72]. Human urotensin-II, an 11-amino-acid peptide [20], retains the cyclohexapeptide sequence of goby U-II that is thought to be important in ligand binding [61, 53, 10]. This sequence is also conserved in the deduced amino-acid sequence of rat urotensin-II (14 amino-acids) and mouse urotensin-II (14 amino-acids), although the N-terminal is more divergent from the human sequence [19]. A second endogenous ligand for the UT has been discovered in rat [86]. This is the urotensin II-related peptide, an octapeptide that is derived from a different gene, but shares the C-terminal sequence (CFWKYCV) common to U-II from other species. Identical sequences to rat urotensin II-related peptide are predicted for the mature mouse and human peptides [32]. UT exhibits relatively high sequence identity with somatostatin, opioid and galanin receptors [93]

    Urotensin receptor in GtoPdb v.2023.1

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    The urotensin-II (U-II) receptor (UT, nomenclature as agreed by the NC-IUPHAR Subcommittee on the Urotensin receptor [26, 36, 94]) is activated by the endogenous dodecapeptide urotensin-II, originally isolated from the urophysis, the endocrine organ of the caudal neurosecretory system of teleost fish [7, 93]. Several structural forms of U-II exist in fish and amphibians [94]. The goby orthologue was used to identify U-II as the cognate ligand for the predicted receptor encoded by the rat gene gpr14 [2, 20, 63, 69, 72]. Human urotensin-II, an 11-amino-acid peptide [20], retains the cyclohexapeptide sequence of goby U-II that is thought to be important in ligand binding [61, 53, 10]. This sequence is also conserved in the deduced amino-acid sequence of rat urotensin-II (14 amino-acids) and mouse urotensin-II (14 amino-acids), although the N-terminal is more divergent from the human sequence [19]. A second endogenous ligand for the UT has been discovered in rat [86]. This is the urotensin II-related peptide, an octapeptide that is derived from a different gene, but shares the C-terminal sequence (CFWKYCV) common to U-II from other species. Identical sequences to rat urotensin II-related peptide are predicted for the mature mouse and human peptides [32]. UT exhibits relatively high sequence identity with somatostatin, opioid and galanin receptors [94]. The urotensinergic system displays an unprecedented repertoire of four or five ancient UT in some vertebrate lineages and five U-II family peptides in teleost fish [91]

    Urotensin receptor (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

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    The urotensin-II (U-II) receptor (UT, nomenclature as agreed by the NC-IUPHAR Subcommittee on the Urotensin receptor [26, 36, 89]) is activated by the endogenous dodecapeptide urotensin-II, originally isolated from the urophysis, the endocrine organ of the caudal neurosecretory system of teleost fish [7, 88]. Several structural forms of U-II exist in fish and amphibians. The goby orthologue was used to identify U-II as the cognate ligand for the predicted receptor encoded by the rat gene gpr14 [20, 62, 68, 70]. Human urotensin-II, an 11-amino-acid peptide [20], retains the cyclohexapeptide sequence of goby U-II that is thought to be important in ligand binding [53, 11]. This sequence is also conserved in the deduced amino-acid sequence of rat urotensin-II (14 amino-acids) and mouse urotensin-II (14 amino-acids), although the N-terminal is more divergent from the human sequence [19]. A second endogenous ligand for the UT has been discovered in rat [83]. This is the urotensin II-related peptide, an octapeptide that is derived from a different gene, but shares the C-terminal sequence (CFWKYCV) common to U-II from other species. Identical sequences to rat urotensin II-related peptide are predicted for the mature mouse and human peptides [32]. UT exhibits relatively high sequence identity with somatostatin, opioid and galanin receptors [89]

    Aligned crystallite powder of NdFeAsO0.86_{0.86}F0.14_{0.14}: magnetic hysteresis and penetration depth

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    We report the basal-plane critical current and superfluid density of magnetically aligned NdFeAsO0.86_{0.86}F0.14_{0.14} powder. This sample has individual crystallite grains permanently oriented with their c axis along the external field. Magnetic irreversibilities at high field suggest strong flux pinning of basal-plane critical currents, with monotonic field dependence and no evidence of the "fishtail" effect. The small particles provide a sensitive indicator of \textit{dc} flux penetration, and allow analysis of the temperature dependence of ab−ab-plane London penetration depth λab,L\lambda_{ab,\mathrm{L}}, which is quadratic at low TT. This feature may not necessarily be due to the nodes in the gap, but may be rather a sign of a strong pair-breaking. A quantitative determination of the absolute magnitude of λab,L\lambda_{ab,\mathrm{L}} is hindered by the need for accurate knowledge of the particle size distribution.Comment: 6 pages, 6 figure

    The nature of point source fringes in mid-infrared spectra acquired with the James Webb Space Telescope

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    The constructive and destructive interference in different layers of the James Webb Space Telescope (JWST) Mid-Infrared Instrument (MIRI) detector arrays modulate the detected signal as a function of wavelength. Additionally, sources of different spatial profiles show different fringe patterns. Dividing by a static fringe flat could hamper the scientific interpretation of sources whose fringes do not match that of the fringe flat. We find point source fringes measured by the MIRI Medium-Resolution Spectrometer (MRS) to be reproducible under similar observing conditions. We want, thus, to identify the variables, if they exist, that would allow for a parametrization of the signal variations induced by point source fringe modulations. We do this by analyzing MRS detector plane images acquired on the ground. We extracted the fringe profile of multiple point source observations and studied the amplitude and phase of the fringes as a function of field position and pixel sampling of the point spread function of the optical chain. A systematic variation in the amplitude and phase of the point source fringes is found over the wavelength range covered by the test sources (4.9-5.8 μ\mum). The variation depends on the fraction of the point spread function seen by the detector pixel. We identify the non-uniform pixel illumination as the root cause of the reported systematic variation. We report an improvement after correction of 50% on the 1σ\sigma standard deviation of the spectral continuum. A 50% improvement is also reported in line sensitivity for a benchmark test with a spectral continuum of 100 mJy. The improvement in the shape of weak lines is illustrated using a T Tauri model spectrum. Consequently, we verify that fringes of extended sources and potentially semi-extended sources and crowded fields can be simulated by combining multiple point source fringe transmissions.Comment: 17 pages, 31 figure

    ESPRESSO Observations of Gaia BH1:High-precision Orbital Constraints and no Evidence for an Inner Binary

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    We present high-precision radial velocity observations of Gaia BH1, the nearest known black hole (BH). The system contains a solar-type G star orbiting a massive dark companion, which could be either a single BH or an inner BH + BH binary. A BH + BH binary is expected in some models where Gaia BH1 formed as a hierarchical triple, which is attractive because they avoid many of the difficulties associated with forming the system through isolated binary evolution. Our observations test the inner binary scenario. We have measured 115 precise RVs of the G star, including 40 from ESPRESSO with a precision of 3–5 m s−1, and 75 from other instruments with a typical precision of 30–100 m s−1. Our observations span 2.33 orbits of the G star and are concentrated near a periastron passage, when perturbations due to an inner binary would be largest. The RVs are well-fit by a Keplerian two-body orbit and show no convincing evidence of an inner binary. Using REBOUND simulations of hierarchical triples with a range of inner periods, mass ratios, eccentricities, and orientations, we show that plausible inner binaries with periods Pinner ≳ 1.5 days would have produced larger deviations from a Keplerian orbit than observed. Binaries with Pinner ≲ 1.5 days are consistent with the data, but these would merge within a Hubble time and would thus imply fine-tuning. We present updated parameters of Gaia BH1's orbit. The RVs yield a spectroscopic mass function f(MBH)=3.9358±0.0002M⊙—about 7000σ above the ∼2.5 M⊙ maximum neutron star mass. Including the inclination constraint from Gaia astrometry, this implies a BH mass of MBH = 9.27 ± 0.10 M⊙
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