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- Feroci, M., et al.
(author)
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The Large Observatory for X-ray Timing (LOFT)
- 2012
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In: Experimental Astronomy. - : Springer Science and Business Media LLC. - 0922-6435 .- 1572-9508. ; 34:2, s. 415-444
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Journal article (peer-reviewed)abstract
- High-time-resolution X-ray observations of compact objects provide direct access to strong-field gravity, to the equation of state of ultradense matter and to black hole masses and spins. A 10 m(2)-class instrument in combination with good spectral resolution is required to exploit the relevant diagnostics and answer two of the fundamental questions of the European Space Agency (ESA) Cosmic Vision Theme "Matter under extreme conditions", namely: does matter orbiting close to the event horizon follow the predictions of general relativity? What is the equation of state of matter in neutron stars? The Large Observatory For X-ray Timing (LOFT), selected by ESA as one of the four Cosmic Vision M3 candidate missions to undergo an assessment phase, will revolutionise the study of collapsed objects in our galaxy and of the brightest supermassive black holes in active galactic nuclei. Thanks to an innovative design and the development of large-area monolithic silicon drift detectors, the Large Area Detector (LAD) on board LOFT will achieve an effective area of similar to 12 m(2) (more than an order of magnitude larger than any spaceborne predecessor) in the 2-30 keV range (up to 50 keV in expanded mode), yet still fits a conventional platform and small/medium-class launcher. With this large area and a spectral resolution of < 260 eV, LOFT will yield unprecedented information on strongly curved spacetimes and matter under extreme conditions of pressure and magnetic field strength.
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| 3. |
- Tanaka, Masaomi, et al.
(author)
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DISCOVERY OF DRAMATIC OPTICAL VARIABILITY IN SDSS J1100+4421 : A PECULIAR RADIO-LOUD NARROW-LINE SEYFERT 1 GALAXY?
- 2014
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In: Astrophysical Journal Letters. - 2041-8205 .- 2041-8213. ; 793:2, s. L26-
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Journal article (peer-reviewed)abstract
- We present our discovery of dramatic variability in SDSS J1100+4421 by the high-cadence transient survey Kiso Supernova Survey. The source brightened in the optical by at least a factor of three within about half a day. Spectroscopic observations suggest that this object is likely a narrow-line Seyfert 1 galaxy (NLS1) at z = 0.840, however, with unusually strong narrow emission lines. The estimated black hole mass of similar to 10(7) M-circle dot implies bolometric nuclear luminosity close to the Eddington limit. SDSS J1100+4421 is also extremely radio-loud, with a radio loudness parameter of R similar or equal to 4 x 10(2)-3 x 10(3), which implies the presence of relativistic jets. Rapid and large-amplitude optical variability of the target, reminiscent of that found in a few radio- and gamma-ray-loud NLS1s, is therefore produced most likely in a blazar-like core. The 1.4 GHz radio image of the source shows an extended structure with a linear size of about 100 kpc. If SDSS J1100+4421 is a genuine NLS1, as suggested here, this radio structure would then be the largest ever discovered in this type of active galaxies.
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| 4. |
- Ayeni, Olufemi R, 1976, et al.
(author)
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Diagnosing femoroacetabular impingement from plain radiographs: Do radiologists and orthopaedic surgeons differ?
- 2014
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In: Orthopaedic Journal of Sports Medicine. - : SAGE Publications. - 2325-9671. ; 2:7
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Journal article (peer-reviewed)abstract
- Background: A diagnosis of femoroacetabular impingement (FAI) requires careful history and physical examination, as well as an accurate and reliable radiologic evaluation using plain radiographs as a screening modality. Radiographic markers in the diagnosis of FAI are numerous and not fully validated. In particular, reliability in their assessment across health care providers is unclear. Purpose: To determine inter- and intraobserver reliability between orthopaedic surgeons and musculoskeletal radiologists. Study Design: Cohort study (diagnosis); Level of evidence, 3. Methods: Six physicians (3 orthopaedic surgeons, 3 musculoskeletal radiologists) independently evaluated a broad spectrum of FAI pathologies across 51 hip radiographs on 2 occasions separated by at least 4 weeks. Reviewers used 8 common criteria to diagnose FAI, including (1) pistol-grip deformity, (2) size of alpha angle, (3) femoral head-neck offset, (4) posterior wall sign abnormality, (5) ischial spine sign abnormality, (6) coxa profunda abnormality, (7) crossover sign abnormality, and (8) acetabular protrusion. Agreement was calculated using the intraclass correlation coefficient (ICC). Results: When establishing an FAI diagnosis, there was poor interobserver reliability between the surgeons and radiologists (ICC batch 1 = 0.33; ICC batch 2 = 0.15). In contrast, there was higher interobserver reliability within each specialty, ranging from fair to good (surgeons: ICC batch 1 = 0.72; ICC batch 2 = 0.70 vs radiologists: ICC batch 1 = 0.59; ICC batch 2 = 0.74). Orthopaedic surgeons had the highest interobserver reliability when identifying pistol-grip deformities (ICC = 0.81) or abnormal alpha angles (ICC = 0.81). Similarly, radiologists had the highest agreement for detecting pistol-grip deformities (ICC = 0.75). Conclusion: These results suggest that surgeons and radiologists agree among themselves, but there is a need to improve the reliability of radiographic interpretations for FAI between the 2 specialties. The observed degree of low reliability may ultimately lead to missed, delayed, or inappropriate treatments for patients with symptomatic FAI. © The Author(s) 2014.
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| 5. |
- Javaherian, Anoosh D., et al.
(author)
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Metal-driven operation of the human large-conductance voltage- and Ca2+-dependent potassium channel (BK) gating ring apparatus
- 2011
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In: Journal of Biological Chemistry. - : American Society for Biochemistry and Molecular Biology. - 0021-9258 .- 1083-351X. ; 286:23, s. 20701-20709
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Journal article (peer-reviewed)abstract
- Large-conductance voltage- and Ca2+-dependent K+ (BK, also known as MaxiK) channels are homo-tetrameric proteins with a broad expression pattern that potently regulate cellular excitability and Ca2+ homeostasis. Their activation results from the complex synergy between the transmembrane voltage sensors and a large (>300 kDa) C-terminal, cytoplasmic complex (the “gating ring”), which confers sensitivity to intracellular Ca2+ and other ligands. However, the molecular and biophysical operation of the gating ring remains unclear. We have used spectroscopic and particle-scale optical approaches to probe the metal-sensing properties of the human BK gating ring under physiologically relevant conditions. This functional molecular sensor undergoes Ca2+- and Mg2+-dependent conformational changes at physiologically relevant concentrations, detected by time-resolved and steady-state fluorescence spectroscopy. The lack of detectable Ba2+-evoked structural changes defined the metal selectivity of the gating ring. Neutralization of a high-affinity Ca2+-binding site (the “calcium bowl”) reduced the Ca2+ and abolished the Mg2+ dependence of structural rearrangements. In congruence with electrophysiological investigations, these findings provide biochemical evidence that the gating ring possesses an additional high-affinity Ca2+-binding site and that Mg2+ can bind to the calcium bowl with less affinity than Ca2+. Dynamic light scattering analysis revealed a reversible Ca2+-dependent decrease of the hydrodynamic radius of the gating ring, consistent with a more compact overall shape. These structural changes, resolved under physiologically relevant conditions, likely represent the molecular transitions that initiate the ligand-induced activation of the human BK channel.
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| 7. |
- Yusifov, Taleh, et al.
(author)
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The RCK1 Domain of the Human BKCa Channel Transduces Ca2+ Binding into Structural Rearrangements
- 2010
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In: The Journal of General Physiology. - : Rockefeller University Press. - 0022-1295 .- 1540-7748. ; 136:2, s. 189-202
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Journal article (peer-reviewed)abstract
- Large-conductance voltage- and Ca2+-activated K+ (BKCa) channels play a fundamental role in cellular function by integrating information from their voltage and Ca2+ sensors to control membrane potential and Ca2+ homeostasis. The molecular mechanism of Ca2+-dependent regulation of BKCa channels is unknown, but likely relies on the operation of two cytosolic domains, regulator of K+ conductance (RCK)1 and RCK2. Using solution-based investigations, we demonstrate that the purified BKCa RCK1 domain adopts an α/β fold, binds Ca2+, and assembles into an octameric superstructure similar to prokaryotic RCK domains. Results from steady-state and time-resolved spectroscopy reveal Ca2+-induced conformational changes in physiologically relevant [Ca2+]. The neutralization of residues known to be involved in high-affinity Ca2+ sensing (D362 and D367) prevented Ca2+-induced structural transitions in RCK1 but did not abolish Ca2+ binding. We provide evidence that the RCK1 domain is a high-affinity Ca2+ sensor that transduces Ca2+ binding into structural rearrangements, likely representing elementary steps in the Ca2+-dependent activation of human BKCa channels.
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