25,674 research outputs found
A 2 h periodic variation in the low-mass X-ray binary Ser X-1
No full textSpectroscopy of the low-mass X-ray binary Ser X-1 using the Gran Telescopio Canarias have revealed a ?2 h periodic variability that is present in the three strongest emission lines. We tentatively interpret this variability as due to orbital motion, making it the first indication of the orbital period of Ser X-1. Together with the fact that the emission lines are remarkably narrow, but still resolved, we show that a main-sequence K dwarf together with a canonical 1.4 M? neutron star gives a good description of the system. In this scenario, the most likely place for the emission lines to arise is the accretion disc, instead of a localized region in the binary (such as the irradiated surface or the stream-impact point), and their narrowness is due instead to the low inclination (?10°) of Ser X-1
PROPERTIES OF HYDROGEN-BONDED COMPLEXES OBTAINED FROM THE B3LYP FUNCTIONAL WITH 6-31G (D, P) AND 6-31+G (D, P) BASIS SETS: COMPARISON WITH MP2/6-31+G (D, P) RESULTS AND EXPERIMENTAL DATA
No full textAuthor Institution: Youngatown State University, Youngatown, Ohio 44555; University of Florida, Gainesville, Florida 32611Density functional B3LYP/6-31G (d, p) calculations fail to yield reliable binding energies, intermolecular distances, and hydrogen-bonded X-H frequency shifts for seven hydrogen-bonded complexes for which experimental data are available. Properties of these complexes obtained with the B3LYP functional and the 6-31+G (d, p) basis are improved, and are often similar to MP2/6-31+G (d, p) values. In those cases where noticeable differences exist between B3LYP/6-31+G (d, p) and MP2/6-31+G (d, p) intermolecular distances and frequency shifts, the MP2/6-31+G (d, p) values are in better agreement with experimental data. Calculation of reliable binding energies requires a basis set larger than 6-31+G (d, p)
OPA1 increases the risk of normal but not high tension glaucoma
No full textBackground Primary open angle glaucoma is a progressive optic neuropathy characterised by the selective loss of retinal ganglion cells, pathological optic disc cupping and visual field defects. The OPA1 gene encodes an inner mitochondrial membrane protein crucial for normal mitochondrial function, and pathogenic mutations cause autosomal dominant optic atrophy by specifically targeting retinal ganglion cells. This raises the distinct possibility that more subtle genetic variations in OPA1 could alter the risk of developing glaucoma.Methods 137 patients with primary open angle glaucoma (67 patients with high-tension glaucoma (HTG), 70 patients with normal-tension glaucoma (NTG)) and 75 controls from the North East of England were studied. Three single-nucleotide polymorphisms in intron 8 (IVS8+4c/t and IVS8+32t/c) and exon 4 (c.473A/G) of the OPA1 gene were genotyped in thestudy group. In addition, the entire OPA1 coding regionwas sequenced in 24 individuals with the CT/TTcompound genotype using standard BigDye chemistries.Results There was no difference in either allele or genotype frequency for the IVS8+32t/c singlenucleotide polymorphisms between patients and controls, but there was a significant association between the T allele at IVS8+4c/t and the risk of developing NTG (OR¼2.04, 95% CI¼1.10 to 3.81, p¼0.004), but not HTG. Logistic regression analysis also confirmed a strong association between the CT/TT compound genotype atIVS8+4 and IVS8+32 with NTG (OR¼29.75, 95% CI¼3.83 to 231.21, p¼0.001).Conclusions The CT/TT compound genotype at IVS8+4 and IVS8+32 is a strong genetic risk determinant for NTG but not HTG
1ST MEASUREMENT OF GAMMA(D(S)(+)-]MU+NU)/GAMMA(D(S)(+)-]PHI-PI+)
No full textComplete Author List:
ACOSTA D, ATHANAS M, MASEK G, PAAR H, BEAN A, GRONBERG J, KUTSCHKE R, MENARY S, MORRISON RJ, NAKANISHI S, NELSON HN, NELSON TK, RICHMAN JD, RYD A, TAJIMA H, SCHMIDT D, SPERKA D, WITHERELL MS, PROCARIO M, YANG S, BALEST R, CHO K, DAOUDI M, FORD WT, JOHNSON DR, LINGEL K, LOHNER M, RANKIN P, SMITH JG, ALEXANDER JP, BEBEK C, BERKELMAN K, BESSON D, BROWDER TE, CASSEL DG, CHO HA, COFFMAN DM, DRELL PS, EHRLICH R, GALIK RS, GARCIASCIVERES M, GEISER B, GITTELMAN B, GRAY SW, HARTILL DL, HELTSLEY BK, JONES CD, JONES SL, KANDASWAMY J, KATAYAMA N, KIM PC, KREINICK DL, LUDWIG GS, MASUI J, MEVISSEN J, MISTRY NB, NG CR, NORDBERG E, OGG M, PATTERSON JR, PETERSON D, RILEY D, SALMAN S, SAPPER M, WORDEN H, WURTHWEIN F, AVERY P, FREYBERGER A, RODRIGUEZ J, STEPHENS R, YELTON J, CINABRO D, HENDERSON S, KINOSHITA K, LIU T, SAULNIER M, SHEN F, WILSON R, YAMAMOTO H, ONG B, SELEN M, SADOFF AJ, AMMAR R, BALL S, BARINGER P, COPPAGE D, COPTY N, DAVIS R, HANCOCK N, KELLY M, KWAK N, LAM H, KUBOTA Y, LATTERY M, NELSON JK, PATTON S, PERTICONE D, POLING R, SAVINOV V, SCHRENK S, WANG R, ALAM MS, KIM IJ, NEMATI B, ONEILL JJ, SEVERINI H, SUN CR, ZOELLER MM, CRAWFORD G, DAUBENMIER CM, FULTON R, FUJINO D, GAN KK, HONSCHEID K, KAGAN H, KASS R, LEE J, MALCHOW R, MORROW F, SKOVPEN Y, SUNG M, WHITE C, WHITMORE J, WILSON P, BUTLER F, FU X, KALBFLEISCH G, LAMBRECHT M, ROSS WR, SKUBIC P, SNOW J, WANG PL, WOOD M, BORTOLETTO D, BROWN DN, FAST J, MCILWAIN RL, MIAO T, MILLER DH, MODESITT M, SCHAFFNER SF, SHIBATA EI, SHIPSEY IPJ, WANG PN, BATTLE M, ERNST J, KROHA H, ROBERTS S, SPARKS K, THORNDIKE EH, WANG CH, DOMINICK J, SANGHERA S, SHELKOV V, SKWARNICKI T, STROYNOWSKI R, VOLOBOUEV I, ZADOROZHNY P, ARTUSO M, HE D, GOLDBERG M, HORWITZ N, KENNETT R, MONETI GC, MUHEIM F, MUKHIN Y, PLAYFER S, ROZEN Y, STONE S, THULASIDAS M, VASSEUR G, ZHU G, BARTELT J, CSORNA SE, EGYED Z, JAIN V, SHELDON P, AKERIB DS, BARISH B, CHADHA M, CHAN S, COWEN DF, EIGEN G, MILLER JS, OGRADY C, URHEIM J, WEINSTEIN A
TRIM72 directly interacts with RABV-M via the SPRY domain.
No full text(A) pCAGGS or pCA-Trim72-flag together with pCA-M-HA were co-transfected into N2a cells respectively. Then Mg132 (10 μM) was treated, and Co-IP assays were performed with anti-flag antibody post-transfection for 48 h. The protein levels of TRIM72-flag and M-HA were analyzed by western blotting. (B) pCAGGS or pCA-M-flag together with pCA-Trim72-HA were co-transfected into N2a cells respectively for 48 h. Then Co-IP assays were performed with anti-flag antibody. The protein levels of TRIM72-flag and M-HA were analyzed by western blotting. (C) N2a cells were infected with RABV (MOI = 1) for 36 h. Then Co-IP assays were performed with anti-TRIM72 antibody. The protein levels of TRIM72 and M were analyzed by western blotting. (D) TRIM72 truncations were designed and constructed based on its functional domain. (E) The over-expression vectors of TRIM72-flag truncations together with pCA-M-HA were co-transfected into N2a cells respectively for 48 h. Then Co-IP assays were performed with anti-flag antibody. The protein levels of TRIM72 truncations and M-HA were analyzed by western blotting. (F) RABV-M truncations were designed and constructed based on its secondary structure. (G) The over-expression vectors of M-HA truncations together with pCA-Trim72-SPRY-flag were co-transfected into N2a cells for 48 h. Then Co-IP assays were performed with anti-HA antibody. The protein levels of M truncations and SPRY-flag were analyzed by western blotting. (H) A structural model of RABV-M was built using SWISS-MODEL online software (https://swissmodel.expasy.org/interactive) based on the crystal structure of Lagos bat virus M protein (PDB code: 2W2S). (I) An interaction model of the human TRIM72-SPRY domain and RABV-M was built with GalaxyWEB online software (https://galaxy.seoklab.org/) based on hTRIM72 structure (PDB code: 6NPY), the potential interaction sites were labeled. (J) Over-expression vectors of RABV-M-HA mutations together with TRIM72-SPRY-flag over-expression vector were co-transfected into N2a cells respectively for 48 h. Then Co-IP assays were performed with anti-HA antibody. The protein levels were analyzed by western blotting. (K) The protein sequences of SPRY domain between hTRIM72 and mouse TRIM72 were compared and analyzed with ESPript 3.0 online software (https://espript.ibcp.fr/ESPript/cgi-bin/ESPript.cgi). (L) Over-expression vectors of TRIM72-SPRY-flag mutations together with M-HA over-expression vectors were co-transfected into N2a cells respectively for 48 h. Then Co-IP assays were performed with anti-flag antibody and protein levels were analyzed by western blotting. (M) Over-expression vectors of TRIM72-flag mutations together with M-HA over-expression vector were co-transfected into N2a cells respectively for 48 h. The protein levels were analyzed by western blotting. (N) Over-expression vectors of TRIM72-flag mutations or empty vectors were transfected into N2a cells respectively for 12 h, then infected with rRABV (MOI = 0.01) for 48 h and the viral titers in the supernatants were analyzed. Statistical analysis of grouped comparisons was carried out by student’s t-test (*P < 0.05; **P<0.01; ***P<0.001; ****P<0.0001). The bar graph represents means ± SD, n = 3. Western blot data are representative of at least two independent experiments.</p
Measurement of the D+/- production asymmetry in 7 TeV pp collisions
No full textThe asymmetry in the production cross-section \sigma of D+/- mesons, A_P = (\sigma(D+) - \sigma(D-))/(\sigma(D+) + \sigma(D-)), is measured in bins of pseudorapidity \eta and transverse momentum p_T within the acceptance of the LHCb detector. The result is obtained with a sample of D+ -> K_S pi+ decays corresponding to an integrated luminosity of 1.0 fb^-1, collected in pp collisions at a centre of mass energy of 7 TeV at the Large Hadron Collider. When integrated over the kinematic range 2.0 K_S pi+ decay is negligible. No significant dependence on \eta or p_T is observed
Climate change, biodiversity loss and mental health: a global perspective
No full textClimate change can have various psychopathological manifestations which have been more actively addressed by scientific research only in recent years. Indeed, extreme weather events and environmental changes have been shown to be associated with a range of mental health problems. Following the destruction of ecosystems, biodiversity loss can cause mental distress and emotional responses, including so-called 'psychoterratic' syndromes arising from negatively felt and perceived environmental change. Studies investigating relationships between biodiversity and mental health reveal a complex landscape of scientific evidence, calling for a better understanding of this challenging issue. Copyright © The Author(s), 2022. Published by Cambridge University Press on behalf of the Royal College of Psychiatrists
Author Correction: A corridor of exposed ice-rich bedrock across Titan’s tropical region (Nature Astronomy, (2019), 3, 7, (642-648), 10.1038/s41550-019-0756-5)
No full textIn the version of this Article originally published, the author Rosaly Lopes was mistakenly affiliated with Northern Arizona University. Her affiliation has now been corrected to: Jet Propulsion Laboratory, California Institute of Technology, Pasadena, CA, USA. © 2019, Springer Nature Limited
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