485 research outputs found
Self-Focused and Other-Focused Health Concerns as Predictors of the Uptake of Corona Contact Tracing Apps: Empirical Study
Background
Corona contact tracing apps are a novel and promising measure to reduce the spread of COVID-19. They can help to balance the need to maintain normal life and economic activities as much as possible while still avoiding exponentially growing case numbers. However, a majority of citizens need to be willing to install such an app for it to be effective. Hence, knowledge about drivers for app uptake is crucial.
Objective
This study aimed to add to our understanding of underlying psychological factors motivating app uptake. More specifically, we investigated the role of concern for oneâs own health and concern to unknowingly infect others.
Methods
A two-wave survey with 346 German-speaking participants from Switzerland and Germany was conducted. We measured the uptake of two decentralized contact tracing apps officially launched by governments (Corona-Warn-App, Germany; SwissCovid, Switzerland), as well as concerns regarding COVID-19 and control variables.
Results
Controlling for demographic variables and general attitudes toward the government and the pandemic, logistic regression analysis showed a significant effect of self-focused concerns (odds ratio [OR] 1.64, P=.002). Meanwhile, concern of unknowingly infecting others did not contribute significantly to the prediction of app uptake over and above concern for oneâs own health (OR 1.01, P=.92). Longitudinal analyses replicated this pattern and showed no support for the possibility that app uptake provokes changes in levels of concern. Testing for a curvilinear relationship, there was no evidence that âtoo muchâ concern leads to defensive reactions and reduces app uptake.
Conclusions
As one of the first studies to assess the installation of already launched corona tracing apps, this study extends our knowledge of the motivational landscape of app uptake. Based on this, practical implications for communication strategies and app design are discussed
Phosphorylation of the ribosomal protein RPL12/uL11 affects translation during mitosis
Emerging evidence indicates that heterogeneity in ribosome composition can give rise to specialized functions. Until now, research mainly focused on differences in core ribosomal proteins and associated factors. The effect of posttranslational modifications has not been studied systematically. Analyzing ribosome heterogeneity is challenging because individual proteins can be part of different subcomplexes (40S, 60S, 80S, and polysomes). Here we develop polysome proteome profiling to obtain unbiased proteomic maps across ribosomal subcomplexes. Our method combines extensive fractionation by sucrose gradient centrifugation with quantitative mass spectrometry. The high resolution of the profiles allows us to assign proteins to specific subcomplexes. Phosphoproteomics on the fractions reveals that phosphorylation of serine 38 in RPL12/uL11, a known mitotic CDK1 substrate, is strongly depleted in polysomes. Follow-up experiments confirm that RPL12/uL11 phosphorylation regulates the translation of specific subsets of mRNAs during mitosis. Together, our results show that posttranslational modification of ribosomal proteins can regulate translation
The evolution of crystalline ordering for ligand-ornamented zinc oxide nanoparticles
Recent total scattering experiments have opened up the possibility to study nanoparticle formation in situ and to observe the structural transformation from precursor clusters to adult particles. Organic ligand molecules interact with precursors of metal oxide nanoparticles, yet their influence onto the evolution of crystallinity during particle formation has not been addressed in detail; nor have in situ total scattering experiments ventured into the field of low-concentration, room-temperature syntheses in organic solvents to date. In this report, we follow the crystallization of ZnO nanoparticles in ethanol in the presence of different organic ligands. Low coordinated zinc precursor clusters rapidly polymerize upon base addition to particles of ca. 1 nm in diameter. In situ SAXS experiments reveal that the overall particle size increases to 2 to 4 nm with advancing reaction time. Complementary in situ PDF experiments show smaller crystalline domain sizes, which are only one third to half as large as the particle diameter. The ZnO particles thus feature a crystalline core surrounded by a disordered shell. Both, the core and the shell diameter are influenced by the different surface-bound organic ligands, which prevent an immediate relaxation to fully crystalline particles. A slow crystallization takes place in solution. We assume a dynamic equilibrium of the ligand and solvent molecules at the particle surface, which enables gradual bond restructuring. With suitably adjusted synthesis conditions, in our case by a continuous base addition, we show how to bypass the disordered intermediates, allowing the spontaneous nucleation of fully crystalline nanoparticles
A Study of Time-Dependent CP-Violating Asymmetries and Flavor Oscillations in Neutral B Decays at the Upsilon(4S)
We present a measurement of time-dependent CP-violating asymmetries in
neutral B meson decays collected with the BABAR detector at the PEP-II
asymmetric-energy B Factory at the Stanford Linear Accelerator Center. The data
sample consists of 29.7 recorded at the
resonance and 3.9 off-resonance. One of the neutral B mesons,
which are produced in pairs at the , is fully reconstructed in
the CP decay modes , , , () and , or in flavor-eigenstate
modes involving and (). The flavor of the other neutral B meson is tagged at the time of
its decay, mainly with the charge of identified leptons and kaons. The proper
time elapsed between the decays is determined by measuring the distance between
the decay vertices. A maximum-likelihood fit to this flavor eigenstate sample
finds . The value of the asymmetry amplitude is determined from
a simultaneous maximum-likelihood fit to the time-difference distribution of
the flavor-eigenstate sample and about 642 tagged decays in the
CP-eigenstate modes. We find , demonstrating that CP violation exists in the neutral B meson
system. (abridged)Comment: 58 pages, 35 figures, submitted to Physical Review
CRNKL1 is a highly selective regulator of intron-retaining HIV-1 and cellular mRNAs
The HIV-1 Rev protein is a nuclear export factor for unspliced and incompletely spliced HIV-1 RNAs. Without Rev, these intron-retaining RNAs are trapped in the nucleus. A genome-wide screen identified nine proteins of the spliceosome, which all enhanced expression from the HIV-1 unspliced RNA after CRISPR/Cas knockdown. Depletion of DHX38, WDR70, and four proteins of the Prp19-associated complex (ISY1, BUD31, XAB2, and CRNKL1) resulted in a more than 20-fold enhancement of unspliced HIV-1 RNA levels in the cytoplasm. Targeting of CRNKL1, DHX38, and BUD31 affected nuclear export efficiencies of the HIV-1 unspliced RNA to a much larger extent than splicing. Transcriptomic analyses further revealed that CRNKL1 also suppresses cytoplasmic levels of a subset of cellular mRNAs, including some with selectively retained introns. Thus, CRNKL1-dependent nuclear retention is a novel cellular mechanism for the regulation of cytoplasmic levels of intron-retaining HIV-1 mRNAs, which HIV-1 may have harnessed to direct its complex splicing pattern. IMPORTANCE: To regulate its complex splicing pattern, HIV-1 uses the adaptor protein Rev to shuttle unspliced or partially spliced mRNA from the nucleus to the cytoplasm. In the absence of Rev, these RNAs are retained in the nucleus, but it is unclear why. Here we identify cellular proteins whose depletion enhances cytoplasmic levels of the HIV-1 unspliced RNA. Depletion of one of them, CRNKL1, also increases cytoplasmic levels of a subset of intron-retaining cellular mRNA, suggesting that CRNKL1-dependent nuclear retention may be a basic cellular mechanism exploited by HIV-1
Measurement of the branching fraction and CP content for the decay B(0) -> D(*+)D(*-)
This is the pre-print version of the Article. The official published version can be accessed from the links below. Copyright @ 2002 APS.We report a measurement of the branching fraction of the decay B0âD*+D*- and of the CP-odd component of its final state using the BABAR detector. With data corresponding to an integrated luminosity of 20.4ââfb-1 collected at the ΄(4S) resonance during 1999â2000, we have reconstructed 38 candidate signal events in the mode B0âD*+D*- with an estimated background of 6.2±0.5 events. From these events, we determine the branching fraction to be B(B0âD*+D*-)=[8.3±1.6(stat)±1.2(syst)]Ă10-4. The measured CP-odd fraction of the final state is 0.22±0.18(stat)±0.03(syst).This work is supported by DOE and NSF (USA), NSERC (Canada), IHEP (China), CEA and CNRS-IN2P3 (France), BMBF (Germany), INFN (Italy), NFR (Norway), MIST (Russia), and PPARC (United Kingdom). Individuals have received support from the A.P. Sloan Foundation, Research Corporation, and Alexander von Humboldt Foundation
Measurement of the B0-anti-B0-Oscillation Frequency with Inclusive Dilepton Events
The - oscillation frequency has been measured with a sample of
23 million \B\bar B pairs collected with the BABAR detector at the PEP-II
asymmetric B Factory at SLAC. In this sample, we select events in which both B
mesons decay semileptonically and use the charge of the leptons to identify the
flavor of each B meson. A simultaneous fit to the decay time difference
distributions for opposite- and same-sign dilepton events gives ps.Comment: 7 pages, 1 figure, submitted to Physical Review Letter
Measurement of D-s(+) and D-s(*+) production in B meson decays and from continuum e(+)e(-) annihilation at âs=10.6 GeV
This is the pre-print version of the Article. The official published version can be accessed from the links below. Copyright @ 2002 APSNew measurements of Ds+ and Ds*+ meson production rates from B decays and from qqÌ
continuum events near the ΄(4S) resonance are presented. Using 20.8 fb-1 of data on the ΄(4S) resonance and 2.6 fb-1 off-resonance, we find the inclusive branching fractions B(BâDs+X)=(10.93±0.19±0.58±2.73)% and B(BâDs*+X)=(7.9±0.8±0.7±2.0)%, where the first error is statistical, the second is systematic, and the third is due to the Ds+âÏÏ+ branching fraction uncertainty. The production cross sections Ï(e+e-âDs+X)ĂB(Ds+âÏÏ+)=7.55±0.20±0.34pb and Ï(e+e-âDs*±X)ĂB(Ds+âÏÏ+)=5.8±0.7±0.5pb are measured at center-of-mass energies about 40 MeV below the ΄(4S) mass. The branching fractions ÎŁB(BâDs(*)+D(*))=(5.07±0.14±0.30±1.27)% and ÎŁB(BâDs*+D(*))=(4.1±0.2±0.4±1.0)% are determined from the Ds(*)+ momentum spectra. The mass difference m(Ds+)-m(D+)=98.4±0.1±0.3MeV/c2 is also measured.This work was supported by DOE and NSF (USA), NSERC (Canada), IHEP (China), CEA and CNRS-IN2P3 (France), BMBF (Germany), INFN (Italy), NFR (Norway), MIST (Russia), and PPARC (United Kingdom). Individuals have received support from the Swiss NSF, A. P. Sloan Foundation, Research Corporation, and Alexander von Humboldt Foundation
Enzymatic Degradation of PrPSc by a Protease Secreted from Aeropyrum pernix K1
BACKGROUND: An R30 fraction from the growth medium of Aeropyrum pernix was analyzed for the protease that can digest the pathological prion protein isoform (PrP(Sc)) from different species (human, bovine, deer and mouse). METHODOLOGY/PRINCIPAL FINDINGS: Degradation of the PrP(Sc) isoform by the R30 fraction and the purified protease was evaluated using the 6H4 anti-PrP monoclonal antibody. Fragments from the N-terminal and C-terminal of PrP(Sc) were also monitored by Western blotting using the EB8 anti-PrP monoclonal antibody, and by dot blotting using the C7/5 anti-PrP monoclonal antibody, respectively. For detection of smaller peptides from incomplete digestion of PrP(Sc), the EB8 monoclonal antibody was used after precipitation with sodium phosphotungstate. Characterization of the purified active protease from the R30 fraction was achieved, through purification by fast protein liquid chromatography, and identification by tandem mass spectrometry the serine metalloprotease pernisine. SDS-PAGE and zymography show the purified pernisine plus its proregion with a molecular weight of ca. 45 kDa, and the mature purified pernisine as ca. 23 kDa. The purified pernisine was active between 58 °C and 99 °C, and between pH 3.5 and 8.0. The temperature and pH optima of the enzymatic activity of the purified pernisine in the presence of 1 mM CaCl(2) were 105 °C ± 0.5 °C and pH 6.5 ± 0.2, respectively. CONCLUSIONS/SIGNIFICANCE: Our study has identified and characterized pernisine as a thermostable serine metalloprotease that is secreted from A. pernix and that can digest the pathological prion protein PrP(Sc)
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