Feasibility and Acceptability of a Mobile-Based Emotion Recognition Approach for Bipolar Disorder

Over the past years, the mobile Health approach has motivated research projects to develop mood monitoring systems for bipolar disorder. Whereas mobile-based approaches have examined self-assessment or sensor data, so far, potentially important emotional aspects of this disease have been neglected. Thus, we developed an emotion-sensitive system that analyzes the verbal and facial expressions of bipolar patients in regard to their emotional cues. In this article, preliminary findings of a pilot study with five bipolar patients with respect to the acceptability and feasibility of the new approach are presented and discussed. There were individual differences in the usage frequency of the participants, and improvements regarding its handling were suggested. From the technical point of view, the video analysis was less dependable than the audio analysis and recognized almost exclusively the facial expressions of happiness. However, the system was feasible and well-accepted. The results indicate that further developments could facilitate the long-term analysis of expressed emotions in bipolar or other disorders without invading the privacy of patients

Emotion and performance

The study of emotions in organizational settings has attained considerable prominence in recent years, but I critical issue remains unresolved. This is the relationship between emotion and performance. in this special issue, 5 articles address this topic from a variety of viewpoints. Two are theoretical essays that deal, respectively, with emotion and creativity and the relationships between individual and team performance. Three are empirical studies that canvass the emotion-performance nexus across levels of analysis: within person, between persons, and in groups. Between them, the 5 articles present a strong case for the nexus of emotions and performance, but, more important, they provide a platform for potentially fruitful future research in this burgeoning area

Varicellovirus UL 49.5 proteins differentially affect the function of the transporter associated with antigen processing, TAP

Cytotoxic T-lymphocytes play an important role in the protection against viral infections, which they detect through the recognition of virus-derived peptides, presented in the context of MHC class I molecules at the surface of the infected cell. The transporter associated with antigen processing (TAP) plays an essential role in MHC class I–restricted antigen presentation, as TAP imports peptides into the ER, where peptide loading of MHC class I molecules takes place. In this study, the UL49.5 proteins of the varicelloviruses bovine herpesvirus 1 (BHV-1), pseudorabies virus (PRV), and equine herpesvirus 1 and 4 (EHV-1 and EHV-4) are characterized as members of a novel class of viral immune evasion proteins. These UL49.5 proteins interfere with MHC class I antigen presentation by blocking the supply of antigenic peptides through inhibition of TAP. BHV-1, PRV, and EHV-1 recombinant viruses lacking UL49.5 no longer interfere with peptide transport. Combined with the observation that the individually expressed UL49.5 proteins block TAP as well, these data indicate that UL49.5 is the viral factor that is both necessary and sufficient to abolish TAP function during productive infection by these viruses. The mechanisms through which the UL49.5 proteins of BHV-1, PRV, EHV-1, and EHV-4 block TAP exhibit surprising diversity. BHV-1 UL49.5 targets TAP for proteasomal degradation, whereas EHV-1 and EHV-4 UL49.5 interfere with the binding of ATP to TAP. In contrast, TAP stability and ATP recruitment are not affected by PRV UL49.5, although it has the capacity to arrest the peptide transporter in a translocation-incompetent state, a property shared with the BHV-1 and EHV-1 UL49.5. Taken together, these results classify the UL49.5 gene products of BHV-1, PRV, EHV-1, and EHV-4 as members of a novel family of viral immune evasion proteins, inhibiting TAP through a variety of mechanisms

A Purcell-enabled monolayer semiconductor free-space optical modulator

Dephasing and non-radiative decay processes limit the performance of a wide variety of quantum devices at room temperature. Here we illustrate a general pathway to notably reduce the detrimental impact of these undesired effects through photonic design of the device electrodes. Our design facilitates a large Purcell enhancement that speeds up competing, desired radiative decay while also enabling convenient electrical gating and charge injection functions. We demonstrate the concept with a free-space optical modulator based on an atomically thin semiconductor. By engineering the plasmonic response of a nanopatterned silver gate pad, we successfully enhance the radiative decay rate of excitons in a tungsten disulfide monolayer by one order of magnitude to create record-high modulation efficiencies for this class of materials at room temperature. We experimentally observe a 10% reflectance change as well as 3 dB signal modulation, corresponding to a 20-fold enhancement compared with modulation using a suspended monolayer in vacuum. We also illustrate how dynamic control of light fields can be achieved with designer surface patterns. This research highlights the benefits of applying radiative decay engineering as a powerful tool in creating high-performance devices that complements substantial efforts to improve the quality of materials.</p

JAZF1, A Novel p400/TIP60/NuA4 Complex Member, Regulates H2A.Z Acetylation at Regulatory Regions

Histone variants differ in amino acid sequence, expression timing and genomic localization sites from canonical histones and convey unique functions to eukaryotic cells. Their tightly controlled spatial and temporal deposition into specific chromatin regions is accomplished by dedicated chaperone and/or remodeling complexes. While quantitatively identifying the chaperone complexes of many human H2A variants by using mass spectrometry, we also found additional members of the known H2A.Z chaperone complexes p400/TIP60/NuA4 and SRCAP. We discovered JAZF1, a nuclear/nucleolar protein, as a member of a p400 sub-complex containing MBTD1 but excluding ANP32E. Depletion of JAZF1 results in transcriptome changes that affect, among other pathways, ribosome biogenesis. To identify the underlying molecular mechanism contributing to JAZF1's function in gene regulation, we performed genome-wide ChIP-seq analyses. Interestingly, depletion of JAZF1 leads to reduced H2A.Z acetylation levels at > 1000 regulatory sites without affecting H2A.Z nucleosome positioning. Since JAZF1 associates with the histone acetyltransferase TIP60, whose depletion causes a correlated H2A.Z deacetylation of several JAZF1-targeted enhancer regions, we speculate that JAZF1 acts as chromatin modulator by recruiting TIP60's enzymatic activity. Altogether, this study uncovers JAZF1 as a member of a TIP60-containing p400 chaperone complex orchestrating H2A.Z acetylation at regulatory regions controlling the expression of genes, many of which are involved in ribosome biogenesis

Crystallographic Orientation Relationship with Geometrically Necessary Dislocation Accumulation During High-Temperature Deformation in RR1000 Nickel-Based Superalloy

In the current study, it is demonstrated that soft grains along 〈100〉 fiber provided a pure shear condition for easy dislocation movement leading to a relatively low dislocation density. The hard grains along the 〈111〉 fiber, however, were not favorably oriented for slip system activation and caused high dislocation accumulation. It is concluded that the average overall dislocation density does not provide a meaningful value, as it is largely dependent on the original material crystallographic texture, the numbers of hard and soft grains in the electron backscatter diffraction (EBSD) mapped area, and the grain size factor

Inter-domain Communication Mechanisms in an ABC Importer: A Molecular Dynamics Study of the MalFGK2E Complex

ATP-Binding Cassette transporters are ubiquitous membrane proteins that convert the energy from ATP-binding and hydrolysis into conformational changes of the transmembrane region to allow the translocation of substrates against their concentration gradient. Despite the large amount of structural and biochemical data available for this family, it is still not clear how the energy obtained from ATP hydrolysis in the ATPase domains is “transmitted” to the transmembrane domains. In this work, we focus our attention on the consequences of hydrolysis and inorganic phosphate exit in the maltose uptake system (MalFGK2E) from Escherichia coli. The prime goal is to identify and map the structural changes occurring during an ATP-hydrolytic cycle. For that, we use extensive molecular dynamics simulations to study three potential intermediate states (with 10 replicates each): an ATP-bound, an ADP plus inorganic phosphate-bound and an ADP-bound state. Our results show that the residues presenting major rearrangements are located in the A-loop, in the helical sub-domain, and in the “EAA motif” (especially in the “coupling helices” region). Additionally, in one of the simulations with ADP we were able to observe the opening of the NBD dimer accompanied by the dissociation of ADP from the ABC signature motif, but not from its corresponding P-loop motif. This work, together with several other MD studies, suggests a common communication mechanism both for importers and exporters, in which ATP-hydrolysis induces conformational changes in the helical sub-domain region, in turn transferred to the transmembrane domains via the “coupling helices”

Discovery of an Auto-Regulation Mechanism for the Maltose ABC Transporter MalFGK2

The maltose transporter MalFGK2, together with the substrate-binding protein MalE, is one of the best-characterized ABC transporters. In the conventional model, MalE captures maltose in the periplasm and delivers the sugar to the transporter. Here, using nanodiscs and proteoliposomes, we instead find that MalE is bound with high-affinity to MalFGK2 to facilitate the acquisition of the sugar. When the maltose concentration exceeds the transport capacity, MalE captures maltose and dissociates from the transporter. This mechanism explains why the transport rate is high when MalE has low affinity for maltose, and low when MalE has high affinity for maltose. Transporter-bound MalE facilitates the acquisition of the sugar at low concentrations, but also captures and dissociates from the transporter past a threshold maltose concentration. In vivo, this maltose-forced dissociation limits the rate of transport. Given the conservation of the substrate-binding proteins, this mode of allosteric regulation may be universal to ABC importers