Table_1_Nonverbal cues to deception: insights from a mock crime scenario in a Chinese sample.DOCX

Nonverbal behaviors could play a crucial role in detecting deception, yet existing studies on deception cues have largely centered on Western populations, predominantly university students, thus neglecting the influence of cultural and sample diversity. To address this gap, our study explored deception cues within an Asian cultural setting, utilizing a mock crime paradigm. Our sample comprised Chinese participants, including both men and women with various socioeconomic status (SES) backgrounds. Our findings revealed that compared to truth tellers, liars exhibited heightened emotions and an increased cognitive load. Furthermore, liars showed a higher frequency of self-adaptors and a longer duration of gaze aversion. Our findings contribute to a more profound understanding of deception cues within Asian culture and have implications for practical fields such as criminal interrogation.</p

Near-Infrared Light Activation of Proteins Inside Living Cells Enabled by Carbon Nanotube-Mediated Intracellular Delivery

Light-responsive proteins have been delivered into the cells for controlling intracellular events with high spatial and temporal resolution. However, the choice of wavelength is limited to the UV and visible range; activation of proteins inside the cells using near-infrared (NIR) light, which has better tissue penetration and biocompatibility, remains elusive. Here, we report the development of a single-walled carbon nanotube (SWCNT)-based bifunctional system that enables protein intracellular delivery, followed by NIR activation of the delivered proteins inside the cells. Proteins of interest are conjugated onto SWCNTs via a streptavidin-desthiobiotin (SA-DTB) linkage, where the protein activity is blocked. SWCNTs serve as both a nanocarrier for carrying proteins into the cells and subsequently a NIR sensitizer to photothermally cleave the linkage and release the proteins. The released proteins become active and exert their functions inside the cells. We demonstrated this strategy by intracellular delivery and NIR-triggered nuclear translocation of enhanced green fluorescent protein, and by intracellular delivery and NIR-activation of a therapeutic protein, saporin, in living cells. Furthermore, we showed that proteins conjugated onto SWCNTs via the SA-DTB linkage could be delivered to the tumors, and optically released and activated by using NIR light in living mice

Visualisation and Identification of the Interaction between STIM1s in Resting Cells

<div><p>Store-operated Ca²⁺ channels are a major Ca²⁺ entry pathway in nonexcitable cells, which drive various essential cellular functions. Recently, STIM1 and Orai proteins have been identified as the major molecular components of the Ca²⁺ release-activated Ca²⁺ (CRAC) channel. As the key subunit of the CRAC channel, STIM1 is the ER Ca²⁺ sensor and is essential for the recruitment and activation of Orai1. However, the mechanisms in transmission of information of STIM1 to Orai1 still need further investigation. Bimolecular fluorescence complementation (BiFC) is one of the most advanced and powerful tools for studying and visualising protein-protein interactions in living cells. We utilised BiFC and acceptor photobleaching fluorescence resonance energy transfer (FRET) experiments to visualise and determine the state of STIM1 in the living cells in resting state. Our results demonstrate that STIM1 exists in an oligomeric form in resting cells and that rather than the SAM motif, it is the C-terminus (residues 233–474) of STIM1 that is the key domain for the interaction between STIM1s. The STIM1 oligomers (BiFC-STIM1) and wild-type STIM1 colocalised and had a fibrillar distribution in resting conditions. Depletion of ER Ca²⁺ stores induced BiFC-STIM1 distribution to become punctate, an effect that could be prevented or reversed by 2-APB. After depletion of the Ca²⁺ stores, BiFC-STIM1 has the ability to form puncta that colocalise with wild-type STIM1 or Orai1 near the plasma membrane. Our data also indicate that the function of BiFC-STIM1 was not altered compared with that of wild-type STIM1.</p> </div

Functional validation of the fusion protein of BiFC-STIM1 in HEK293T cells.

<p>SOCE was assayed using Ca²⁺ microfluorimetry in HEK293T cells transfected with eYFP-STIM1 alone or with both VN173-ST1 and VC155-ST1 plasmids. The cells were first treated with TG (2 µM) in a Ca²⁺-free solution to empty the Ca²⁺ stores and subsequently switched to normal extracellular solution containing 2 mM Ca²⁺; this induced a transient increase in the cytosolic Ca²⁺ concentration. Part A: representative trace of Ca²⁺ dynamics in control HEK293T cells overexpressing pH-STIM1. Part B: representative trace of Ca²⁺ dynamics in cells cotransfected with both VN173-ST1 and VC155-ST1. Part C: mean data showing the effect of 50 µM 2-APB on SOCE from experiments such as those shown in A (n = 18 cells; **p<0.001). Part D: mean data showing the effect of 50 µM 2-APB on SOCE in experiments in part B (n = 18 cells; **p<0.001).</p

FRET measured by donor dequenching after acceptor photobleaching in HEK293T cells cotransfected with eCFP-STIM1 and eYFP-STIM1.

<p>Part A: CFP-STIM1 images before and after photobleaching of the acceptor within the indicated region (Left column); acceptor YFP-STIM1 intensities before and after photobleaching in the indicated region (Right column). Part B: images acquired near the cell adhesion surface after stimulation of cells with 2 µM TG. Part C: the bar graphs representing FRET efficiency (E) are from 20 independent experiments such as those in part A. The efficiency was determined by the acceptor photobleaching method and was measured only in the (acceptor) bleached area. Cells outside the bleached region were used as controls. Part D: the bar graphs representing FRET efficiency (E) are from the 20 independent experiments in part B. All data are represented as mean±S.D. The significance levels indicated are as follows: **P<0.001. Scale bars, 20 µm.</p

Visualisation of the STIM1-STIM1 interaction using a Venus-based BiFC system in resting mammalian cells.

<p>Part A shows the principles of the Venus BiFC system. The two non-fluorescent fragments of Venus, VN (N terminus of Venus) and VC (C terminus of Venus), are each fused to one of a pair of interacting (test) proteins, A and B. The fusion proteins, VN-A and VC-B, do not fluoresce when expressed separately. If proteins A and B interact or associate, the two fluorescent fragments are brought together, and this facilitates reconstruction of the fluorescent protein. Part B is a schematic view of the fusion protein constructs used in this study. WT-STIM1 and STIM1 mutants were fused to the N- and C-terminal fragments of Venus. The functional domains of STIM1 include an EF-hand, a SAM domain, a transmembrane domain, a coiled-coil (CC) region, an ERM domain, a Ser/Pro-rich domain (SP), and a polylysine residue region (K). Part C shows images of HEK293T cells 24 h after transfection with plasmids encoding VN173-ST1, VC155-ST1 or VN173-ST1/VC155-ST1 (full length STIM1). VN173-ST1 or VC155-ST1 expressed alone did not emit fluorescence under excitation, but coexpression of VN173-ST1 and VC155-ST1 produced strong yellow fluorescence emission. Part D shows HEK293T cells coexpressing VN173-ST1 and VC155-ST1 under resting and TG-stimulated conditions. Coexpression of VN173-ST1 and VC155-ST1 produced fluorescence that displayed a fibrillar distribution in resting cells and that became punctate and localised to the ER-PM junctions following stimulation of cells with 2 uM TG. Scale bars, 20 µm.</p

A C-terminal region of STIM1 (233–474) is critical for the oligomerisation of STIM1 in resting cells.

<p>Part A shows images of HEK293T cells cotransfected with the VN173-ST1 and VC155-ST1, VN173-ΔSAM and VC155-ΔSAM, or VN173-ΔC and VC155-ΔC constructs. Images were acquired 24 h after transfection. Part B shows quantitative analysis of Venus-based BiFC efficiency measured from experiments such as those shown in Part A. Part C shows that VN173-ST1 and VC155-ST1, VN173-ΔSAM and VC155-ΔSAM, or VN173-ΔC and VC155-ΔC constructs were cotransfected into HEK293T cells, respectively, and these proteins were detected by immunoblotting with anti-STIM1 Ab(Upper). Tubulin protein was detected as a loading control (Lower). All data are given as mean±S.D. (n>50). The statistical significance was evaluated using a two-tailed Student’s t-test when compared with the combination of VN173-ST1 and VC155-ST1. ST1, ΔC and ΔSAM represent full length STIM1, truncated STIM1-ΔC (Δ233–474) and STIM1-ΔSAM (Δ132–200), respectively. The significance level indicated is as follows: **P<0.001. Scale bar, 20 µm.</p

Reaction Kinetics of Ethylene Combustion in a Carbon Dioxide Stream over a Cu–Mn–O Hopcalite Catalyst in Low Temperature Range

The intrinsic kinetics of the catalytic combustion of a trace amount of ethylene in a CO₂ stream over a Cu–Mn–O catalyst prepared with a coprecipitation method is investigated. The experiments are carried out in a fixed-bed reactor with 0.3 g of catalyst in a low temperature range (470 to 620 K) and varying the concentration of C₂H₄ and O₂ in the feed stream. The power rate law, Langmuir–Hinshelwood (LH), Eley–Rideal (ER), and Mars–van Krevelen (MVK) models are compared. The residual error distribution of the ethylene conversion is employed to optimize the model equations. The extended MVK model containing desorption terms of the combustion products fit the data well. The pilot test with a fixed-bed reactor and a commercial feed stream is carried out, and the macro kinetic equations are obtained. Combined with the extended MVK model equations of the intrinsic kinetics, the effectiveness factor is calculated, which gives further prediction of the performance of the extruded catalyst under commercial conditions

2-APB reverses or prevents BiFC-STIM1 relocalisation to puncta near the plasma membrane.

<p>HEK293T cells were cotransfected with VN173-ST1 and VC155-ST1 constructs. After 24 h, live cells were examined under a confocal microscope at the cell footprint. Part A: VN173-ST1 and VC155-ST1 coexpressed in HEK293T cells redistributed from a fibrillar appearance (Rest) to puncta at the cell periphery after Ca²⁺ store depletion with TG. Puncta were visible at the cell footprint. The addition of 50 µM 2-APB rapidly reversed the relocalisation of BiFC-STIM1 to plasma membrane puncta (2-APB). Part B: 2-APB prevented BiFC-STIM1 relocalisation to puncta near the plasma membrane. Confocal imaging was carried out in experiments in which cells expressing BiFC-STIM1 were pretreated with 50 µM 2-APB for 5 min prior to store depletion with TG. Scale bars, 20 µm.</p

Ca²⁺ store depletion causes relocalisation of coexpressed BiFC-STIM1 and mCherry-STIM1, or coexpressed BiFC-STIM1 and Orai1-eCFP to ER-PM junctions to form colocalised puncta.

<p>Part A: HEK293T cells were cotransfected with VN173-ST1, VC155-ST1 and mCh-STIM1 constructs. Live cells were examined under a confocal microscope at the cell footprint. Confocal images of the same cells were taken before (Rest) and 3 min after addition of TG (TG). In resting cells, mCh-STIM1 and BiFC-STIM1 exhibited a colocalised fibrillar distribution (Rest). Ca²⁺ store depletion caused BiFC-STIM1 and mCh-STIM1 to form colocalised puncta. Part B: HEK293T cells were cotransfected with VN173-ST1, VC155-ST1 and Orai1-eCFP constructs. After Ca²⁺ store depletion, Orai1-eYFP accumulated with BiFC-STIM1 as puncta localised near the plasma membrane. Scale bars, 20 µm.</p