15 research outputs found

    ERP profiles for face and word recognition are based on their status in semantic memory not their stimulus category

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    Previous research has suggested that faces and words are processed and remembered differently as reflected by different ERP patterns for the two types of stimuli. Specifically, face stimuli produced greater late positive deflections for old items in anterior compared to posterior regions, while word stimuli produced greater late positive deflections in posterior compared to anterior regions. Given that words have existing representations in subjects׳ long-term memories (LTM) and that face stimuli used in prior experiments were of unknown individuals, we conducted an ERP study that crossed face and letter stimuli with the presence or absence of a prior (stable or existing) memory representation. During encoding, subjects judged whether stimuli were known (famous face or real word) or not known (unknown person or pseudo-word). A surprise recognition memory test required subjects to distinguish between stimuli that appeared during the encoding phase and stimuli that did not. ERP results were consistent with previous research when comparing unknown faces and words; however, the late ERP pattern for famous faces was more similar to that for words than for unknown faces. This suggests that the critical ERP difference is mediated by whether there is a prior representation in LTM, and not whether the stimulus involves letters or faces

    Post-pneumonectomy syndrome: a systematic review of the current evidence and treatment options

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    Objectives: Post-pneumonectomy syndrome (PPS) is rare and predominantly characterised by dynamic airway obstruction due to mediastinal rotation at any time point following pneumonectomy. The objective of this systematic review was to identify the optimal treatment strategy for PPS based on subjective symptomatic relief, objective radiological imaging, and treatment durability. Methods: A systematic review was performed up to and including February 2022 based on the "Preferred Reporting Items for Systematic Reviews and Meta-Analyses" guidelines. All studies that presented the management of symptomatic patients > 16 years of age with radiologically confirmed PPS were included. The primary outcome was the identification of the optimal treatment strategy and the secondary outcome was durability of the treatment. The Oxford Centre for Evidence Based Medicine level was assigned to each study. Results: A total of 330 papers were identified and reviewed; 41 studies met the inclusion criteria. Data including patient demographics, indication for initial pneumonectomy, presenting symptoms, management approach, outcomes, and follow-up were assessed and analysed. Management approaches were divided into three categories: (a) mediastinal repositioning using implant prostheses; (b) endobronchial stenting; (c) other corrective procedures. One hundred and four patients were identified in total and of those, 87 underwent mediastinal repositioning with insertion of a prosthetic implant. Complications included over- or under-filling of the prosthesis (8.5%) and implant leakage (8.9%). Conclusion: Management of PPS using a prosthetic implant to reposition the mediastinum is the treatment of choice. Key adjuncts to optimise surgical approach and minimise complications include pre-operative CT volumetric analysis to guide implant size and intra-operative transoesophageal echocardiography to guide mediastinal repositioning.</p

    Fixed firefighting systems — Automatic sprinkler systems — Design, installation and maintenance

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    Key residues involved in electrostatic and hydrophobic interactions at the Src-Csk interface and recombinant Chk mutants generated. A. The five conserved basic residues in the αD-helix and αF-αG loop of Csk interact electrostatically and hydrophobically with Lys-442 and acidic and hydrophobic residues in the αH-αI loop, αI and αI’ helices of Src. The image was generated by Molsoft L.L.C. using the coordinates of the structure of Csk/Src complex (PDB ID: 3D7T). The C-terminal tail tyrosine (Tyr-527) is shown in green. B. Alignment showing the five conserved basic residues in the Csk and Chk sequences. Lys-442 and the C-terminal tail sequence of Src at the Csk/Src interface are shown. The key residues participating in direct interactions with Csk are in red. C. Coomassie blue-stained gels showing the purity of purified Chk and its mutants used in this study. (TIFF 279 kb

    Additional file 10: Figure S9. of Csk-homologous kinase (Chk) is an efficient inhibitor of Src-family kinases but a poor catalyst of phosphorylation of their C-terminal regulatory tyrosine

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    Comparison of the molecular binding activities (M.B.A.) of Chk, Csk-Chk chimera and Csk. The M.B.A. values of Chk, Csk-Chk Chimera and Csk were plotted against at the designated concentrations used in the surface plasmon resonance spectroscopic analysis of the kinetics of their binding to the immobilised Hck (2PA-YEEI) (Figs. 4 and 5). Calculation of the M.B.A. values was presented in Additional file 8: Table S1. (TIFF 309 kb

    Additional file 1: Figure S1. of Csk-homologous kinase (Chk) is an efficient inhibitor of Src-family kinases but a poor catalyst of phosphorylation of their C-terminal regulatory tyrosine

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    Hypothetical conformations of the SFK and mutants used in this study. The two SFK members Src and Hck were chosen for our analyses. The N-terminal unique domain of both Src and Hck mutants is replaced by poly-His (His6) and Flag tags. For Src (K295M), Lys-295 critical to binding ATP is replaced by Met, hence the mutant is inactive. For Hck (2PA-YEEI), two conserved prolines in the SH2-kinase linker are replaced by alanines (referred to as the 2PA mutation), and the C-terminal YQQQP motif is replaced by the YEEIP motif (referred to as the YEEI mutation). The 2PA mutation prevents the Hck mutant from adopting the “closed” inactive conformation because the two conserved prolines are critical for intramolecular interactions between the PQKP motif with the SH3 domain. The mutant is therefore constitutively active. The YEEI mutation converts the motif around the C-terminal tail tyrosine into YEEIP motif which is an optimal phosphorylation sequence of SFKs. The constitutively active mutant undergoes autophosphorylation at both the conserved autophosphorylation site (YA) and the C-terminal tail tyrosine (YT). Upon phosphorylation, the pYEEIP motif can bind to the SH2 domain of the mutant with high affinity. Based upon the results of the structural and biochemical analyses of the Src and Hck mutants presented by Lerner, et al. [40] and Cowan-Jacob, et al. [82], the predicted conformations of the Src and Hck mutants are depicted in the left column. (TIFF 623 kb

    Additional file 3: of Csk-homologous kinase (Chk) is an efficient inhibitor of Src-family kinases but a poor catalyst of phosphorylation of their C-terminal regulatory tyrosine

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    Figure S7. Extracted ion chromatogram (XIC) for the C terminal peptide containing the Tyr-527 phosphorylation site of Src in the presence and absence of Csk. A-D Src (K295M) alone (A) Src (K295M) with Csk (B), Src alone (C) and Src with Csk (D) were incubated with ATP and assay buffer. Peptides are identified by Mascot in accordance of retention time. Retention time and mass error (ppm) are shown. E. Isotope dot product (idotp) comparing the observed and theoretical distribution of the precursor isotope with 1.0 being an optimal match. (TIFF 688 kb

    Additional file 14: Table S2. of Csk-homologous kinase (Chk) is an efficient inhibitor of Src-family kinases but a poor catalyst of phosphorylation of their C-terminal regulatory tyrosine

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    Identification of tryptic fragments derived from Src co- immunoprecipitated with Chk-GFP from the DLD-1-Chk-GFP cell lysate. Proteins immunoprecipitated from lysate of the DLD-1-Chk-GFP cells and that of the DLD-1-GFP cells (Control) were processed and digested with trypsin as described previously by Ang and Nice [56]. The tryptic fragments were analysed by LC-MS/MS as described in the experimental procedures. The SRC peptides identified by LC MS/MS and using the SEQUEST search engine are listed. A total of 4 different peptides were identified with high confidence at 1% FDR. The identify of these peptides were further validated with the Percolator algorithm for discrimination between correct and incorrect spectrum identifications as described by Kall, et al [84]. These fragments were not detected in the anti-GFP immunoprecipitate of the DLD-1-GFP cell lysate (Control lysate), suggesting that Src was specifically bound to Chk-GFP in the DLD-1-Chk-GFP cells. (PDF 93 kb

    Modeling of Cytosponge-TFF3 testing and risk stratification in the primary care population with reflux symptoms.

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    <p>Extrapolation of findings to a hypothetical population of 10,000 individuals with reflux symptoms using a sensitivity and specificity of 79.9% and 92.4%, respectively, for the TFF3 screen, and a sensitivity and specificity of 86% (95% CI of 65%–96%) and 100% (95% CI of 94.6%–100%), respectively, for <i>TP53</i> mutation screening for detection of HGD. The assumed prevalence of BE was 3%. In patients found to be high risk, endoscopy within 6–8 wk would be recommended. For low-risk patients, a repeat Cytosponge-TFF3 test would be performed at an interval of several years (exact timing to be determined) in case they had become TP53 positive over this time period. In the TFF3-negative arm, the repeat Cytosponge testing might not be necessary. If it took place, repeat testing would be recommended within 6 to 8 wk of the delivery of the TFF3-negative results.</p

    Sensitivity of the Cytosponge-TFF3 in different groups of patients (full dataset in S2 and S3 Tables).

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    <p>C, Circumferential length; IMC, intramucosal carcinoma; LGD, low grade dysplasia; M, maximal length; NDBE, non-dysplastic BE.</p><p>Sensitivity of the Cytosponge-TFF3 in different groups of patients (full dataset in <a href="http://www.plosmedicine.org/article/info:doi/10.1371/journal.pmed.1001780#pmed.1001780.s005" target="_blank">S2</a> and <a href="http://www.plosmedicine.org/article/info:doi/10.1371/journal.pmed.1001780#pmed.1001780.s006" target="_blank">S3</a> Tables).</p
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