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Reduced graphene oxide-zinc oxide composite (rGO-ZnO) was incorporated at 0.2 mass% content in immiscible 1:1 poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV)/ poly(ethylene-co-vinyl acetate) (EVA) blends by melt extrusion. Using the same conditions, samples of PHBV, EVA, the neat blend and plasticized hybrids were also obtained. The effect of rGO-ZnO and the plasticizers, acetyl tert-butyl citrate (ATBC) and ionic 1-butyl-3-methylimidazolium hexafluorophosphate (bmim+PF6ˉ), on the properties of the hybrid materials were evaluated. X-ray diffraction results indicated that rGO-ZnO and the plasticizers affected the materials crystallinity. Differential scanning calorimetry showed that rGO-ZnO influenced the melt and cold crystallization, functioning as heterogeneous nucleating agent for PHBV. Dynamic mechanical analyses revealed improved compatibilization by adding ATBC to the hybrid blend. Using bmim+PF6ˉ as the plasticizer led to hybrid materials with significantly better oxygen barrier properties, similar to polyethylene.
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Murine macrophage-like RAW 264.7 cells studied with ATR-FTIR. Control group was treated with phosphate-buffered saline (0.9% PBS; Sigma, USA), CpG DNA stimulated group was treated with 1 µM K3 ODN (Endotoxin-free; Integrated DNA Technologies, Belgium), and LPS stimulated group was treated with 0.5 µg/ml LPS (Sigma, USA). Four different times points following treatment were used for measurements to evaluate the kinetics of induced effects: 10 min, 30 min, 2 h, and 6 h.
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Supplemental Figure 1. Cutaneous T-cell lymphoma (CTCL) progression on dupilumab, Case 1: 64- year-old man with presumed atopic dermatitis later found to be CTCL A) prior to receiving dupilumab and B) erythrodermic after 8 months on dupilumab.
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Movies in animated GIF format showing the binding kinetics of human beta-amyloid fibrils of various sizes, derived from NMR structures (PDB: 2BEG), to phase separated lipid rafts consisting of saturated (DPPC) and unsaturated (DLPC) phospholipids, cholesterol (CHOL), head-group (C1-CHOL) or tail-group (P1-CHOL) modified cholesterol. These modified cholesterols mimic the oxidized cholesterols. The GM1 rafts contain asymmetrically distributed monosialotetrahexosylganglioside (GM1) clusters. These movies show coarse-grained (CG) MD simulations of fibril/raft complexes as described in Cheng et al. "Coarse-Grained MD Simulations Reveal Beta-Amyloid Fibrils of Various Sizes Bind to Interfacial Liquid-Ordered and Liquid-Disordered Regions in Phase Separated Lipid Rafts with Diverse Membrane-Bound Conformational States" Biophysical Chemistry 2020 in press (DOI: 10.1016/j.bpc.2020.106355). Each movie contains 500 frames, with a time step of 40 ns, spanning 0 to 20 microseconds of CG MD simulations. Periodic membrane structures along the z-axis are shown. The lipid acyl chains are not shown for clarity. The membrane-bound states include: C, T, N, I and L, and these states refer to the segment of the fibril that binds to the lipid membrane via the C-terminal, C-and N-termini, N-terminal, transmembrane-insertion along the C- and N-terminals, and loop region, respectively. 1. 01-CO-ABCD-2-0to20us-hgrs.gif A movie of a tetramer fibril (4 chains - ABCD) binding to a lipid raft (DPPC/DLPC/CHOL). The fibril starts from solution, binds to membrane at 4.2 microseconds, and establishes an equilibrated membrane-bound C-state. 2. 02-CO-ABCD-3-0to20us-hgrs.gif A movie of tetramer fibril (4 chains - ABCD) binding to a lipid raft (DPPC/DLPC/CHOL). The fibril starts from solution, binds to membrane at 0.4 microseconds, and establishes an equilibrated membrane-bound T-state. 3. 03-C1-ABC-3-0to20us-hgrs.gif A movie of a trimer fibril (3 chains - ABC) binding to a lipid raft (DPPC/DLPC/C1-CHOL). The fibril starts from solution, binds to membrane at 0.7 microseconds, and establishes an equilibrated membrane-bound N-state. 4. 04-P1-ABC-2-0to20us-hgrs.gif A movie of trimer fibril (3 chain - ABC) binding to a lipid raft (DPPC/DLPC/P1-CHOL). The fibril starts from solution, binds to membrane at 0.3 microseconds, and establishes an equilibrated membrane-bound I-state. 5. 05-GM-ABCD-1-0to20us-hgrs.gif A movie of a tetramer (ABCD) fibril binding to an asymmetrical lipid raft (DPPC/DLPC/CHOL/GM1). The fibril starts from solution, binds to membrane at 0.2 microseconds, and establishes an equilibrated membrane-bound C-state. 6. 06-GM-ABCD-2-0to2us-hgrs.gif A movie of a tetramer (ABCD) fibril binding to an asymmetrical lipid raft (DPPC/DLPC/CHOL/GM1). The fibril starts from solution, binds to asymmetric GM1 cluster at 1 microsecond, and establishes an equilibrated membrane-bound L-state.
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The aim of this study is to utilize reverse engineering approach for the identification of the elements and phases available on the commercial CERMET inserts with the help of characterization techniques such as Scanning Electron Microscope (SEM), Energy-dispersive X-ray spectroscopy (EDS), and X-Ray Deposition (XRD). Four commercial CERMET inserts were investigated in this research work and the effect of the composition and phases are related to it’s tool wear mechanism and performance. Each CERMET insert is used to perform a turning process on a CNC lathe for machining stainless steel (SS) under dry condition at a fix cutting length interval. Once it completes machining for a fix cutting length, the CERMET insert is taken out to investigate its wear mechanism with the help of SEM, EDS, XRD and using focus-variation microscope (Alicona). A correlation study is performed to relate progressive tool wear mechanism with elements and their relevant phases of various carbides. The approach of corelating wear property with the phase content will contribute for understanding of the wear mechanism under such extreme machining conditions. It will serve as a reference for the improvement of the performance of these CERMET inserts for such harsh machining condition by development of protective coatings for these CERMET inserts based on the identification of the composition and phases that improves tool life and reduces wear.
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This data comprises the full simulation and analysis protocol performed as a part of this work. A README file is contained with a drectory structure and guildlines.
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This is the primary data used in our publication by Kori et al., 2020
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This raw data is related to the identification of proteins produced directly into water by three Pseudomonas strains: Fl4BN1, Fl4BN2 and Fl5BN2. The folder entitled "MS" contains all the Mascot searches linked to Data in Brief Table 5. The folder entitled "MS-MS" contains two subfolders linked to Data in Brief Table 6-11: "NCBI" and "SwissProt" related to searches performed using NCBI and SwissProt databases, respectively. The search was carried out in the "bacteria" database reviewed (_R) or not (_NR) and in the "P. protegens" database.
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Stack of 2D reconstructed X-Ray Microtomography images of the plant remain sample SMC_02 from Monte Castelo archaeological site (RO), Brazil. X-Ray MicroCT System: v|tome|x m (LG) Museum of Zoology, University of São Paulo (MZ-USP) Source voltage (keV): 60.0 Source current (µA): 180.0 Exposure time/projection (s): 1.0 Number of projections (n): 1000 Total scan angles (n): 360 Filters: none Pixel size (µm): 2.84 Source to sample distance (FOD) (mm): 11.548 Source to detector distance (FDD) (mm): 814.075 Reconstruction software: x|datos; slightly enhanced using FIJI-ImageJ Technical support Alberto B. Carvalho Image credits: Calo, C. M. and Rizzutto M. A.
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We hypothesize that biotin favors BCAA utilization and its deficiency accumulates BCAA to prolong autophagy inhibition and ER stress by chronic activation of mTORC1. Ganesan, D, Ramaian Santhaseela, A, Rajasekaran, S, Selvam, S, Jayavelu, T. Astroglial biotin deprivation under endoplasmic reticulum stress uncouples BCAA‐mTORC1 role in lipid synthesis to prolong autophagy inhibition in the aging brain. J. Neurochem. 2020; 00: 1– 14. https://doi.org/10.1111/jnc.14979
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