Adlerharper0262

In this study, the association of expressional alterations in neuronal G protein-coupled receptors (GPCRs) with induction of protective response to polystyrene nanoparticles (PS-NPs) was investigated in Caenorhabditis elegans. On the basis of both phenotypic analysis and expression levels, the alterations in expressions of NPR-1, NPR-4, NPR-8, NPR-9, NPR-12, DCAR-1, GTR-1, DOP-2, SER-4, and DAF-37 in neuronal cells mediated the protective response to PS-NPs exposure. In neuronal cells, NPR-9, NPR-12, DCAR-1, and GTR-1 controlled the PS-NPs toxicity by activating or inhibiting JNK-1/JNK MAPK signaling. Neuronal NPR-8, NPR-9, DCAR-1, DOP-2, and DAF-37 controlled the PS-NPs toxicity by activating or inhibiting MPK-1/ERK MAPK signaling. Neuronal NPR-4, NPR-8, NPR-9, NPR-12, GTR-1, DOP-2, and DAF-37 controlled the PS-NPs toxicity by activating or inhibiting DBL-1/TGF-β signaling. Neuronal NPR-1, NPR-4, NPR-12, and GTR-1 controlled the PS-NPs toxicity by activating or inhibiting DAF-7/TGF-β signaling. Our data provides an important neuronal basis for induction of protective response to PS-NPs in C. elegans.The two sulfonyl-bridged Geländer helices 1a and 2a are obtained by oxidation of the corresponding sulfide bridged precursors 1b and 2b. Both Geländer structures are fully characterized by NMR, high-resolution mass spectrometry, and optical spectroscopies. X-ray diffraction with a single crystal of 2a provides its solid-state structure. Both Geländer helices 1a and 2a are separated into enantiomers, and their racemizations are monitored by circular dichroism. For 1a, consisting of two equally sized macrocycles, a substantial increase in the enantiomerization barrier is observed upon going from the sulfide to the sulfone, and only a subtle rise is detected for the constitutional isomer 2a with two macrocycles of different size during the same transformation. This results not only in 1a with the highest configurational stability in the series of hitherto investigated Geländer structures but also challenges the so far hypothesized correlations between bridging structures and the Gibbs free energy of enantiomerization. The simulation of the enantiomerization process in the macrocyclic subunits suggests the proximity of the endotopic hydrogens as parameter responsible for the heights of the enantiomerization barrier.The excess electron in solution is a highly reactive radical involved in various radiation-induced reactions. Its solvation state critically determines the subsequent pathway and rate of transfer. For instance, water plays a dominating role in the electron-induced dealkylation of n-tributyl phosphate in actinide extraction processing. However, the underlying electron solvation processes in such systems are lacking. Herein, we directly observed the solvation dynamics of electrons in H-bonded water and n-tributyl phosphate (TBP) binary solutions with a mole fraction of water (X w ) varying from 0.05 to 0.51 under ambient conditions. Following the evolution of the absorption spectrum of trapped electrons (not fully solvated) with picosecond resolution, we show that electrons statistically distributed would undergo preferential solvation within water molecules extracted in TBP. We determine the time scale of excess electron full solvation from the deconvoluted transient absorption-kinetical data. The process of solvent reorganization accelerates by increasing the water molar fraction, and the rate of this process is 2 orders of magnitude slower compared to bulk water. We assigned the solvation process to hydrogen network reorientation induced by a negative charge of the excess electron that strongly depends on the local water environment. Our findings suggest that water significantly stabilizes the electron in a deeper potential than the pure TBP case. In its new state, the electron is likely to inhibit the dealkylation of extractants in actinide separation.Top-down mass spectrometry (TD-MS) of peptides and proteins results in product ions that can be correlated to polypeptide sequence. Fragments can either be terminal fragments, which contain either the N- or the C-terminus, or internal fragments that contain neither termini. Normally, only terminal fragments are assigned due to the computational difficulties of assigning internal fragments. Here we describe ClipsMS, an algorithm that can assign both terminal and internal fragments generated by top-down MS fragmentation. Further, ClipsMS can be used to locate various modifications on the protein sequence. Using ClipsMS to assign TD-MS generated product ions, we demonstrate that for apo-myoglobin, the inclusion of internal fragments increases the sequence coverage up to 78%. Interestingly, many internal fragments cover complementary regions to the terminal fragments that enhance the information that is extracted from a single top-down mass spectrum. Analysis of oxidized apo-myoglobin using terminal and internal fragment matching by ClipsMS confirmed the locations of oxidation sites on the two methionine residues. Internal fragments can be beneficial for top-down protein fragmentation analysis, and ClipsMS can be a valuable tool for assigning both terminal and internal fragments present in a top-down mass spectrum. Data are available via the MassIVE community resource with the identifiers MSV000086788 and MSV000086789.The study of hard-particle packings is of fundamental importance in physics, chemistry, cell biology, and discrete geometry. Much of the previous work on hard-particle packings concerns their densest possible arrangements. By contrast, we examine kinetic effects inevitably present in both numerical and experimental packing protocols. Terfenadine Potassium Channel inhibitor Specifically, we determine how changing the compression/shear rate of a two-dimensional packing of noncircular particles causes it to deviate from its densest possible configuration, which is always periodic. The adaptive shrinking cell (ASC) optimization scheme maximizes the packing fraction of a hard-particle packing by first applying random translations and rotations to the particles and then isotropically compressing and shearing the simulation box repeatedly until a possibly jammed state is reached. We use a stochastic implementation of the ASC optimization scheme to mimic different effective time scales by varying the number of particle moves between compressions/shears. We generate dense, effectively jammed, monodisperse, two-dimensional packings of obtuse scalene triangle, rhombus, curved triangle, lens, and "ice cream cone" (a semicircle grafted onto an isosceles triangle) shaped particles, with a wide range of packing fractions and degrees of order.