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https://www.selleckchem.com/products/Nolvadex.html Sulfur mustard (SM) has been the most frequently used chemical warfare agent. Here, we present the efficient containment of SM and its simulants by per-ethylated pillar[5]arene (EtP5). EtP5 exhibited strong binding abilities toward SM and its simulants not only in solution but also in the solid state. The association constant (Ka) between SM and EtP5 was determined as (6.2 ± 0.6) × 103 M-1 in o-xylene-d10. Single crystal structure of SM@EtP5 showed that a 11 inclusion complex was formed, which was driven by multiple C-H···π/Cl/S and S···π interactions. In addition, activated crystal materials of EtP5 (EtP5α) could effectively adsorb SM simulants at solid-vapor phase; powder X-ray diffraction patterns and host-guest crystal structures indicated that the uptake process triggered a solid-state structural transformation. More interestingly, the captured guest molecules could be stably contained in EtP5α for at least 6 months in air at room temperature.Events at a receptor ectodomain affect the intracellular domain conformation, activating signal transduction (out-to-in conformational effects). We investigated the reverse direction (in-to-out) where the intracellular domain may impact on ectodomain conformation. The primary sequences of naturally occurring TrkC receptor isoforms (TrkC-FL and TrkC.T1) only differ at the intracellular domain. However, owing to their differential association with Protein Disulfide Isomerase the isoforms have different disulfide bonding and conformations at the ectodomain. Conformations were exploited to develop artificial ligands, mAbs, and small molecules, with isoform-specific binding and biased activation. Consistent, the physiological ligands NT-3 and PTP-sigma bind both isoforms, but NT-3 activates all signaling pathways, whereas PTP-sigma activates biased signals. Our data support an "in-to-out" model controlling receptor ectodomain conformation, a strategy that enables heterogeneity

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