نتایج جستجو برای: rdx
تعداد نتایج: 933 فیلتر نتایج به سال:
Cyclic nitramine hexahydro-1,3,5-trinitro-s-triazine (RDX), is an important energetic ingredient for propellants and explosives. To understand RDX explosive nature, the molecular structure needs to be examined in detail. Solid state RDX exist as three polymorphs: α, β and γ. The α-form is the stable polymorph at room temperature with Cs symmetry, β-polymorph has a molecular symmetry of C3v and ...
Heart failure is characterized by the loss of sympathetic innervation to the ventricles, contributing to impaired cardiac function and arrhythmogenesis. We hypothesized that renal denervation (RDx) would reverse this loss. Male Wistar rats underwent myocardial infarction (MI) or sham surgery and progressed into heart failure for 4 wk before receiving bilateral RDx or sham RDx. After additional ...
Previously, we hypothesized that hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) can be biotransformed by anaerobic sludge via three different routes: (1) direct ring cleavage via alpha-hydroxylation of a-CH(2) group, (2) reduction of one of the -NO(2) groups to -NO, (3) N-denitration prior to ring cleavage. The present study describes biotransformation of RDX via route 3 by a diaphorase (EC 1.8....
Decomposition of γ-cyclotrimethylene trinitramine (γ-RDX) under high pressure-high temperature conditions was examined to elucidate the reactive behavior of RDX crystals. Vibrational spectroscopy measurements were obtained for single crystals in a diamond anvil cell (DAC) at pressures from 6 to 12 GPa and temperatures up to 600 K. Global decomposition rates, activation energies, and activation ...
Shewanella halifaxensis and Shewanella sediminis were among a few aquatic gamma-proteobacteria that were psychrophiles and the first anaerobic bacteria that degraded hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX). Although many mesophilic or psychrophilic strains of Shewanella and gamma-proteobacteria were sequenced for their genomes, the genomic evolution pathways for temperature adaptation wer...
Polyclonal and monoclonal antibodies were raised to protein carrier molecules haptenized with RDX, a major component of many plastic explosives including Semtex. Sera from immunized mice detected RDX protein conjugates in standard ELISA. Clonally purified monoclonal antibodies had detection limits in the sub-ng/mL range for underivatized RDX in competition ELISA. The monoclonal antibodies are n...
The explosive-degrading cytochrome P450 system is highly conserved among strains of Rhodococcus spp.
Hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) is a widely used explosive and a serious environmental pollutant. Nineteen strains of Rhodococcus spp. capable of utilizing RDX as the sole nitrogen source have been isolated. The cytochrome P450 system XplA-XplB, which is responsible for RDX breakdown, is present in 18 of these strains.
The final step in Hedgehog (Hh) signal transduction is post-translational regulation of the transcription factor, Cubitus interruptus (Ci). Ci resides in the cytoplasm in a latent form, where Hh regulates its processing into a transcriptional repressor or its nuclear access as a transcriptional activator. Levels of latent Ci are controlled by degradation, with different pathways activated in re...
The electrostatic hazards of nitramine explosives (RDX, HMX) were assessed in this paper. The resistivities of different particle-size RDX and HMX were tested by a device designed and manufactured according to the standard ISO/ IEC 80079-20-2:2016. This work shows that the resistivities of uncompacted RDX and HMX increase as the particle size decreases. Charging characteristics test experiments...
In this paper, the decomposition reaction models and thermal hazard properties of 1,3,5-trinitro-1,3,5-triazinane (RDX) and its PBXs bonded by Formex P1, Semtex 1A, C4, Viton A and Fluorel polymer matrices have been investigated based on isoconversional and combined kinetic analysis methods. The established kinetic triplets are used to predict the constant decomposition rate temperature profile...
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