The mission operations planning assistant

The Mission Operations Planning Assistant (MOPA) is a knowledge-based system developed to support the planning and scheduling of instrument activities on the Upper Atmospheric Research Satellite (UARS). The MOPA system represents and maintains instrument plans at two levels of abstraction in order to keep plans comprehensible to both UARS Prinicpal Investigators and Command Management personnel. The hierarchical representation of plans also allows MOPA to automatically create detailed instrument activity plans from which spacecraft command loads may be generated. The MOPA system was developed on a Symbolics 3640 computer using the ZETALISP and ART languages. MOPA's features include a textual and graphical interface for plan inspection and modification, recognition of instrument operational constraint violations during the planning process, and consistency maintenance between the different planning levels. This paper describes the current MOPA system

Atmospheric chemistry of gas-phase polycyclic aromatic hydrocarbons: formation of atmospheric mutagens.

The atmospheric chemistry of the 2- to 4-ring polycyclic aromatic hydrocarbons (PAH), which exist mainly in the gas phase in the atmosphere, is discussed. The dominant loss process for the gas-phase PAH is by reaction with the hydroxyl radical, resulting in calculated lifetimes in the atmosphere of generally less than one day. The hydroxyl (OH) radical-initiated reactions and nitrate (NO3) radical-initiated reactions often lead to the formation of mutagenic nitro-PAH and other nitropolycyclic aromatic compounds, including nitrodibenzopyranones. These atmospheric reactions have a significant effect on ambient mutagenic activity, indicating that health risk assessments of combustion emissions should include atmospheric transformation products

10-Hy­droxy-10-(1,3-thia­zol-2-ylmeth­yl)phenanthren-9(10H)-one

In the title phenanthrenone compound, C18H13NO2S, the dihydro­phenanthrene ring system is not planar, with its central ring distorted to a screw-boat conformation. The essentially planar thia­zole ring [maximum deviation = 0.005 (1) Å] is inclined at an inter­planar angle of 23.36 (5)° with respect to the mean plane through the dihydro­phenanthrene ring system. In the crystal packing, inter­molecular O—H⋯N hydrogen bonds link the mol­ecules into infinite chains along the a axis. Weak inter­molecular C—H⋯π inter­actions further stabilize the crystal packing

Capillary liquid chromatography with MS 3 for the determination of enkephalins in microdialysis samples from the striatum of anesthetized and freely–moving rats

In vivo microdialysis sampling was coupled to capillary liquid chromatography (LC)/electrospray ionization quadrupole ion trap mass spectrometry (MS) to monitor [Met]enkephalin and [Leu]enkephalin in the striatum of anesthetized and freely–moving rats. The LC system utilized a high-pressure pump to load 2.5 µl samples and desalt the 25 µm i.d. by 2 cm long column in 12 min. Samples were eluted with a separate pump at ∼100 nl min −1 . A rapid gradient effectively separated the endogenous neuropeptides in 4 min. A comparison was made for operating the mass spectrometer in the MS 2 and MS 3 modes for detection of the peptides. In standard solutions, the detection limits were similar at 1–2 pM (2–4 amol injected); however, the reproducibility was improved with MS 3 as the relative standard deviation was <5% compared with 20% for MS 2 for 60 pM samples. For dialysate solutions, reconstructed ion chromatograms and tandem mass spectra had much higher signal-to-noise ratios in the MS 3 mode, resulting in more confident detection at in vivo concentrations. The method was successfully used to monitor the peptides under basal conditions and with stimulation of peptide secretion by infusion of elevated K + concentration. Copyright © 2005 John Wiley & Sons, Ltd.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/35204/1/733_ftp.pd

Autoinflammatory mutation in NLRC4 reveals a leucine-rich repeat (LRR)-LRR oligomerization interface

Background Monogenic autoinflammatory disorders are characterized by dysregulation of the innate immune system, for example by gain-of-function mutations in inflammasome-forming proteins, such as NOD-like receptor family CARD-containing 4 protein (NLRC4). Objective Here we investigate the mechanism by which a novel mutation in the leucine-rich repeat (LRR) domain of NLRC4 (c.G1965C, p.W655C) contributes to autoinflammatory disease. Methods: We studied 2 unrelated patients with early-onset macrophage activation syndrome harboring the same de novo mutation in NLRC4. In vitro inflammasome complex formation was quantified by using flow cytometric analysis of apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC) specks. Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR)/Cas9 techniques and lentiviral transduction were used to generate THP-1 cells with either wild-type or mutant NLRC4 cDNA. Cell death and release of IL-1β/IL-18 were quantified by using flow cytometry and ELISA, respectively. Results The p.W655C NLRC4 mutation caused increased ASC speck formation, caspase-1–dependent cell death, and IL-1β/IL-18 production. ASC contributed to p.W655C NLRC4–mediated cytokine release but not cell death. Mutation of p.W655 activated the NLRC4 inflammasome complex by engaging with 2 interfaces on the opposing LRR domain of the oligomer. One key set of residues (p.D1010, p.D1011, p.L1012, and p.I1015) participated in LRR-LRR oligomerization when triggered by mutant NLRC4 or type 3 secretion system effector (PrgI) stimulation of the NLRC4 inflammasome complex. Conclusion This is the first report of a mutation in the LRR domain of NLRC4 causing autoinflammatory disease. c.G1965C/p.W655C NLRC4 increased inflammasome activation in vitro. Data generated from various NLRC4 mutations provides evidence that the LRR-LRR interface has an important and previously unrecognized role in oligomerization of the NLRC4 inflammasome complex