3,223 research outputs found

    A Near-Infrared L Band Survey of the Young Embedded Cluster NGC 2024

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    We present the results of the first sensitive L band (3.4 micron) imaging study of the nearby young embedded cluster NGC 2024. Two separate surveys of the cluster were acquired in order to obtain a census of the circumstellar disk fraction in the cluster. From an analysis of the JHKL colors of all sources in our largest area, we find an infrared excess fraction of > 86%. The JHKL colors suggest that the infrared excesses arise in circumstellar disks, indicating that the majority of the sources which formed in the NGC 2024 cluster are currently surrounded by, and likely formed with circumstellar disks. The excess fractions remain very high, within the errors, even at the faintest L magnitudes from our deeper surveys suggesting that disks form around the majority of the stars in very young clusters such as NGC 2024 independent of mass. From comparison with published JHKL observations of Taurus, we find the K - L excess fraction in NGC 2024 to be consistent with a high initial incidence of circumstellar disks in both NGC 2024 and Taurus. Because NGC 2024 represents a region of much higher stellar density than Taurus, this suggests that disks may form around most of the YSOs in star forming regions independent of environment. We find a relatively constant JHKL excess fraction with increasing cluster radius, indicating that the disk fraction is independent of location in the cluster. In contrast, the JHK excess fraction increases rapidly toward the central region of the cluster, and is most likely due to contamination of the K band measurements by bright nebulosity in the central regions of the cluster. We identify 45 candidate protostellar sources in the central regions of the NGC 2024 cluster, and find a lower limit on the protostellar phase of early stellar evolution of 0.4 - 1.4 X 10^5 yr, similar to that in Taurus.Comment: 37 pages, 8 figures, 3 tables, To appear in the Astronomical Journa

    Model Selection in Variational Mixed Effects Models

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    Variational inference is an alternative estimation technique for Bayesian models. Recent work shows that variational methods provide consistent estimation via efficient, deterministic algorithms. Other tools, such as model selection using variational AICs (VAIC) have been developed and studied for the linear regression case. While mixed effects models have enjoyed some study in the variational context, tools for model selection are lacking. One important feature of model selection in mixed effects models, particularly longitudinal models, is the selection of the random effects which in turn determine the covariance structure for the repeatedly sampled outcome. To address this, we derive a VAIC specifically for variational mixed effects (VME) models. We also implement a parameter-efficient VME as part of our study which reduces any general random effects structure down to a single subject-specific score. This model accommodates a wide range of random effect structures including random intercept and slope models as well as random functional effects. Our VAIC can model and perform selection on a variety of VME models including more classic longitudinal models as well as longitudinal scalar-on-function regression. As we demonstrate empirically, our VAIC performs well in discriminating between correctly and incorrectly specified random effects structures. Finally, we illustrate the use of VAICs for VMEs on two datasets: a study of lead levels in children and a study of diffusion tensor imaging

    The Trypanosoma cruzi enzyme TcGPXI is a glycosomal peroxidase and can be linked to trypanothione reduction by glutathione or tryparedoxin.

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    Trypanosoma cruzi glutathione-dependent peroxidase I (TcGPXI) can reduce fatty acid, phospholipid, and short chain organic hydroperoxides utilizing a novel redox cycle in which enzyme activity is linked to the reduction of trypanothione, a parasite-specific thiol, by glutathione. Here we show that TcGPXI activity can also be linked to trypanothione reduction by an alternative pathway involving the thioredoxin-like protein tryparedoxin. The presence of this new pathway was first detected using dialyzed soluble fractions of parasite extract. Tryparedoxin was identified as the intermediate molecule following purification, sequence analysis, antibody studies, and reconstitution of the redox cycle in vitro. The system can be readily saturated by trypanothione, the rate-limiting step being the interaction of trypanothione with the tryparedoxin. Both tryparedoxin and TcGPXI operate by a ping-pong mechanism. Overexpression of TcGPXI in transfected parasites confers increased resistance to exogenous hydroperoxides. TcGPXI contains a carboxyl-terminal tripeptide (ARI) that could act as a targeting signal for the glycosome, a kinetoplastid-specific organelle. Using immunofluorescence, tagged fluorescent proteins, and biochemical fractionation, we have demonstrated that TcGPXI is localized to both the glycosome and the cytosol. The ability of TcGPXI to use alternative electron donors may reflect their availability at the corresponding subcellular sites

    Site-specific identification and quantitation of endogenous SUMO modifications under native conditions.

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    Small ubiquitin-like modifier (SUMO) modification regulates numerous cellular processes. Unlike ubiquitin, detection of endogenous SUMOylated proteins is limited by the lack of naturally occurring protease sites in the C-terminal tail of SUMO proteins. Proteome-wide detection of SUMOylation sites on target proteins typically requires ectopic expression of mutant SUMOs with introduced tryptic sites. Here, we report a method for proteome-wide, site-level detection of endogenous SUMOylation that uses α-lytic protease, WaLP. WaLP digestion of SUMOylated proteins generates peptides containing SUMO-remnant diglycyl-lysine (KGG) at the site of SUMO modification. Using previously developed immuno-affinity isolation of KGG-containing peptides followed by mass spectrometry, we identified 1209 unique endogenous SUMO modification sites. We also demonstrate the impact of proteasome inhibition on ubiquitin and SUMO-modified proteomes using parallel quantitation of ubiquitylated and SUMOylated peptides. This methodological advancement enables determination of endogenous SUMOylated proteins under completely native conditions
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