Given a context passage, generate a question from the passage such that its answer is shortest continous span from the passage.

Rates of remission were examined in two controlled 12-week studies of sertraline and placebo for post-traumatic stress disorder (PTSD). The performance of three scales was evaluated: the self-rated Davidson Trauma Scale (DTS), and two interviewer scales: the Clinician Administered PTSD Scale (CAPS) and Clinical Global Impressions (CGI). Sertraline proved significantly superior to placebo with respect to remission on all three ratings. Rates of remission were very similar for all scales, ranging from 23.1-26.3% for sertraline and 13.9-14.9% for placebo. Traditional thresholds for the CAPS and DTS were tested relative to the CGI and to each other. The CAPS and DTS thresholds of < 20 and < 18 were found to be valid.
Symptoms of which disorder are evaluated with the Davidson Trauma Scale?

In plant, primary transcripts (pri-miRNAs) transcribed from miRNA genes by RNA polymerase II are first processed into stem-loop pre-miRNAs and further chopped into 21nt long miRNAs by RNase III-like enzyme DCL1. SERRATE (SE) protein is an essential component for miRNA processing by assisting DCL1 for accurate cleavage. Here we report the crystal structure of Arabidopsis SE core (residues 194-543) at 2.7A. SE core adopts the 'walking man-like' topology with N-terminal helices, C-terminal non-canonical zinc-finger domain and novel Middle domain resembling the leading leg, the lagging leg and the body, respectively. Pull-down assay shows that SE core provides the platform for HYL1 and DCL1 binding, whereas in vitro RNA binding and in vivo mutant rescue experiments suggest that the non-canonical zinc-finger domain coupled with C-terminal tail binds miRNA precursors. SE presumably works as a scaffold-like protein capable of binding both protein and RNA to guide the positioning of miRNA precursor toward DCL1 catalytic site within miRNA processing machinery in plant.
Which polymerase transcribes pri-miRNAs?

Growth differentiation factor 15 (GDF15), a distant member of the transforming growth factor (TGF)- family, is a secreted protein that circulates as a 25-kDa dimer. In humans, elevated GDF15 correlates with weight loss, and the administration of GDF15 to mice with obesity reduces body weight, at least in part, by decreasing food intake. The mechanisms through which GDF15 reduces body weight remain poorly understood, because the cognate receptor for GDF15 is unknown. Here we show that recombinant GDF15 induces weight loss in mice fed a high-fat diet and in nonhuman primates with spontaneous obesity. Furthermore, we find that GDF15 binds with high affinity to GDNF family receptor -like (GFRAL), a distant relative of receptors for a distinct class of the TGF- superfamily ligands. Gfral is expressed in neurons of the area postrema and nucleus of the solitary tract in mice and humans, and genetic deletion of the receptor abrogates the ability of GDF15 to decrease food intake and body weight in mice. In addition, diet-induced obesity and insulin resistance are exacerbated in GFRAL-deficient mice, suggesting a homeostatic role for this receptor in metabolism. Finally, we demonstrate that GDF15-induced cell signaling requires the interaction of GFRAL with the coreceptor RET. Our data identify GFRAL as a new regulator of body weight and as the bona fide receptor mediating the metabolic effects of GDF15, enabling a more comprehensive assessment of GDF15 as a potential pharmacotherapy for the treatment of obesity.
How does increased GDF15 affect body weight?