(S)-2-(Pyrrolidinium-2-ylmethyl­sulfan­yl)pyridinium dibromide

In the title compound, C10H16N2S2+·2Br−, the pyrrolidine ring displays an envelope conformation, with the flap C atom lying 0.484 (5) Å out of the plane of the rest of the pyrrolidine ring. The thio­ether group connects the pyridine ring and the 2-methyl­pyrrolidine group. Both pyrrolidine NH bonds form hydrogen bonds to the bromide anions. These hydrogen bonds link the cations and anions in a helical chain along the c axis

(S)-1-(2-Ammonio-3-methyl­butyl)-1,2-dihydro­pyridin-2-iminium dibromide

In the title compound, C10H19N3 2+·2Br−, the plane of the three butyl C atoms nearest to the pyridine ring is almost perpendicular to the ring [dihedral angle = 84.80 (2)°]. The N atom of the ammonium group is displaced by 1.150 (8) Å from the plane of these three C atoms. The iminium N atom lies on the opposite side of this plane. The crystal structure is stabilized by hydrogen bonds between the N and Br atoms, as well as by inter­molecular C—H⋯Br inter­actions

Learning Robust Medical Image Segmentation from Multi-source Annotations

Collecting annotations from multiple independent sources could mitigate the impact of potential noises and biases from a single source, which is a common practice in medical image segmentation. Learning segmentation networks from multi-source annotations remains a challenge due to the uncertainties brought by the variance of annotations and the quality of images. In this paper, we propose an Uncertainty-guided Multi-source Annotation Network (UMA-Net), which guides the training process by uncertainty estimation at both the pixel and the image levels. First, we developed the annotation uncertainty estimation module (AUEM) to learn the pixel-wise uncertainty of each annotation, which then guided the network to learn from reliable pixels by weighted segmentation loss. Second, a quality assessment module (QAM) was proposed to assess the image-level quality of the input samples based on the former assessed annotation uncertainties. Importantly, we introduced an auxiliary predictor to learn from the low-quality samples instead of discarding them, which ensured the preservation of their representation knowledge in the backbone without directly accumulating errors within the primary predictor. Extensive experiments demonstrated the effectiveness and feasibility of our proposed UMA-Net on various datasets, including 2D chest X-ray segmentation, fundus image segmentation, and 3D breast DCE-MRI segmentation

1-[3,5-Bis(trifluoro­meth­yl)phen­yl]-3-(2-pyrid­yl)thio­urea

The title compound, C14H9F6N3S, exhibits a nearly planar conformation in the solid state, with a dihedral angle between the planes of the benzene and pyridine rings of 14.86 (3)°. The pyridine N atom allows for the formation of a six-membered N—H⋯Npy hydrogen-bonded ring, thus forcing the two amide H atoms of the thio­urea group to point in opposite directions. The second N—H group forms an inter­molecular N—H⋯S hydrogen bond with the S atom of an adjacent mol­ecule. The F atoms of the two trifluoro­methyl groups display rotational disorder around the C—CF3 axis, with an occupancy ratio of 0.54 (1):0.46 (1)

(1S,4S,5S,6R)-6-(4-Bromo­phen­yl)-5-nitro­bicyclo­[2.2.2]octan-2-one

The title compound, C14H14BrNO3, contains a bicyclic ring system with four chiral centers. The absolute structure was established by the Flack method

Sodium 5-amino-1,3,4-thia­diazole-2-thiol­ate dihydrate

There are two 5-amino-1,3,4-thia­diazole-2(3H)-thiolate anions in the asymmetric unit of the title compound, Na+·C2H2N3S2 −·2H2O, which are almost perpendicular to each other [dihedral angle = 84.64 (6)°]. The two Na+ cations are in distorted fourfold coordinations by O atoms of the water molecules. The crystal structure is stabilized by N—H⋯S, O—H⋯N and O—H⋯S hydrogen bonds

Mitochondria-Localized Glutamic Acid-Rich Protein (MGARP) Gene Transcription Is Regulated by Sp1

Background: Mitochondria-localized glutamic acid-rich protein (MGARP) is a novel mitochondrial transmembrane protein expressed mainly in steroidogenic tissues and in the visual system. Previous studies showed that MGARP functions in hormone biosynthesis and its expression is modulated by the HPG axis. Methodology/principal findings: By bioinformatics, we identified two characteristic GC-rich motifs that are located proximal to the transcription start site (TSS) of MGARP, and each contains two Specificity protein 1 (Sp1) binding elements. We then determined that the −3 kb proximal MGARP promoter is activated in a Sp1-dependent manner using reporter assays and knockdown of Sp1 led to decreased expression of endogenous MGARP messages. We also demonstrated that one of the two GC-rich motifs, GC-Box1, harbors prominent promoter activity mediated by Sp1, and that it requires both GC boxes for full transcriptional activation. These findings suggest a dominant role for these GC boxes and Sp1 in activating the MGARP promoter through a synergistic mechanism. Consistently, the results of an Electrophoretic Mobility Gel Shift Assay (EMSA) and Chromatin Immunoprecipitation (ChIP) confirmed that Sp1 specifically interacts with the GC-rich region. We further found that estrogen receptor α (ERα), a known Sp1 co-activator, could potentiate GC-boxes containing MGARP promoter activity and this effect is mediated by Sp1. Knockdown of Sp1 significantly diminished the MGARP promoter transactivation and the expression of endogenous MGARP mediated by both Sp1 and ERα. Conclusions/significance: The present study identified a proximal core sequence in the MGARP promoter that is composed of two enriched Sp1 binding motifs and established Sp1 as one major MGARP transactivator whose functions are synergistic with ERα, providing a novel understanding of the mechanisms of MGARP gene transcriptional regulation

(S)-2-Amino-1-(pyrrolidinium-2-ylmeth­yl)pyridinium dibromide

In the title compound, C10H17N3 2+·2Br−, the pyrrolidinium ring displays an envelope conformation, with the flap N atom lying 0.564 (6) Å from the mean plane of the remaining four C atoms. The attached methyl­ene C atom, which connects the pyrrolidinium ring and the 2-amino­pyridine group, is displaced from the plane of the four pyrrolidinium C atoms by 0.811 (8) Å in the same direction as the pyrrolidinium N atom. The amine N lies on the opposite side of this plane