Select, Purify, and Exchange: A Multisource Unsupervised Domain Adaptation Method for Building Extraction.

Accurately extracting buildings from aerial images has essential research significance for timely understanding human intervention on the land. The distribution discrepancies between diversified unlabeled remote sensing images (changes in imaging sensor, location, and environment) and labeled historical images significantly degrade the generalization performance of deep learning algorithms. Unsupervised domain adaptation (UDA) algorithms have recently been proposed to eliminate the distribution discrepancies without re-annotating training data for new domains. Nevertheless, due to the limited information provided by a single-source domain, single-source UDA (SSUDA) is not an optimal choice when multitemporal and multiregion remote sensing images are available. We propose a multisource UDA (MSUDA) framework SPENet for building extraction, aiming at selecting, purifying, and exchanging information from multisource domains to better adapt the model to the target domain. Specifically, the framework effectively utilizes richer knowledge by extracting target-relevant information from multiple-source domains, purifying target domain information with low-level features of buildings, and exchanging target domain information in an interactive learning manner. Extensive experiments and ablation studies constructed on 12 city datasets prove the effectiveness of our method against existing state-of-the-art methods, e.g., our method achieves 59.1% intersection over union (IoU) on Austin and Kitsap → Potsdam, which surpasses the target domain supervised method by 2.2% . The code is available at https://github.com/QZangXDU/SPENet.

KIAA1199 promotes sorafenib tolerance and the metastasis of hepatocellular carcinoma by activating the EGF/EGFR-dependent epithelial-mesenchymal transition program.

Patients with advanced hepatocellular carcinoma (HCC) will almost always develop acquired tolerance after sorafenib therapy, and the molecular mechanism of sorafenib tolerance remains poorly characterized. Here, using our established sorafenib-resistant HCC cell and xenograft models, we identified a novel gene, KIAA1199, which was markedly elevated among the differentially expressed genes involved in sorafenib tolerance. Moreover, elevated expression of KIAA1199 was positively correlated with a high risk of recurrence and metastasis and advanced TNM stage in HCC patients. Functionally, loss- and gain-of-function studies showed that KIAA1199 promoted the migration, invasion, and metastasis of sorafenib-resistant HCC cells. Mechanistically, KIAA1199 is required for EGF-induced epithelial-mesenchymal transition (EMT) in sorafenib-resistant HCC cells by aiding in EGFR phosphorylation. In summary, our data uncover KIAA1199 as a novel sorafenib-tolerant promoting gene that plays an indispensable role in maintaining sorafenib-resistant HCC cell metastasis.

[piRNA: a novel member of small RNA family].

It has been demonstrated that microRNA (miRNA) and small interfering RNA(siRNA) play an important role in the basically physiological regulation of eukaryotic organisms. With the intensive study on siRNA and miRNA, scientists recently have discovered that there exists a novel type of small RNA named as piRNA in the mammalian testes, which is essential for physiological modulation of spermiogenesis and different from miRNA or siRNA in functions, gene distributions and characteristics. It is well believed that the more intensive research on piRNA will throw light on the delicate mechanisms of gene expression modulation for eukaryotic species.

The different roles of metal ions and water molecules in the recognition and catalyzed hydrolysis of ATP by phenanthroline-containing polyamines.

The phenanthroline bridging polyaza ligands L1, L2 and L3 can selectively and strongly bind nucleotides at physiological pH, and hence accelerate the hydrolysis rate of the bound ATP. It is interesting that a phosphoramidate intermediate at 2.88 ppm (should be added 5.63 ppm when compared with other models) was found in the hydrolysis process of L/ATP. By introduction of metal ions (critical Zn(2+) or hard Mg(2+), Ca(2+)) to the L/ATP system, recognition of the anionic substrates by the protonated ligands was greatly promoted. However, due to the different affinities of metal ions to the receptor and the substrate, ATP hydrolysis in Zn(2+)/L/ATP system and Mg(2+)(Ca(2+))/L/ATP system occurs through different mechanisms. By comparison with the M/ATP (M=Zn(2+), Mg(2+), Ca(2+)) system, the rates of ATP-hydrolysis in the Mg(2+)Ca(2+)/L/ATP system and the Zn(2+)/L/ATP system were enhanced and retarded, respectively. Moreover, the reasons contributing to large rate range of the L/ATP systems and M(2+)/L/ATP systems were given. The results show that metal ions vertically regulate the recognition and hydrolysis of ATP. On the other hand, water molecule participates in the hydrolysis reactions at different steps with different functions in the L/ATP systems and M(Zn(2+), Mg(2+), Ca(2+))L/ATP systems.

Recognition promoted by Zn2+ between phenanthroline bridging polyaza ligands and nucleotides--Zn2+ acts as 'messenger' between the receptor and substrate.

The stability constants of the supramolecular complexes formed between L ((a,b,c,d)) or their Zn(2+) complexes, and adenosine 5'-triphosphate (ATP) in aqueous solution were determined by potentiometric titrations (25 degrees C, I = 0.1 mol dm(-3) KNO(3)). The results show that protonated aliphatic-substituted L (a,d) and aromatic-substituted L (b,c) ligands and/or Zn(II) ion can efficiently recognition the substrate, ATP. All of the equilibrium studies, (1)H and (31)P nuclear magnetic resonance spectra indicate that multiple interactions, including coordination, pi-stacking, ion-pairing, H-bonding, and possible ion-pi-donor, hydrophobic and even van der Waals interactions exist in the Zn(II)-L-ATP systems. On the other hand, the recognition of the substrates by the protonated ligands was significantly promoted by the addition of Zn(II), which leads to coordination competition between the mixed ligands, L and nucleotide. In Zn(II)/L/ATP systems the tendency for phosphate chain to receive proton and metal ion increases, facilitating the cleavage of the phosphate chain of the nucleotide.