SSAH: Semi-supervised Adversarial Deep Hashing with Self-paced Hard Sample Generation

Deep hashing methods have been proved to be effective and efficient for large-scale Web media search. The success of these data-driven methods largely depends on collecting sufficient labeled data, which is usually a crucial limitation in practical cases. The current solutions to this issue utilize Generative Adversarial Network (GAN) to augment data in semi-supervised learning. However, existing GAN-based methods treat image generations and hashing learning as two isolated processes, leading to generation ineffectiveness. Besides, most works fail to exploit the semantic information in unlabeled data. In this paper, we propose a novel Semi-supervised Self-pace Adversarial Hashing method, named SSAH to solve the above problems in a unified framework. The SSAH method consists of an adversarial network (A-Net) and a hashing network (H-Net). To improve the quality of generative images, first, the A-Net learns hard samples with multi-scale occlusions and multi-angle rotated deformations which compete against the learning of accurate hashing codes. Second, we design a novel self-paced hard generation policy to gradually increase the hashing difficulty of generated samples. To make use of the semantic information in unlabeled ones, we propose a semi-supervised consistent loss. The experimental results show that our method can significantly improve state-of-the-art models on both the widely-used hashing datasets and fine-grained datasets

A cytoplasmic Cu-Zn superoxide dismutase SOD1 contributes to hyphal growth and virulence of Fusarium graminearum

AbstractSuperoxide dismutases (SODs) are scavengers of superoxide radicals, one of the main reactive oxygen species (ROS) in the cell. SOD-based ROS scavenging system constitutes the frontline defense against intra- and extracellular ROS, but the roles of SODs in the important cereal pathogen Fusarium graminearum are not very clear. There are five SOD genes in F. graminearum genome, encoding cytoplasmic Cu-Zn SOD1 and MnSOD3, mitochondrial MnSOD2 and FeSOD4, and extracellular CuSOD5. Previous studies reported that the expression of SOD1 increased during infection of wheat coleoptiles and florets. In this work we showed that the recombinant SOD1 protein had the superoxide dismutase activity in vitro, and that the SOD1-mRFP fusion protein localized in the cytoplasm of F. graminearum. The Δsod1 mutants had slightly reduced hyphal growth and markedly increased sensitivity to the intracellular ROS generator menadione. The conidial germination under extracellular oxidative stress was significantly delayed in the mutants. Wheat floret infection assay showed that the Δsod1 mutants had a reduced pathogenicity. Furthermore, the Δsod1 mutants had a significant reduction in production of deoxynivalenol mycotoxin. Our results indicate that the cytoplasmic Cu-Zn SOD1 affects fungal growth probably depending on detoxification of intracellular superoxide radicals, and that SOD1-mediated deoxynivalenol production contributes to the virulence of F. graminearum in wheat head infection

5-Amino-7-(3-chloro­phen­yl)-3,7-di­hydro-2H-thieno[3,2-b]pyran-6-carbo­nitrile 1,1-dioxide

The title compound, C14H11ClN2O3S, with fused thiophene and pyran rings, was synthesized via the condensation of dihydro­thio­phen-3(2H)-one 1,1-dioxide and 2-(3-chloro­benz­yl­idene)malononitrile catalysed by triethyl­amine in ethanol. The thio­phene ring adopts an envelope conformation and the pyran ring is planar (r.m.s. deviation = 0.0067 Å). The dihedral angle between the pyran and phenyl rings is 80.8 (1)°. The crystal packing is stabilized by inter­molecular N—H⋯N and N—H⋯O hydrogen bonds in which the cyano N and sulphone O atoms, respectively, acting as acceptors

Ethyl 7-(4-bromo­phen­yl)-5-trifluoro­methyl-4,7-dihydro­tetra­zolo[1,5-a]pyrimidine-6-carboxyl­ate

In the title compound, C14H11BrF3N5O2, the pyrimidine ring adopts a flattened envelope conformation with sp 3-hybridized carbon as the flap [deviation = 0.177 (3) Å]. The dihedral angle between tetra­zole and bromo­phenyl rings is 84.3 (1)°. In the crystal, mol­ecules are linked into centrosymmetric dimers by pairs of N—H⋯N hydrogen bonds

5′-Amino-2-oxo-2′,3′-dihydro­spiro­[indoline-3,7′-thieno[3,2-b]pyran]-6′-carbonitrile 1′,1′-dioxide

In the title compound, C15H11N3O4S, the dihedral angle between the mean planes of the dihydro­indol-2-one (r.m.s. deviation = 0.015 Å) and dihydro­thieno[3,2-b]pyran (r.m.s. deviation = 0.011 Å) ring systems is 89.53 (3)°. The crytal packing is consolidated by inter­molecular N—H⋯O and N—H⋯N hydrogen bonds, which link the mol­ecules into a two-dimensional network into sheets lying parallel to (100)

5-Amino-7-(4-bromo­phen­yl)-3,7-di­hydro-2H-thieno[3,2-b]pyran-6-carbo­nitrile 1,1-dioxide

In the title compound, C14H11BrN2O3S, the 2,3-dihydro­thio­phene ring is almost planar [maximum deviation = 0.006 (1) Å]. The pyran ring is in an envelope conformation [puckering parameters Q = 0.115 (2) Å, θ = 77.5 (10), ϕ = 172.9 (10)°]. The pyran and phenyl rings are approximately perpendicular, making a dihedral angle of −76.4 (2)°. The crystal packing is stabilized by inter­molecular N—H⋯O hydrogen bonds, with the sulfone O atoms acting as acceptors