AdaBin: Improving Binary Neural Networks with Adaptive Binary Sets

This paper studies the Binary Neural Networks (BNNs) in which weights and activations are both binarized into 1-bit values, thus greatly reducing the memory usage and computational complexity. Since the modern deep neural networks are of sophisticated design with complex architecture for the accuracy reason, the diversity on distributions of weights and activations is very high. Therefore, the conventional sign function cannot be well used for effectively binarizing full-precision values in BNNs. To this end, we present a simple yet effective approach called AdaBin to adaptively obtain the optimal binary sets $\{b_1, b_2\}$ ($b_1, b_2\in \mathbb{R}$) of weights and activations for each layer instead of a fixed set (\textit{i.e.}, $\{-1, +1\}$). In this way, the proposed method can better fit different distributions and increase the representation ability of binarized features. In practice, we use the center position and distance of 1-bit values to define a new binary quantization function. For the weights, we propose an equalization method to align the symmetrical center of binary distribution to real-valued distribution, and minimize the Kullback-Leibler divergence of them. Meanwhile, we introduce a gradient-based optimization method to get these two parameters for activations, which are jointly trained in an end-to-end manner. Experimental results on benchmark models and datasets demonstrate that the proposed AdaBin is able to achieve state-of-the-art performance. For instance, we obtain a 66.4% Top-1 accuracy on the ImageNet using ResNet-18 architecture, and a 69.4 mAP on PASCAL VOC using SSD300. The PyTorch code is available at \url{https://github.com/huawei-noah/Efficient-Computing/tree/master/BinaryNetworks/AdaBin} and the MindSpore code is available at \url{https://gitee.com/mindspore/models/tree/master/research/cv/AdaBin}.Comment: ECCV 202

Influence of terrestrial and marine air mass on the constituents and intermixing of bioaerosols over a coastal atmosphere

Coastal environments provide an ideal setting for investigating the intermixing processes between terrestrial and marine aerosols. In this study, fine particulate matter (PM2.5) samples categorized into terrestrial, marine, and mixed air masses were collected from a coastal location in northern China. The chemical and biological constituents, including water-soluble ions (WSIs), metallic elements, and bacterial and fungal aerosols, were investigated from January to March 2018, encompassing both the winter heating and spring dust seasons. Terrestrial air masses constituted 59.94 % of the total air masses throughout the sampling period, with a significant increase during severe haze pollution (up to 90 %). These air masses exhibited a higher concentration of PM2.5 (240 µg m−3) and carried more water-soluble ions and metal elements. The terrestrial air mass also contained a larger number of animal parasites or symbionts, as well as human pathogens from anthropogenic emissions, such as Staphylococcus, Deinococcus, Sphingomonas, Lactobacillus, Cladosporium, and Malassezia. Conversely, a significant quantity of saprophytic bacteria such as hydrocarbon-degrading and gut bacteria from the genera Comamonas, Streptococcus, Novosphingobium, and Aerococcus and the saprophytic fungus Aspergillus were the most abundant species in the marine air mass samples. The mixed air mass elucidates the intermixing process of terrestrial and marine sources, a result of microorganisms originating from both anthropogenic and terrestrial emissions, which includes pathogenic microorganisms from hospitals and sewage treatment plants, and a multitude of soil bacteria. A stronger correlation was noted between microorganisms and continental elements in both terrestrial and mixed air mass samples, specifically K+, Mg2+, and Ca2+ derived from soil dust. Marine air masses exhibited a significant correlation with sea salt ions, specifically Na+. In the mixed air mass sample, a fusion of marine and terrestrial microorganisms is characterized by alterations in the ratio of pathogenic to saprophytic microorganisms when compared to samples derived from either terrestrial or marine sources. This study on the constituents and amalgamation of bioaerosols over the coastal atmosphere encompassing distinct air masses is crucial to understand the transport, intermixing processes, and health implications of terrestrial and marine air masses.</p

Characterization of two functional NKX3.1 binding sites upstream of the PCAN1 gene that are involved in the positive regulation of PCAN1 gene transcription

<p>Abstract</p> <p>Background</p> <p><it>NKX3.1 </it>and <it>PCAN1 </it>are both prostate-specific genes related to prostate development and prostate cancer. So far, little is known about the regulatory mechanisms of the expression of these two genes. In the present study, we found that NKX3.1 upregulated <it>PCAN1 </it>gene transcription in LNCaP prostate cancer cells. To understand the regulatory mechanisms, our work focused on identifying the functional NKX3.1 binding sites upstream of the <it>PCAN1 </it>gene, which might be involved in the positive regulation of <it>PCAN1 </it>expression by NKX3.1.</p> <p>Results</p> <p>We cloned and characterized a 2.6 kb fragment upstream of the <it>PCAN1 </it>gene. Analysis of the 2.6 kb sequence with MatInspector 2.2 revealed five potential binding sites of NKX3.1 transcription factor. Luciferase reporter assays, electrophoretic mobility shift assays, chromatin immunoprecipitation and RNA interference were performed to study the effects of NKX3.1 on <it>PCAN1 </it>gene expression in prostate cancer cells. Our results showed that <it>PCAN1 </it>promoter activity and mRNA expression were increased by transfection with the <it>NKX3.1 </it>containing plasmid (pcDNA3.1-<it>NKX3.1</it>) and that <it>PCAN1 </it>mRNA expression was decreased by RNA interference targeting human <it>NKX3.1 </it>in LNCaP prostate cancer cells. The results of electrophoretic mobility shift assays and chromatin immunoprecipitation showed that NKX3.1 bound to NBS1 (-1848 to -1836) and NBS3 (-803 to -791) upstream of the <it>PCAN1 </it>gene. The luciferase reporter assays showed that NBS1 and NBS3 enhanced the promoter activity in pGL₃-promoter vector with cotransfection of the <it>NKX3.1 </it>containing plasmid. Furthermore, the deletion of NBS1 or both NBS1 and NBS3 reduced <it>PCAN1 </it>promoter activity and abolished the positive regulation of <it>PCAN1 </it>expression by NKX3.1.</p> <p>Conclusion</p> <p>Our results suggested that two functional NKX3.1 binding sites located at -1848 to -1836 and -803 to -791 upstream of the <it>PCAN1 </it>gene were involved in the positive regulation of <it>PCAN1 </it>gene transcription by NKX3.1.</p