Image dehazing is a fundamental task for the computer vision and multimedia and usually in the face of the challenge from two aspects, i) the uneven distribution of arbitrary haze and ii) the distortion of image pixels caused by the hazed image. In this paper, we propose an end-to-end trainable framework, named Weighted-Fusion Network with Poly-Scale Convolution (WFN-PSC), to address these dehazing issues. The proposed method is designed based on the Poly-Scale Convolution (PSConv). It can extract the image feature from different scales without upsampling and downsampled, which avoids the image distortion. Beyond this, we design the spatial and channel weighted-fusion modules to make the WFN-PSC model focus on the hard dehazing parts of image from two dimensions. Specifically, we design three Part Architectures followed by the channel weighted-fusion module. Each Part Architecture consists of three PSConv residual blocks and a spatial weighted-fusion module. The experiments on the benchmark demonstrate the dehazing effectiveness of the proposed method. Furthermore, considering that image dehazing is a low-level task in the computer vision, we evaluate the dehazed image on the object detection task and the results show that the proposed method can be a good pre-processing to assist the high-level computer vision task.

Motivation: Protein-DNA interactions are essential for regulating many cellular processes, such as transcription, replication, recombination and translation. Amino acid mutations occurring in DNA-binding proteins have profound effects on protein-DNA binding and are linked with many diseases. Hence, accurate and fast predictions of the effects of mutations on protein-DNA binding affinity are essential for understanding disease-causing mechanisms and guiding plausible treatments. Results: Here we report a new method Single Amino acid Mutation binding free energy change of Protein-DNA Interaction (SAMPDI). The method utilizes modified Molecular Mechanics Poisson-Boltzmann Surface Area (MM/PBSA) approach along with an additional set of knowledge-based terms delivered from investigations of the physicochemical properties of protein-DNA complexes. The method is benchmarked against experimentally determined binding free energy changes caused by 105 mutations in 13 proteins (compiled ProNIT database and data from recent references), and results in correlation coefficient of 0.72. Availability and implementation: http://compbio.clemson.edu/SAMPDI. Contact: [email protected]. Supplementary information: Supplementary data are available at Bioinformatics online.

SUMMARY: Electrostatic force is an essential component of the total force acting between atoms and macromolecules. Therefore, accurate calculations of electrostatic forces are crucial for revealing the mechanisms of many biological processes. We developed a DelPhiForce web server to calculate and visualize the electrostatic forces at molecular level. DelPhiForce web server enables modeling of electrostatic forces on individual atoms, residues, domains and molecules, and generates an output that can be visualized by VMD software. Here we demonstrate the usage of the server for various biological problems including protein-cofactor, domain-domain, protein-protein, protein-DNA and protein-RNA interactions. AVAILABILITY AND IMPLEMENTATION: The DelPhiForce web server is available at: http://compbio.clemson.edu/delphi-force. CONTACT: [email protected]. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.