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Articles by Bin Xia
Total Records ( 2 ) for Bin Xia
  Bin Xia , Xingming Sun , Lingyun Xiang , Haijun Luo and Hengfu Yang
  This study presented a method to detect Least Significant Bit (LSB) matching steganography in gray images based on the neighborhood node degree characteristic. Natural images have a strong correlation between adjacent pixels and it’s disturbed by LSB matching. Accordingly the effects of LSB matching steganography on neighborhood node degree were examined at first. Then features were extracted from neighborhood node degree histogram. A new calibration algorithm based on neighborhood node degree was proposed to get more effective features. Support Vector Machine (SVM) was used as classifier. Experimental results demonstrated that the proposed method was efficient to detect the LSB matching steganography and had superior results compared with other recently proposed algorithms on compressed images and low embedding rate uncompressed images.
  Nan Zhong , Shengnan Zhang , Peng Zou , Jiaxuan Chen , Xue Kang , Zhe Li , Chao Liang , Changwen Jin and Bin Xia
  The main protease (Mpro) of severe acute respiratory syndrome coronavirus (SARS-CoV) plays an essential role in the extensive proteolytic processing of the viral polyproteins (pp1a and pp1ab), and it is an important target for anti-SARS drug development. It was found that SARS-CoV Mpro exists in solution as an equilibrium of both monomeric and dimeric forms, and the dimeric form is the enzymatically active form. However, the mechanism of SARS-CoV Mpro dimerization, especially the roles of its N-terminal seven residues (N-finger) and its unique C-terminal domain in the dimerization, remain unclear. Here we report that the SARS-CoV Mpro C-terminal domain alone (residues 187 to 306; Mpro-C) is produced in Escherichia coli in both monomeric and dimeric forms, and no exchange could be observed between them at room temperature. The Mpro-C dimer has a novel dimerization interface. Meanwhile, the N-finger deletion mutant of SARS-CoV Mpro also exists as both a stable monomer and a stable dimer, and the dimer is formed through the same C-terminal-domain interaction as that in the Mpro-C dimer. However, no C-terminal domain-mediated dimerization form can be detected for wild-type SARS-CoV Mpro. Our study results help to clarify previously published controversial claims about the role of the N-finger in SARS-CoV Mpro dimerization. Apparently, without the N-finger, SARS-CoV Mpro can no longer retain the active dimer structure; instead, it can form a new type of dimer which is inactive. Therefore, the N-finger of SARS-CoV Mpro is not only critical for its dimerization but also essential for the enzyme to form the enzymatically active dimer.
 
 
 
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