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Articles by QingHua Wang
Total Records ( 3 ) for QingHua Wang
  Hui Zhang , JiFeng Zhang , Ran Huang and QingHua Wang
  The existing Web services integration systems have three major disadvantages, in order to improve these disadvantages, this study propose extend the traditional contract net model so as to improve its disadvantage in allocating tasks. In the extended model, the tendering tactic is developed based on creditworthiness of task acquaintance and the bid awarded tactic is advanced based on the fuzzy comprehensive evaluation. Hence, it not only guarantees the quality of task fulfillment but also solves the problem of excessive communication in the traditional contract net model.
  Caiyun Fan , Jianbo Cheng , Jinlian Li , Qinghua Wang and Dugarjaviin Manglai
  In this study, partial sequence of horse DRD4 gene was cloned including intron 1, partial exon 1 and exon 2. And restriction endonuclease Stu I was used to analyze the polymorphism of the DRD4 gene sequences of 270 horses from six types including importing breed, cultivating breed and local breed. The products of endonuclease cutting were detected by 8% non-denatured polyacrylamide gel electrophoresis and showing in silver staining protocol.The result indicated restriction endonuclease Stu I showed polymorphism. Six kinds of genotypes were found in six populations which were controlled by three alleles. The results of Chi-square (χ2) test showed that genotypes of horse DRD4 gene in TB, SH, XN did not fit with Hardy-Weinberg equilibrium (p<0.05) but in WS, BH and WZ fit with Hardy-Weinberg equilibrium (p>0.05).
  Qinghua Wang , Feng Cheng , Mingyang Lu , Xia Tian and Jianpeng Ma
  Here we report the crystal structure of hemagglutinin (HA) from influenza B/Hong Kong/8/73 (B/HK) virus determined to 2.8 Å. At a sequence identity of ∼25% to influenza A virus HAs, B/HK HA shares a similar overall structure and domain organization. More than two dozen amino acid substitutions on influenza B virus HAs have been identified to cause antigenicity alteration in site-specific mutants, monoclonal antibody escape mutants, or field isolates. Mapping these substitutions on the structure of B/HK HA reveals four major epitopes, the 120 loop, the 150 loop, the 160 loop, and the 190 helix, that are located close in space to form a large, continuous antigenic site. Moreover, a systematic comparison of known HA structures across the entire influenza virus family reveals evolutionarily conserved ionizable residues at all regions along the chain and subunit interfaces. These ionizable residues are likely the structural basis for the pH dependence and sensitivity to ionic strength of influenza HA and hemagglutinin-esterase fusion proteins.
 
 
 
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