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Articles by Jian-Ping Ding
Total Records ( 2 ) for Jian-Ping Ding
  Yinghui Ling , Lijuan Wang , Xiaodong Zhang , Lina Xu , Jian-Ping Ding , Yun-Hai Zhang , Zijun Zhang and Xiao-Rong Zhang
  This study is about the correlation between COX II gene genetic variation and adult buck sperm motility traits, to provide genetics reference for the goat breeding. In this study, 120 adult male goat semen samples were collected from four populations. COX II gene polymorphism information was rapid screened using DNA pool and sequencing method. Each individual polymorphism of these goats was detected by RFLP. Sequencing results of DNA pool showed a single nucleotide mutation in COX II gene (A→G). The mutation caused a change of Hind III restriction site. RFLP results showed that the mutation associated with goat sperm traits. The vitality of fresh sperm and frozen sperm from BB-type goats was significantly higher than AA-type. This study provided foundation for establishment relationship between COX II gene SNP and goat sperm motility traits. It could be considered as a reference marker-assisted selection for buck semen quality traits and goat breeding.
  Xiao-Ling Yu , Tiancen Hu , Jia-Mu Du , Jian-Ping Ding , Xiang-Min Yang , Jian Zhang , Bin Yang , Xu Shen , Zheng Zhang , Wei-De Zhong , Ning Wen , Hualiang Jiang , Ping Zhu and Zhi-Nan Chen
  CD147, a member of the immunoglobulin superfamily (IgSF), plays fundamental roles in intercellular interactions in numerous pathological and physiological processes. Importantly, our previous studies have demonstrated that HAb18G/CD147 is a novel hepatocellular carcinoma (HCC)-associated antigen, and HAb18G/CD147 stimulates adjacent fibroblasts and HCC cells to produce elevated levels of several matrix metalloproteinases, facilitating invasion and metastasis of HCC cells. In addition, HAb18G/CD147 has also been shown to be a novel universal cancer biomarker for diagnosis and prognostic assessment of a wide range of cancers. However, the structural basis underlying the multifunctional character of CD147 remains unresolved. We report here the crystal structure of the extracellular portion of HAb18G/CD147 at 2.8Å resolution. The structure comprises an N-terminal IgC2 domain and a C-terminal IgI domain, which are connected by a 5-residue flexible linker. This unique C2-I domain organization is distinct from those of other IgSF members. Four homophilic dimers exist in the crystal and adopt C2-C2 and C2-I dimerization rather than V-V dimerization commonly found in other IgSF members. This type of homophilic association thus presents a novel model for homophilic interaction between C2 domains of IgSF members. Moreover, the crystal structure of HAb18G/CD147 provides a good structural explanation for the established multifunction of CD147 mediated by homo/hetero-oligomerizations and should represent a general architecture of other CD147 family members.
 
 
 
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