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Articles by Ping Zhu
Total Records ( 2 ) for Ping Zhu
  Mei-Ling Liu , Wen Gu , Zhen-Ping Ma , Ping Zhu , Yue-Qiang Gao and Xin Liu
  Two new dinuclear copper(II) complexes, [Cu2(bpca)2(WO4) (H2O)2] · H2O (1) and [Cu2(bpca)2(MoO4) (H2O)2] · H2O (2) [bpca = bis(2-pyridylcarbonyl)amide anion], have been synthesized and their magnetic behavior investigated as a function of temperature. The structures of 1 and 2 have been determined by single-crystal X-ray diffraction. Complexes 1 and 2 are both 3D supramolecules with intermolecular hydrogen-bonding and p-p stacking interactions. The magnetic susceptibilities measured over the range 2-300 K show ferromagnetic interaction between the two copper(II) ions in 1, while there is antiferromagnetic interaction between the two copper(II) ions in 2. Based on the Hamiltonian written as Ĥ = -2JS1 .S2, best fitting for the experimental data leads to J = 0.557 cm-1 (1) and -77.2 cm-1 (2).
  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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