Yan Feng

Tongji University, Shanghai, Shanghai Shi, China

Are you Yan Feng?

Claim your profile

Publications (3)3.72 Total impact

  • [Show abstract] [Hide abstract]
    ABSTRACT: In the present study, a yeast two-hybrid screening system was used to identify the interaction partners of cardiac troponin I-interacting kinase (TNNI3K) that might serve as regulators or targets, and thus in turn to gain some insights on the roles of TNNI3K. After screening the adult heart cDNA library with a bait construct encoding the ANK motif of TNNI3K, antioxidant protein 1 (AOP-1) was isolated. The interaction between TNNI3K and AOP-1 was confirmed by the in vitro binding assay and coexpression experiments in vivo. The colocalization of TNNI3K and AOP-1 was clarified by confocal immunofluorescence. Moreover, coexpression of AOP-1 inhibited TNNI3K kinase activity in the in vitro kinase assay.
    No preview · Article · Dec 2007 · Biochemistry (Moscow)
  • [Show abstract] [Hide abstract]
    ABSTRACT: The interaction of nelin, a cardiac-specific expressed protein of human novel genenelin, with F-actin was studied by both F-actin cosedimentationin vitro and colocalization assays. The results showed that nelin is a new F-actin binding protein and is colocolized with F-actin in cytoplasm of cells. Three new nelin binding proteins, filamin C subtype, titin N2B subtype and inter-alpha trypsin inhibitor heavy chain precursor (ITIH), were identified from human heart cDNA library using yeast two-hybrid screening. The binding activity of filamin C with nelin was confirmed by coimmunoprecipitation. Filamin C binds to nelin through its C-terminal region. It is indicated that nelin is a cytoskeleton associated protein and acts as a membrane-cytoskeleton associated protein involved in the formation of focal adhesions. KeywordsNelin-F-actin-yeast two-hybrid-coimmunoprecipitation-cytoskeleton
    No preview · Article · Dec 2004 · Chinese Science Bulletin
  • [Show abstract] [Hide abstract]
    ABSTRACT: To construct the eukaryotic expression plasmid of human PRX3 and measure its expression in the HEK-293FT cells, the full-length coding region of human PRX3 was cloned by PCR and inserted into the eukaryotic expression vector pcDNA4-Xpress (A). HEK-293FT cells were transiently transfected with the recombinant plasmid. Western blot and immuofluorescence were used to detect the expression of the fusion protein. In the experiment, restriction analysis identified the construction of the recombinant plasmid and the inserted sequence was identical with that published on GenBank. Western blot and immunofluorescence confirmed the expression of the recombinant protein in transfected HEK-293FT cells. It was concluded that the eukaryotic expression plasmid of human PRX3 was constructed successfully and the recombinant could be expressed efficiently in HEK-293FT cells, which provides a sound basis for the further study on human PRX3.
    No preview · Article · Feb 2004 · Journal of Huazhong University of Science and Technology

Publication Stats

13 Citations
3.72 Total Impact Points


  • 2004-2007
    • Tongji University
      Shanghai, Shanghai Shi, China
    • Huazhong University of Science and Technology
      Wu-han-shih, Hubei, China