Xifeng Qiao
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Xifeng Qiao has a total of 5 co-authors. Here are the top co-authors by number of shared publications:
- Chao Wang
Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, China
1 shared publication - Jiazuan Ni
Shenzhen Key Laboratory of Marine Biotechnology and Ecology, Department of Marine Biology, Shenzhen University, Shenzhen 518060, China
1 shared publication - Jing Tian
Department of Marine Biology, Shenzhen Key Laboratory of Marine Biotechnology and Ecology, Shenzhen University, Shenzhen 518060, China
1 shared publication - Ping Chen
School of Biological and Chemical Engineering, Nanyang Institute of Technology, Nanyang, China, China
1 shared publication - Qiong Liu
Shenzhen Key Laboratory of Marine Biotechnology and Ecology, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, China
1 shared publication
Latest Publications
- Open Access
- 11 November 2013
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 14 (11) , 22233-22245
Galectin-1 Is an Interactive Protein of Selenoprotein M in the Brain
Selenium, an essential trace element for human health, mainly exerts its biological function through selenoproteins. Selenoprotein M (SelM) is one of the highly expressed selenoproteins in the brain, but its biological effect and molecular mechanism remain unclear. Thus, the interactive protein of SelM was investigated in this paper to guide further study. In order to avoid protein translational stop, the selenocysteine-encoding UGA inside the open reading frame of SelM was site-directly changed to the cysteine-encoding UGC to generate the SelM' mutant. Meanwhile, its N terminal transmembrane signal peptide was also cut off. This truncated SelM' was used to screen a human fetal brain cDNA library by the yeast two-hybrid system. A new interactive protein of SelM' was found to be galectin-1 (Gal-1). This protein-protein interaction was further verified by the results of fluorescence resonance energy transfer techniques, glutathione S-transferase pull-down and co-immunoprecipitation assays. As Gal-1 plays important roles in preventing neurodegeneration and promoting neuroprotection in the brain, the interaction between SelM' and Gal-1 displays a new direction for studying the biological function of SelM in the human brain.
- 11 November 2013
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 14 (11) , 22233-22245
Open AccessGalectin-1 Is an Interactive Protein of Selenoprotein M in the Brain
Selenium, an essential trace element for human health, mainly exerts its biological function through selenoproteins. Selenoprotein M (SelM) is one of the highly expressed selenoproteins in the brain, but its biological effect and molecular mechanism remain unclear. Thus, the interactive protein of SelM was investigated in this paper to guide further study. In order to avoid protein translational stop, the selenocysteine-encoding UGA inside the open reading frame of SelM was site-directly changed to the cysteine-encoding UGC to generate the SelM' mutant. Meanwhile, its N terminal transmembrane signal peptide was also cut off. This truncated SelM' was used to screen a human fetal brain cDNA library by the yeast two-hybrid system. A new interactive protein of SelM' was found to be galectin-1 (Gal-1). This protein-protein interaction was further verified by the results of fluorescence resonance energy transfer techniques, glutathione S-transferase pull-down and co-immunoprecipitation assays. As Gal-1 plays important roles in preventing neurodegeneration and promoting neuroprotection in the brain, the interaction between SelM' and Gal-1 displays a new direction for studying the biological function of SelM in the human brain.