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山东农业大学生命科学学院研究生导师简介-王晓云

山东农业大学 免费考研网/2016-03-15




  
 

姓名王晓云学历博士职称教授
所属部门生物化学与分子生物学系
招生专业生物化学与分子生物学(博士、硕士)
联系方式电话:**-8430 E-mail:xyunwang@sdau.edu.cn

 
  
::教师简介::
王晓云,女,博士,1962年6月出生。1983年山东农业大学本科毕业,1985以来任教至今,先后获得山东农业大学硕士和博士学位。2002-2003在清华大学做访问学者,2008-2010年两度到哈佛大学做访问学者,2011年获高等学校教学名师称号,曾获得山东省首届教学名师和山东农业大学学生心目中十大优秀教师称号。一直以来从事生物化学与分子生物学、植物生理生化方面的科研与教学工作,着重研究酶的催化机制以及结构与功能的关系。主持承担国家自然基金、高等学校博士学科点专项科研基金、山东省优秀中青年科学家科研奖励基金、作物生物学国家重点实验室基金等课题。作为第一作者或通讯作者在“Antioxidant and Redox Signalling”、“International Journal of Biochemistry and Cell Biology” 、“International Journal of Biological Macromolecules”、“中国农业科学”等国内外学术刊物发表学术论文60多篇。

  
::教学工作::
承担本科生《生物化学》、《分子生物学》、《基础生物化学实验》;硕士研究生《生物化学》;博士研究生《蛋白质结构与功能》等课程的教学工作,主持的生物化学课程为教育部双语建设课程、山东省首届精品课程和山东省重点建设课程,所在的教学团队为生物化学与分子生物学系列课程国家级教学团队。

  
::研究方向::
主要研究方向为蛋白质(酶)的结构与功能的关系,在克隆、表达基因的基础上,利用定点突变技术,研究关键氨基酸残基对蛋白质结构及功能的影响等,特别是逆境胁迫下蛋白质表达与氧化胁迫的关系,以及二硫键形成途径中关键酶的研究等,也包括酶的抑制动力学及生物体内代谢调控酶的分离纯化、性质研究及调控机理的研究。

  
::科研项目::
1. 农业部公益性行业科研专项“我国重要野生果树资源的收集、评价与优异种质创新利用技术研究与示范” (**).

2. 国家自然科学基金《利用定点突变技术研究二硫键对植酸酶结构、催化活性及热稳定性的作用》( No.**)

3. 国家自然科学基金《通过引入二硫键、增加糖基化位点等方式提高植酸热稳定性的研究》(No. **)

4. 高等学校博士点专项基金:《糖基化及二硫键对植酸酶稳定性的研究》(No. **)

5. 山东省中青年科学家科研奖励基金《叶片衰老关键酶分离纯化及调控衰老物质的研制与开发》

  
::学术论文::


1. Yang, X.J., H.R. Cui, Z.B. Yu, J.J. Du, J.N. Xu, and X.Y. Wang, Key Amino Acids of Arabidopsis VKOR in the Activity of

Phylloquinone Reduction and Disulfide Bond Formation. Protein Pept Lett, 2015. 22: p. 81-6.

2. Du, J.-J., C.-Y. Zhan, Y. Lu, H.-R. Cui, and X. Wang, The conservative cysteines in transmembrane domain of AtVKOR/LTO1 are

critical for photosynthetic growth and photosystem II activity in Arabidopsis. Frontiers in Plant Science, 2015. doi:

10.3389/fpls.2015.00238.

3. Cui, H.-R., Z.-R. Zhang, W. lv, J.-N. Xu, and X.-Y. Wang, Genome-wide characterization and analysis of F-box protein-encoding genes

in the Malus domestica genome. Molecular Genetics and Genomics, 2015: p. 1-12.

4. Wu, Q.Y., H.Y. Guo, H.L. Geng, B.M. Ru, J. Cao, C. Chen, L.Y. Zeng, X.Y. Wang, F. Li, and K.L. Xu, T273 plays an important role in

the activity and structural stability of arginine kinase. Int J Biol Macromol, 2014. 63: p. 21-8.

5. Wang, P., X.Z. Li, H.R. Cui, Y.G. Feng, and X.Y. Wang, Identification and functional analysis of a novel parvulin-type peptidyl-prolyl

isomerase from Gossypium hirsutum. Plant Physiol Biochem, 2014. 76C: p. 58-66.

6. Wan, C.M., X.J. Yang, J.J. Du, Y. Lu, Z.B. Yu, Y.G. Feng, and X.Y. Wang, Identification and characterization of SlVKOR, a disulfide

bond formation protein from Solanum lycopersicum, and bioinformatic analysis of plant VKORs. Biochemistry (Mosc), 2014. 79: p. 440-

9.

7. Lu, Y., J.J. Peng, Z.B. Yu, J.J. Du, J.N. Xu, and X.Y. Wang, Thylakoid membrane oxidoreductase LTO1/AtVKOR is involved in ABA-

mediated response to osmotic stress in Arabidopsis. Physiol Plant, 2014. doi: 10.1111/ppl.12268.

8. Geng, H.L., M.R. Bian, Y. Liu, J. Cao, C. Chen, Z.Y. Wang, Z.Y. Li, L.Y. Zeng, X.Y. Wang, Q.Y. Wu, and K.L. Xu, The D14 and

R138 ion pair is involved in dimeric arginine kinase activity, structural stability and folding. Int J Biol Macromol, 2014. 66: p. 302-10.

9. Du, F., J.-N. Xu, C.-Y. Zhan, Z.-B. Yu, and X.-Y. Wang, An obesity-like gene MdTLP7 from apple (Malus× domestica) enhances

abiotic stress tolerance. Biochemical and biophysical research communications, 2014. 445: p. 394-397.

10. Du, F., J.N. Xu, D. Li, and X.Y. Wang, The identification of novel and differentially expressed apple-tree genes under low-temperature

stress using high-throughput Illumina sequencing. Mol Biol Rep, 2014. doi: 10.1007/s11033-014-3802-5

11. Yu, Z.B., Y. Lu, J.J. Du, J.J. Peng, and X.Y. Wang, The chloroplast protein LTO1/AtVKOR is involved in the xanthophyll cycle and the

acceleration of D1 protein degradation. J Photochem Photobiol B, 2013. 130C: p. 68-75.

12. Lu, Y., H.R. Wang, H. Li, H.R. Cui, Y.G. Feng, and X.Y. Wang, A chloroplast membrane protein LTO1/AtVKOR involving in redox

regulation and ROS homeostasis. Plant Cell Rep, 2013. 32: p. 1427-40.

13. Wu, Q.Y., F. Li, X.Y. Wang, and K.L. Xu, Evidence that the amino acid residue Ile121 is involved in arginine kinase activity and structural

stability. Int J Biol Macromol, 2012. 51: p. 369-77.

14. Wu, Q.Y., F. Li, H.Y. Guo, J. Cao, C. Chen, W. Chen, K. Zhao, L.Y. Zeng, Z.X. Han, Z.Y. Li, X.Y. Wang, and K.L. Xu, Amino acid

residue E543 in JAK2 C618R is a potential therapeutic target for myeloproliferative disorders caused by JAK2 C618R mutation. Arch

Biochem Biophys, 2012. 528: p. 57-66.

15. Li, F., Wu, Q.Y., and Wang, X.Y. (2013). The amino acid residue L113 is involved in arginine kinase activity and structural stability. Int J

Biol Macromol. 52, 198-205

16. Wu, Q.Y., F. Li, X.Y. Wang, and Z.J. Chen, Impact of inter-subunit interactions on the dimeric arginine kinase activity and structural

stability. Arch Biochem Biophys, 2011. 512: p. 61-8.

17. Wu, Q.Y., K.Z. Jin, F. Li, Z.Q. Hu, and X.Y. Wang, Impact of intra-subunit interactions on the dimeric arginine kinase activity and

structural stability. Int J Biol Macromol, 2011. 49: p. 822-31.

18. Wang, X., R.J. Dutton, J. Beckwith, and D. Boyd, Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a

protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase. Antioxid Redox Signal, 2011. 14:

p. 1413-20.

19. Wang, H.R., W.J. Zhu, and X.Y. Wang, Mechanism of inhibition of arginine kinase by flavonoids consistent with thermodynamics of

docking simulation. Int J Biol Macromol, 2011. 49: p. 985-91.

20. Jing, X.L., M.N. Fan, G. Jia, L.W. Liu, L. Ma, C.C. Zheng, X.P. Zhu, H.M. Liu, and X.Y. Wang, A Multifunctional Protein Encoded by

Turkey Herpesvirus Suppresses RNA Silencing in Nicotiana benthamiana. J Virol, 2011. 85: p. 12792-803.

21. Feng, W.K., L. Wang, Y. Lu, and X.Y. Wang, A protein oxidase catalysing disulfide bond formation is localized to the chloroplast

thylakoids. FEBS J, 2011. 278: p. 3419-30.

22. Li, F., Wu, Q. Y., Sun, Y. L., Ma, N. N., Wang, X. Y., and Meng, Q. W. (2010) Evidence that the amino acid residue Cys117 of

chloroplastic monodehydroascorbate reductase is involved in its activity and structural stability,Int J Biol Macromol 46, 350-355.

23. Wu, X. Q., Zhu, W. J., Lu, Z. R., Xia, Y., Yang, J. M., and Wang, X. Y*. (2009) The effect of rutin on arginine kinase: inhibition kinetics and thermodynamics merging with docking simulation, Int J Biol Macromol 44, 149-155.

24. Wu, X. Q., Xu, H., Yue, H., Liu, K. Q., and Wang, X. Y*. (2009) Inhibition kinetics and the aggregation of alpha-glucosidase by different denaturants, Protein J 28, 448-456.

25. Wu, Q. Y., Li, F., and Wang, X. Y*. (2009) Val65 plays an important role in the substrate synergism, structural stability and activity of arginine kinase, Int J Biol Macromol 45, 393-398.

26. Shi, X. W., Sun, M. L., Zhou, B., and Wang, X. Y*. (2009) Identification, characterization, and overexpression of a phytase with potential industrial interest,Can J Microbiol 55, 599-604.

27. Zhou, J., Yang, Z., Yang, W., Wang, X., Jiang, S., and Zhang, G. (2008) Effects of a New Recombinant Phytase on the Performance and Mineral Utilization of Broilers Fed Phosphorus-Deficient Diets, The Journal of Applied Poultry Research 17, 331.

28. Wu, Q. Y., Li, F., and Wang, X. Y*. (2008) Evidence that amino-acid residues are responsible for substrate synergism of locust arginine kinase, Insect Biochem Mol Biol 38, 59-65.

29. Wu, Q. Y., Li, F., and Wang, X. Y*. (2008) Evidence that the amino acid residue P272 of arginine kinase is involved in its activity, structure and stability, Int J Biol Macromol 43, 367-372.

30. Zhu, W. J., Li, M., and Wang, X. Y*. (2007) Chemical modification studies on arginine kinase: essential cysteine and arginine residues at the active site, Int J Biol Macromol 41, 564-571.

31. Zhao, D. M., Wang, M., Mu, X. J., Sun, M. L., and Wang, X. Y*. (2007) Screening, cloning and overexpression of Aspergillus niger phytase (phyA) in Pichia pastoris with favourable characteristics, Lett Appl Microbiol 45, 522-528.

32. Xia, Y., Park, Y. D., Mu, H., Zhou, H. M., Wang, X. Y*., and Meng, F. G. (2007) The protective effects of osmolytes on arginine kinase unfolding and aggregation, Int J Biol Macromol 40, 437-443.

33. Wu, Q. Y., Li, F., Zhu, W. J., and Wang, X. Y*. (2007) Cloning, expression, purification, and characterization of arginine kinase from Locusta migratoria manilensis, Comp Biochem Physiol B Biochem Mol Biol 148, 355-362.

34. Wei, X., Wang, X*., Zhou, B., and Zhou, H. (2006) Effect of Urea on Activity and Conformation of a Glycoprotein, TSINGHUA SCIENCE AND TECHNOLOGY11, 400.

35. Wang, X. Y*., Sun, M. L., Zhao, D. M., and Wang, M. (2006) Kinetics of inactivation of phytase (phy A) during modification of histidine residue by IAA and DEP, Protein Pept Lett 13, 565-570.

36. Li, M., Wang, X. Y*., and Bai, J. G. (2006) Purification and characterization of arginine kinase from locust, Protein Pept Lett 13, 405-410.

37. Fei, M., Chen, J., and Wang, X*. (2006) Biochemical Properties and Inhibition Kinetics of Phosphatase from Wheat Thylakoid Membranes, Journal of Integrative Plant Biology 48, 294.

38. Wang, X., LIU, C., Zhang, J., and LUO, W. (2005) Inhibitory kinetics of quercetin on phenoloxidase from loopworm, Insect Science 12, 435-441.

39. Song, G. Y., Wang, X. Y*., and Wang, M. (2005) Influence of disulfide bonds on the conformational changes and activities of refolded phytase, Protein Pept Lett12, 533-535.

40. Wang, X. Y., Meng, F. G., and Zhou, H. M. (2004) Unfolding and inactivation during thermal denaturation of an enzyme that exhibits phytase and acid phosphatase activities, Int J Biochem Cell Biol 36, 447-459.

41. Wang, X. Y., Meng, F. G., and Zhou, H. M. (2004) The role of disulfide bonds in the conformational stability and catalytic activity of phytase, Biochem Cell Biol 82, 329-334.

42. Liu, Y., Wang, X*., and Liu, L. (2004) Analysis of genetic variation in surviving apple shoots following cryopreservation by vitrification, Plant science 166, 677-685.

43. Wang, X. Y., Meng, F. G., and Zhou, H. M. (2003) Inactivation and conformational changes of creatine kinase at low concentrations of hexafluoroisopropanol solutions, Biochem Cell Biol 81, 327-333.


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