李明辉
博士 药学院高级副教授 Meng.Lee@xjtlu.edu.cn
西浦慧湖药学院副教授
发表文献
    Jiang, B.J., Xu, Y.W., Zhang, Y.H., Lee. M. (2019) “Translocating a High-Affinity Designer TIMP-1 to the Cell Membrane for Total Renal Carcinoma Inhibition: Putting the Prion Protein to Good Use.” Mol Cell Biol. 27; 39 (18). pii: e00128-19. doi: 10.1128/MCB.00128-19.
    Jiang, B.J., Liu, J., Lee, M. (2019). Targeting a Designer TIMP-1 to the Cell Surface for Effective MT1-MMP Inhibition: A Potential Role for the Prion Protein in Renal Carcinoma Therapy. Molecules 11;24(2). pii: E255. doi: 10.3390/molecules24020255.
    Jiang, B.J., Zhang, Y., Liu, J., Tsigkou, A., Rapti, M., Lee, M. (2017). Ensnaring membrane type 1-matrix metalloproteinase (MT1-MMP) with tissue inhibitor of metalloproteinase (TIMP)-2 using the haemopexin domain of the protease as a carrier: a targeted approach in cancer inhibition. Oncotarget (8(14):22685-22699. doi: 10.18632/oncotarget.15165).
    Guo, C., Tsigkou, A., Lee, M. (2016). ADAMTS13 and 15 are not regulated by the full length and N-terminal domain forms of TIMP-1, -2, -3 and -4. Biomed Rep. (4), 73-78.
    Duan, J.X., Rapti, M., Tsigkou, A., Lee, M. (2015) Expanding the Activity of Tissue Inhibitors of Metalloproteinase (TIMP)-1 against Surface-Anchored Metalloproteinases by the Replacement of Its C-Terminal Domain: Implications for Anti-Cancer Effects. PLoS One. (10), e0136384.
    Tsigkou, A., Reis, F.M., Ciarmela, P., Lee, M., Jiang, B., Tosti, C., Shen, F.R., Shi, Z., Chen, Y.G., F. Petraglia (2015). Expression Levels of Myostatin and Matrix Metalloproteinase 14 mRNAs in Uterine Leiomyoma are Correlated with Dysmenorrhea. Reprod Sci. (22),1597-1602.
    Tsigkou, A., Reis, F.M., Lee, M., Jiang, B., Tosti, C., Centini, G., Shen, F.R., Chen, Y.G., F. Petraglia (2015). Increased progesterone receptor expression in uterine leiomyoma: correlation with age, number of leiomyomas, and clinical symptoms. Fertil Steril. (104),170-175.
    Troeberg,, L., Mulloy, B., Ghosh, P., Lee, M., Murphy, G., H. Nagase (2012). Pentosan polysulfate increases affinity between ADAMTS-5 and TIMP-3 through formation of an electrostatically driven trimolecular complex. Biochem. (443), 307-315.
    Lee, M., Atkinson, S., Handsley, M., Curry, V., Edwards, D.R., G. Murphy (2010). Mutations of the MMP binding ridge render N-TIMP-1 an effective inhibitor of cell membrane associated MT1 MMP. Cancer Lett. (290), 114-122.
    Kveiborg, M., Jacobsen, J., Lee, M., Nagase, H., Wewer, U.M., G. Murphy (2010). Selective inhibition of ADAM12 catalytic activity through engineering of tissue inhibitor of metalloproteinase 2 (TIMP-2). Biochem (430), 79-86.
    Rapti, M., Atkinson, S., Lee, M., Trim, A., Moss, M., G. Murphy (2008). The isolated N- terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition. Biochem (411), 433-439.
    Grossman, M., Tworowski, D., Dym, O., Lee, M., Levy, Y., G. Murphy, I. Sagi (2010). The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function. Biochem. (49), 6184-6192.
    Lee, M., Atkinson, S., G. Murphy (2007). Identification of the Extracellular Matrix (ECM)- binding motifs of Tissue Inhibitor of Metalloproteinase (TIMP)-3 and effective transfer to TIMP-1. J. Biol. Chem (282), 6887-6898.
    Lee, M., Rapti, M., G. Murphy (2005). Total conversion of Tissue Inhibitor of Metalloproteinase (TIMP) for specific metalloproteinase targeting: fine-tuning TIMP-4 for optimal inhibition of tumor necrosis factor. J. Biol.Chem (280), 15967-15975.
    Murphy, G. M. Lee (2005). What are the roles of metalloproteinases in cartilage and bone damage. Ann Rheum Dis (64), 4-47.
    Lee, M., Rapti, M., G. Murphy (2004). Delineating the molecular basis of the inactivity of Tissue Inhibitor of Metalloproteinase-2 against Tumor Necrosis Factor-alpha converting enzyme. J. Biol. Chem. (279), 45121-45129.
    Lee, M., G. Murphy (2004). Matrix metalloproteinases at a glance. J. Cell Sci. (117), 4015-4016.
    Worley, J.R., Thompkins, P.B., Lee, M., Hutton, M., Soloway, P., Edwards, D.R., Murphy, G., V. Knäuper (2004). Sequence motifs of TIMP-2 determining proMMP-2 binding and activation by MT1-MMP. Biochem. J. (372), 799-809.
    Lee, M., Rapti, M., Knaüper, V., G. Murphy (2004). Threonine 98, the pivotal residue of tissue inhibitor of metalloproteinases (TIMP)-1 in metalloproteinase recognition. J. Biol. Chem. (279), 17562 – 17569
    Lee, M., Dodds, P., Verma, V., Maskos, K., Knäuper, V., G. Murphy (2003). Tailoring tissue inhibitor of metalloproteinases-3 to overcome the weakening effects of the cysteine-rich domains of tumour necrosis factor-alpha converting enzyme. Biochem. J. (371), 369-376.
    Lee, M., Rapti, M., G. Murphy (2003). Unveiling the surface epitopes that render tissue inhibitor of metalloproteinase-1 inactive against membrane type 1-matrix metalloproteinase. J. Biol. Chem. (278), 40224-40230.
    Lee, M., Verma, V., Maskos, K., Nath, D., Knäuper, V., Dodds, P., G. Murphy (2002). Engineering N-terminal domain of Tissue Inhibitor of Metalloproteinase (TIMP)-3 to be a better inhibitor against Tumour Necrosis Factor-aNConcerting Enzyme (TACE). Biochem. J. (364), 227-234.
    Lee, M., Maskos, K., Knäuper, V., G. Murphy (2002). Mapping and characterization of the functional epitopes of Tissue Inhibitor of Metalloproteinases (TIMP)-3 using TIMP-1 as the scaffold: A new frontier in TIMP engineering. Protein Sci. (11), 2493-250311.
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研究领域
① 抗肿瘤药物研究：“TIMPs”对肿瘤转移的抑制作用、CAR-T治疗
② 通过mRNA/LNP/双抗技术挖掘更多“TIMPs”的医疗潜能：如关节炎、骨质疏松及骨坏死方面。
应用场景
工作经历
2011 年 8 月起至今，西交利物浦大学高级副教授。
2010 - 2011 年，研究科学家，Domainex Ltd，剑桥科学园，英国。
2000 - 2010，英国剑桥大学高级研究员
教育背景
1998，PhD,牛津大学,瓦德汉学院
科研项目
产学研合作
专利项目

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