Xi'an Jiaotong-Liverpool University

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ACADEMIC BACKGROUND

D.Phil. University of Oxford / Wadham College, 1998 (Supervisor: Prof J E Baldwin, FRS)
B.Sc. University of Science Malaysia, Pharmacy, 1994 (1st class)

Qualifications
- D.Phil. University of Oxford / Wadham College, 1998 (Supervisor: Prof J E Baldwin, FRS)
Experience
- Associate Professor, Biological Sciences, Xi’an Jiaotong Liverpool Univ. (Honorary Lecturer, University of Liverpool). (since Aug 2011)
- Research Scientist, Domainex Ltd, Cambridge Science Park, UK (2010 - 2011).
- Senior Research Associate, Cambridge University, UK (2000 - 2010)
Articles
- 1. 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- 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.
- Lee, M., Verma, V., Maskos, K., Becherer, J.D., Knäuper, V., Dodds, P., G. Murphy (2002). The C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3. FEBS Lett. (520), 102-106.
- Lee, M., Knäuper, V., Becherer, J.D., G. Murphy (2001). Full-length and N-TIMP-3 display equal inhibitory activities towards TNF-αconvertase. Biochem. Biophys. Res. Comm. (280), 945-950.
- Crouch, N.P., Baldwin, J.E., Lee, M., MacKinnon, C.H., & Z.H. Zhang (1996). Initial Studies on the Substrate Specificity of the Soluble Recombinant 4-Hydroxyphenylpyruvate Dioxygenase From Rat Liver. Bio. Med. Chem. Lett. (6), 1503-1506.
- Crouch, N.P., Adlington, R.M., Baldwin, J.E., Lee, M., C.H. MacKinnon (1997). A Mechanistic Rationalisation for the Substrate Specificity of Recombinant Mammalian 4-Hydroxyphenylpyruvate Dioxygenase (4-HPPD). Tetrahedron (53), 6993-7010.
- Adlington, R.M., Baldwin, J.E., Crouch, N.P., Lee, M., C.H. MacKinnon (1996). Identification and Stereochemistry of the Product of 4HPPD Catalysed Oxidation of the Ketoacid of Methionine. Bio. Med. Chem. Lett. (6), 2003-2006.
- Adlington, R.M., Baldwin, J.E., Crouch, N.P, Lee, M, MacKinnon, C.H., D.R. Paul (1996). Stereochemistry of Hydroxylation during the Conversion of alpha-Ketoisocaproate to Hydroxyisovalerate by 4-Hydroxyphenylpyruvate Dioxygenase. Bio. Med. Chem. Lett. (6), 2721-2724.
- Lee, M., Zhang, Z.H., MacKinnon, C.H., Baldwin, J.E., N.P. Crouch (1996). The C-Terminal of Rat 4-Hydroxyphenylpyruvate Dioxygenase is Indispensable for Enzyme Activity. FEBS Lett. (393), 269-272.
- Baldwin, J.E., Crouch, N.P., Fujishima, Y., Lee, M., Mackinnon, C.H., Pitt, J., A.C. Willis (1995). 4-Hydroxyphenylpyruvate Dioxygenase Appears to Display Some Properties of alpha-Ketoisocaproate Dioxygenase in Rat Liver. Bio. Med. Chem. Lett. (5), 1255-1260.
Books, monographs, compilations and manuals
- Crouch, N.P., Lee, M., Iturriagagoitia-Bueno, T., C.H. MacKinnon (2000). “Cloning, Expression, and Purification of Mammalian 4-Hydroxyphenylpyruvate Dioxygenase/α-Ketoisocaproate Dioxygenase” Methods in Enzymol. (324), 342-354.
- Murphy, G., Knäuper, V., Lee. M., Amour, A., Worley, J.R., Hutton, M., Atkinson, S., Rapti, M., R. Williamson (2003). “Role of TIMPs (tissue inhibitors of metalloproteinases) in pericellular proteolysis: the specificity is in the detail” Biochem. Soc. Symp. Portland Press Chapter 6: (70), 65-80.

电话
+86 (0)51288161652
电子邮件
Meng.Lee@xjtlu.edu.cn
地址
P239(SIP Campus-Public Building)
Suzhou Dushu Lake Science and Education Innovation District
Suzhou Industrial Park
Suzhou
P.R.China
215123

Meng Huee LeeD.Phil

Profile

Qualifications

Experience

Articles

Books, monographs, compilations and manuals