姓    名: 黄明东
性    别:

 

职    称: 教授
学    历: 博士研究生
职    务: 生物药光动力国家地方工程中心主任
电    话:
专    业: 化学生物学
电子邮件: HMD_lab@fzu.edu.cn
研究方向: 化学生物学、结构生物学、光动力学、凝血与纤溶

教育工作经历
教育经历(按时间倒排序):
1989/1 - 1993/3,美国俄勒冈州立大学,博士
1982/9 - 1985/7,厦门大学,物理化学,硕士
1978/9 - 1982/7,福州大学,物理化学,学士

工作经历(科研与学术工作经历,按时间倒序排序):
2016/05至今, 福州大学,化学学院,教授
1999/09-2015/06, 哈佛医学院贝思以色列研究中心结构生物学实验室,主任
2003/07-2016.01,中科院福建物构所化学生物学研究室,研究室主任
1993/03-1999/07,美国斯奎伯斯研究所,分子生物学系,博士后
1985/09-1988/12,中科院福建物质结构研究生所,助理研究员
 

教学简介
在哈佛医学院工作期间,培养博士后6名。

回国后,在中科院福建物构所工作期间成功申报“生物化学和分子生物学”博士点(2005年),并作为学科带头人负责该博士点11年。

培养硕博士研究生29名,已毕业博士13名,硕士8名。12名博士到国外进修博士后,其中四人已经回国在国内高校担任教授。4名硕士到国外继续深造博士学位。多年来与国外单位开展研究生联合培养,中国丹麦联合培养硕博士,已有一人获得丹麦博士学位,一人获得了丹麦的Danida奖金,两人获得丹麦奖学金获得丹麦博士学位,同时开展中法博士联合培养,已毕业2人。
 

科研简介
黄明东教授先后主持了多项研究课题,包括中国科学院“百人计划”、 国家杰出青年基金、国家基金委重点项目、国家基金委重大国际合作项目、国家基金委面上项目、科技部863、福建省基金委重点项目等。迄今为止,共在国内外期刊发表论文140余篇,有五篇发表在《科学》和《自然》及子刊杂志上,其中三篇为第一或通讯作者,主编和参编著作3部。

两个主要研究方向:See below for the introduction of my research in English.
1. 光动力学抗菌和抗肿瘤研究。发展了一种抗菌的药物,主要特点是广谱性:可以杀灭包括革兰氏阳性和阴性的多种细菌,特别是能够杀灭耐药菌。该项技术目前已经转让给青岛阳光动力公司,并发展出抗菌PM2.5口罩等已经上市产品,并正在开发新一代产品。
2. 结构生物学研究。在水解酶及其调控蛋白、受体蛋白领域,特别是尿激酶和尿激酶受体的结构和功能研究方面处于世界一流行列:在国际学术杂志上发表了系列的研究论文和综述,获得了国家基金委重大国际合作和科技部863等国家级项目的资助,也获得国外机构如澳大利亚国家健康与医学研究理事会(NHMRC)的资助,此外,还获得了制药公司的资助,包括了美国辉瑞制药、中科院诺和诺德中心、和浙江海正制药。基于这些结果组建了中国丹麦肿瘤和水解酶联合研究中心,这是中国丹麦第一个双边研究中心。
基于结构研究发展了系列尿激酶、尿激酶受体、PAI-1的抑制剂,用于抗肿瘤、溶血栓、促纤溶等应用。

英文:My recent research focuses on 3 directions:
(1) One focus of our research is on the structures and functions of fibrinolytic proteins, including urokinase (uPA), its receptor (uPAR), inhibitor (PAI-1), and tPA [1-3]. We determined the crystal structures of uPAR [4-6], uPAR:vitronectin complex [7], uPA in complex with various inhibitors, and the Michael complexes of tPA:PAI-1[8] and uPA:PAI-1 [9]. PAI-1 and uPA are biomarkers for cancer metastasis, having the highest level of clinical evidence, level of evidence 1, as recommended by American Society for Clinical Oncology and the German Breast Cancer. However, no inhibitors of either uPA or PAI-1 go into clinical trials. We developed inhibitors for PAI-1 (small molecule [10] and protein-based, named PAItrap [11]) and uPA (cyclic peptides) [12-15], and discovered new principles for inhibitor development [12, 14, 16]. The study was extended to other types of proteases, including kallikrein [17], matriptase [18, 19], and factor XI. We also developed inhibitors for uPAR [2, 20], and one inhibitor (ATF) was fused to human serum albumin (HSA) by recombinant technique to not only increase plasma half-life, but also to render drug carrier properties of the fusion protein [21, 22].

(2) Another focus is on structures of cell surface receptors [18, 19, 23-25] and human serum albumin [26-32]. Despite its long history, HSA remains to be an actively studied protein due to its wide applications and its abundance and important functions in human (~0.4 mM in human blood). I determined a series of crystal structures of HSA in the presence of various ligands. A surprising finding is the conversion of glucose from cyclic form to linear form induced by HSA as defined by our crystal structure studies [30], demonstrating a new function for this old protein [29].

(3) On the area of chemical biology, we developed a technology for biomedical imaging, cancer therapy, and antimicrobial applications. We synthesized a unique fluorescent probe (beta-Carboxy Zinc Phthalocyanine, CPZ[33]) in large quantity, which has three important features: (a) it has strong fluorescence (ex610nm/em690nm); (b) when illuminated at 680nm, CPZ generates reactive oxygenated species (ROS); (c) CPZ contains a carboxy group which can be activated and attached to protein or peptide. We conjugated CPZ to a number of peptides: (a) urokinase receptor targeting peptide (ATF, [34]); (b) polylysine peptide [35, 36]; (c) Gonadotropin-releasing hormone (GnRH) peptide targeting at GnRH receptor [37], and demonstrated the tumor targeting capability of the conjugates in mice models. We also used the lysine-conjugated CPZ for antimicrobial applications [38-40] and demonstrated that it also inactivated drug resistant bacterial strains. This conjugate was later found practical applications in facial masks and various fabric materials (http://www.sundynamictech.com/).

References:
See also https://www.ncbi.nlm.nih.gov/pubmed/?term=Huang%2CMingdong%5BAU%5D+OR+Huang%2CMing-dong%5BAU%5D
1. Yuan, C. and M. Huang, Does the urokinase receptor exist in a latent form? Cell Mol Life Sci, 2007. 64(9): p. 1033-7.
2. Chen, Z., et al., Challenges for drug discovery - a case study of urokinase receptor inhibition. Comb Chem High Throughput Screen, 2009. 12(10): p. 961-7.
3. Ngo, J.C., et al., Structural basis for therapeutic intervention of uPA/uPAR system. Curr Drug Targets, 2011. 12(12): p. 1729-43.
4. Huai, Q., et al., Structure of human urokinase plasminogen activator in complex with its receptor. Science, 2006. 311(5761): p. 656-9.
5. Xu, X., et al., Identification of a new epitope in uPAR as a target for the cancer therapeutic monoclonal antibody ATN-658, a structural homolog of the uPAR binding integrin CD11b (alphaM). PLoS One, 2014. 9(1): p. e85349.
6. Lin, L., et al., Structure-based engineering of species selectivity in the interaction between urokinase and its receptor: implication for preclinical cancer therapy. J Biol Chem, 2010. 285(14): p. 10982-92.
7. Huai, Q., et al., Crystal structures of two human vitronectin, urokinase and urokinase receptor complexes. Nat Struct Mol Biol, 2008. 15(4): p. 422-3.
8. Gong, L., et al., Crystal Structure of the Michaelis Complex between Tissue-type Plasminogen Activator and Plasminogen Activators Inhibitor-1. J Biol Chem, 2015. 290(43): p. 25795-804.
9. Lin, Z., et al., Structural basis for recognition of urokinase-type plasminogen activator by plasminogen activator inhibitor-1. J Biol Chem, 2011. 286(9): p. 7027-32.
10. Lin, Z., et al., Structural insight into inactivation of plasminogen activator inhibitor-1 by a small-molecule antagonist. Chem Biol, 2013. 20(2): p. 253-61.
11. Gong, L., et al., Structural basis of specific inhibition of tissue-type plasminogen activator by plasminogen activators inhibitor-1. Data Brief, 2016. 6: p. 550-5.
12. Jiang, L., et al., Distinctive binding modes and inhibitory mechanisms of two peptidic inhibitors of urokinase-type plasminogen activator with isomeric P1 residues. Int J Biochem Cell Biol, 2015. 62: p. 88-92.
13. Sorensen, H.P., et al., Selection of High-Affinity Peptidic Serine Protease Inhibitors with Increased Binding Entropy from a Back-Flip Library of Peptide-Protease Fusions. J Mol Biol, 2015. 427(19): p. 3110-22.
14. Jiang, L., et al., Insights into the serine protease mechanism based on structural observations of the conversion of a peptidyl serine protease inhibitor to a substrate. Biochim Biophys Acta, 2016. 1860(3): p. 599-606.
15. Kromann-Hansen, T., et al., A Camelid-derived Antibody Fragment Targeting the Active Site of a Serine Protease Balances between Inhibitor and Substrate Behavior. J Biol Chem, 2016. 291(29): p. 15156-68.
16. Jiang, L., et al., Rezymogenation of active urokinase induced by an inhibitory antibody. Biochem J, 2013. 449(1): p. 161-6.
17. Xu, P., et al., Design of Specific Serine Protease Inhibitors Based on a Versatile Peptide Scaffold: Conversion of a Urokinase Inhibitor to a Plasma Kallikrein Inhibitor. J Med Chem, 2015. 58(22): p. 8868-76.
18. Yuan, C., et al., Structure of catalytic domain of Matriptase in complex with Sunflower trypsin inhibitor-1. BMC Struct Biol, 2011. 11: p. 30.
19. Zhao, B., et al., Crystal structures of matriptase in complex with its inhibitor hepatocyte growth factor activator inhibitor-1. J Biol Chem, 2013. 288(16): p. 11155-64.
20. Rullo, A.F., et al., Re-engineering the Immune Response to Metastatic Cancer: Antibody-Recruiting Small Molecules Targeting the Urokinase Receptor. Angew Chem Int Ed Engl, 2016. 55(11): p. 3642-6.
21. Li, R., et al., A novel tumor targeting drug carrier for optical imaging and therapy. Theranostics, 2014. 4(6): p. 642-59.
22. Zheng, K., et al., Dual actions of albumin packaging and tumor targeting enhance the antitumor efficacy and reduce the cardiotoxicity of doxorubicin in vivo. Int J Nanomedicine, 2015. 10: p. 5327-42.
23. Yuan, C., et al., Crystal structures of the ligand-binding region of uPARAP: effect of calcium ion binding. Biochem J, 2016. 473(15): p. 2359-68.
24. Jiang, L., et al., Dimer conformation of soluble PECAM-1, an endothelial marker. Int J Biochem Cell Biol, 2016. 77(Pt A): p. 102-8.
25. Liu, M., et al., Recombinant hepatocyte growth factor activator inhibitor 1: expression in Drosophila S2 cells, purification and crystallization. Acta Crystallogr F Struct Biol Commun, 2017. 73(Pt 1): p. 45-50.
26. Guo, S., et al., Structural basis of transport of lysophospholipids by human serum albumin. Biochem J, 2009. 423(1): p. 23-30.
27. Luo, Z., et al., Structural evidence of perfluorooctane sulfonate transport by human serum albumin. Chem Res Toxicol, 2012. 25(5): p. 990-2.
28. Wang, Y., et al., A fluorescent fatty acid probe, DAUDA, selectively displaces two myristates bound in human serum albumin. Protein Sci, 2011. 20(12): p. 2095-101.
29. Wang, Y., S. Wang, and M. Huang, Structure and enzymatic activities of human serum albumin. Curr Pharm Des, 2015. 21(14): p. 1831-6.
30. Wang, Y., et al., Structural mechanism of ring-opening reaction of glucose by human serum albumin. J Biol Chem, 2013. 288(22): p. 15980-7.
31. Yang, F., et al., Effect of human serum albumin on drug metabolism: structural evidence of esterase activity of human serum albumin. J Struct Biol, 2007. 157(2): p. 348-55.
32. Zhu, L., et al., A new drug binding subsite on human serum albumin and drug-drug interaction studied by X-ray crystallography. J Struct Biol, 2008. 162(1): p. 40-9.
33. Chen, J., et al., Derivatizable phthalocyanine with single carboxyl group: Synthesis and purification. Inorganic Chemistry Communications, 2006. 9(3): p. 313-315.
34. Chen, Z., et al., Zinc phthalocyanine conjugated with the amino-terminal fragment of urokinase for tumor-targeting photodynamic therapy. Acta Biomater, 2014. 10(10): p. 4257-68.
35. Chen, Z., et al., Pentalysine beta-carbonylphthalocyanine zinc: an effective tumor-targeting photosensitizer for photodynamic therapy. ChemMedChem, 2010. 5(6): p. 890-8.
36. Li, L., et al., Enhanced photodynamic efficacy of zinc phthalocyanine by conjugating to heptalysine. Bioconjug Chem, 2012. 23(11): p. 2168-72.
37. Xu, P., et al., Receptor-targeting phthalocyanine photosensitizer for improving antitumor photocytotoxicity. PLoS One, 2012. 7(5): p. e37051.
38. Chen, J., et al., Substituted zinc phthalocyanine as an antimicrobial photosensitizer for periodontitis treatment. Journal of Porphyrins and Phthalocyanines, 2011. 15(04): p. 293-299.
39. Chen, Z., et al., Photodynamic antimicrobial chemotherapy using zinc phthalocyanine derivatives in treatment of bacterial skin infection. J Biomed Opt, 2016. 21(1): p. 18001.
40. Chen, Z., et al., An effective zinc phthalocyanine derivative for photodynamic antimicrobial chemotherapy. Journal of Luminescence, 2014. 152: p. 103-107.


 

社会兼职
中国晶体学会第三、第四届理事会理事
《结构化学》杂志编委
Nature Structural and Molecular Biology,PNAS,Blood等期刊通讯审稿人
中国光学学会第二届生物医学光子学专业委员会常委
中国生物医学工程学会生物医学光子学分会常委
中国化学会应用化学学科卟啉-酞菁专业委员会委员
福建省生物工程协会副主席
福建省化学生物学重点实验室学术委员会委员
福建省药物新靶点研究重点实验室学术委员会委员
国家自然科学基金委员会第十一和十二届生命科学部专家评审组成员
 

科研项目
1. 澳大利亚国家健康与医学研究理事会(NHMRC), “Repurposing Amiloride into Breast Cancer Drugs with a Dual-Targeting Mechanism”,项目起止时间:2016.01-2020.12,批准号:APP1100432,经费:65.1995万澳元,共同申请人,在研.
2. 基金委面上项目,“GPI-LU亚家族蛋白的结构研究”,项目起止时间:2017.01-2020.12,经费:60万元, 申请人,在研.
3. 基金委面上项目,“纤溶酶原激活物抑制因子及其新型抑制剂的结构研究”,项目起止时间:2014.01-2017.12,批准号:31370737,经费:80万元,在研
4. 中科院-诺和诺德专项研究经费,项目起止时间:2012.01-2014.12,批准号:NNCAS-2012-5,经费:60万元
5. 基金委面上项目,项目起止时间:2012.01-2015.12,批准号:21171167,经费:60万元
6. 基金委重大国际合作,项目起止时间:2012.01-2014.12,批准号:31161130356,经费:250万元
7. 美国国立卫生院,项目起止时间:2012.09-2017.04,批准号:U54 HL112302,经费:205万美元
8. 中法蔡元培交流项目,项目起止时间:2011.05-2013.05,批准号:【2011】6019
9. 福建省科技重点项目,项目起止时间:2010.3-2012.3,批准号:2010Y0057,经费:15万元
10. 辉瑞公司横向合作项目,项目起止时间:2009.11-2011.12,经费:6.5万美元
11. 浙江海正药业股份有限公司委托项目,项目起止时间:2008.12-2009.12,经费:15万元
12. 苏州技术研究院委托项目,项目起止时间:2008.05-2009.12,经费:20万元
13. 基金委重大国际合作,项目起止时间:2008.09-2011.8,批准号:30811130467,经费:100万元
14. 美国国立卫生院,项目起止时间:2007.01-2011.12,批准号:R01 HL086584,经费:191.25万美元
15. 美国国立卫生院,项目起止时间:2008.09-2014.05,批准号:P01 HL087203,经费:867.5万美元
16. 基金委杰出青年,项目起止时间:2008.01-2010.12,批准号:30625011,经费:200万元
17. 科技部863项目,项目起止时间:2007.01-2010.12,批准号:2006AA02A313,经费:495万元17.中科院创新基地重要方向项目,项目起止时间:2007.01-2010.12,批准号:C01050402,经费:100万元
18. 科技部973项目,项目起止时间:2007.01-2011.7,批准号:2007CB914304,经费:100万元
19. 福建省发改委产业技术开发专项, 2006.01-2007.12,经费:20万元
20. 基金委重点项目,项目起止时间:2005.01-2008.12,批准号:30430190,经费:135万元
21. 中法先进研究计划,项目起止时间:2005.01-2006.12,经费:5万元
22. 国家人事部高级人才,项目起止时间:2004.12-2005.12,批准号:41052,经费:30万元
23. 结构化学国家重点实验室,项目起止时间:2004.01-2006.12,批准号:40073,经费:9万元
24. 中科院百人计划,项目起止时间:2003.03-2006.02,批准号:IB021061,经费:200万元
25. 福建省自然基金重点,项目起止时间:2003.11-2006.12,批准号:C0320003,经费:15万元
26. 中科院物构所创新前沿交叉基金,项目起止时间:2003.10-2006.12,批准号:IP031049,经费:16万元
27. 福建省青年创新基金,项目起止时间:2003.10-2006.12,批准号:2002J013,经费:6万元
28. 美国心脏协会SDG项目,项目起止时间:2003.01-2006.12,批准号: 0330089N,经费:26万美元
29. 教育部回国人员启动经费,项目起止时间:2003.01-2004.12,经费:2.5万元
 

代表性论文
PEER-REVIEWED PUBLICATIONS: See https://www.ncbi.nlm.nih.gov/pubmed/?term=Huang%2CMingdong%5BAU%5D+OR+Huang%2CMing-dong%5BAU%5D

1. Huang M, Lu SF, Huang JQ and Huang JL (1987). Synthesis and crystal structure of Mo3(3µ-O)(µ-S)3[S2P(OEt)2]4(C3H3N). J. Struc. Chem. 6:29.
2. Huang M, Chen YZ, Tian ZW (1987). The Surface Enhanced Raman Scattering (SERS) effect of Ag(delta+) complex on Ag electrode surface. Acta Physico-Chimica Sinica 3:178.
3. Huang JQ, Lu SF, Shang MY, Lin XT, Huang M, Lin YH, Wu DM, Zhuang HH, Huang JL, Lu JX (1987). Reactivity of the trinuclear Mo-S cluster Mo3S4[S2P(OEt)2]4(H2O) and an interesting "pseudo-aromaticity" of the Mo3(µ-S)3 structural unit. J. Struc. Chem. 6:219.
4. Huang M, Lu SF, Huang JQ, Huang JL (1988). Research on the substitution reaction of the ligands in Mo3S4(dtp)4(H2O) ---Synthesis and crystal structure of Mo3S4(η-dtp)( η?-dtp)2(µ-dtp)(bpy). Acta Physico-Chimica Sinica 4:611.
5. Huang JL, Huang JQ, Shang MY, Zhuang HH, Lu SF, Lin XT, Lin YH, Huang M, Lu JX (1988). Structure and reactivity of molybdenum clusters with loose coordination site, Mo3S4[S2P(OEt)2]4L. Pure & Appl. Chem. 60:1185.
6. Lu SF, Huang JQ, Huang M, Huang JL (1989). The reactivities of Mo clusters - A selective substitution reaction of the bridging (dtp) ligand and the crystal structure of Mo3S4(µ-O2CR)(dtp)3(py). Acta Chimica Sinica English Edition 1:24
7. Lu SF, Huang M, Huang JQ, Huang JL, Lu JX (1989). Substitution reaction of ligands in trinuclear Mo clusters with "loose coordination site" as well as synthesis and crystal structure of [Mo3S4(dtp)3(C3H3N2)3](dtp).(CH3)2CO. Scientia Sinica B32:139.
8. Huang M, Lu SF, Huang JQ, and Huang JL (1989). The replacement reaction of trinuclear molybdenum cluster --- Syntheses and crystal structures of two molybdenum clusters [Mo3S4(dtc)4(DMF)](EtOH) and [Mo3S4(dtc)4(py)](py)2(H2O). Acta Chimica Sinica 47:121.
9. Lu SF, Huang M, Huang JQ, Huang ZX, Huang JL (1990). Structure of Tris(diethyldithiophosphato-S,S')--(diethylthiophosphate-O,S)-mu(Oxazole)-3-sulfido-tri-2-sulfido-cyclo-trimolybdenum (3 Mo-Mo). Acta Cryst. C46:2036.
10. Huang M, DeKock CW (1993). Triphenylsiloxy Complexes. A Novel Compound Containing a Mo(VI)-P bond: MoO2(OSiPh3)2(PPh3). Inorg. Chem. 32:4.
11. Schalk I, Zeng K, Wu SK, Stura EA, Matteson J, Huang M, Tandon A, Wilson IA, Balch WE (1996). Structure and mutational analysis of Rab GDP-dissociation inhibitor. Nature 381:42.
12. Garcia KC, Degano M, Pease LR, Huang M, Peterson PA, Teyton L, Wilson IA (1998). Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen. Science 279:1166.
13. Huang M, Syed R, Stura EA, Stone MJ, Stefanko RS, Ruf W, Edgington TS, Wilson IA (1998). The Mechanism of an Inhibitory Antibody on TF-initiated Blood Coagulation Revealed by the Crystal Structures of Human Tissue Factor, Fab 5G9 and TF-5G9 Complex. J. Mol. Biol. 275:873.
14. Rudd PM, Wormald, MR, Stanfield RL, Huang M, Mattsson N, Speir JA, DeGennaro JA, Fetrow, JS, Dwek RA, Wilson RA (1999). Roles for Glycosylation of Cell Surface Receptors Involved in Cellular Immune Recognition J. Mol. Biol. 293:351.
15. Shliom O, Huang M, Sachais B, Kuo A, Weisel CN, Nassar T, Bdeir K, Hiss E, Gawlak S, Harris S, Mazar A, Higazi AA (2000). Novel Interactions between Urokinase and Its Receptor, J. Biol. Chem. 275:24304.
16. Huang M, Huang GQ, Furie B, Furie BC, Seaton B (2000). Molecular basis of vitamin K-dependent protein-membrane interaction: Xray structure of prothrombin-phospholipid complex at 2.0 angstrom. Blood 96(11):1928.
17. Huang M, Ruf W, Edgington TS, Wilson IA (2000). Crystal Structure of a TF-VIIa Complex – Conformation of a Mobile Loop. FASEB J. 14:LB152.
18. Rudolph MG, Huang M, Teyton L, Wilson IA (2001). Crystal Structure of an Isolated Vα Domain of the 2C T-cell Receptor, J. Mol. Biol. 314:1.
19. Huang M, Weissman, JT, Wang C, Chen W, Wilson IA, Balch WE (2001). Crystal Structure of Sar1-GDP at 1.7Å Resolution and the Role of the N-terminus in ER Export. J. Cell Biology, 155(6):937.
20. Huang M, Weissman JT, Wang C, Balch WE, Wilson IA (2002). Protein engineering for crystallization of the GTPase Sar1 that regulates ER vesicle budding. Acta Cryst. D58:700.
21. Luz JG, Huang M, Garcia KC, Rudolph NG, Teyton L, and Wilson IA (2002). Structural comparison of allogeneic and syngeneic TCR-pMHC complexes: a buried alloreactive mutation subtly alters peptide presentation substantially increasing Vβ interaction. J. Exp. Med, 195(9):1175-1186.
22. Huang M, Rigby AC, Morelli X, Grant MA, Huang G, Furie B, Seaton B & Furie BC (2003). Structural basis of membrane binding by Gla domains of vitamin K–dependent proteins. Nature Structural Biology, 10(9):751-6.
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86. Liu Y, Zhou S, Tu D, Chen Z, Huang M, Zhu H, Ma E, Chen X (2012). Amine-functionalized lanthanide-doped zirconia nanoparticles: optical spectroscopy, time-resolved fluorescence resonance energy transfer biodetection, and targeted imaging. J Am Chem Soc. Sep 12;134(36):15083-90.
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获奖情况
中科院“百人计划”(2003年)
国家“杰出青年科学基金”获得者(2006年)
国家级百千万人才(2007年)
国务院政府特殊津贴(2013年)
福建省科技创新领军人才(2016年)
 

其他
 国际合作:
1. 2008年起成立了《中国丹麦肿瘤和水解酶联合研究中心》(http://www.proteasesandcancer.org/chinese%20welcome.html)。丹麦是全世界创新力排名第五的国家,中丹共成立了十个联合研究中心,本中心是第一个中丹研究中心(http://www.nsfc.gov.cn/Portal0/InfoModule_396/25904.htm),本中心在第一期的资助结束后,2011年经过了国际范围的评估,得到了第二期资助。2013.5通过了丹麦国家研究基金委第二期资助的中期考核。多年来开展研究生联合培养,已有一人获得博士学位,两人获得丹麦奖学金在攻读丹麦博士学位,一人获得了丹麦的Danida奖金。
2. 获得中法先进研究项目和中法蔡元培基金的资助,共同开展研究工作和研究生联合培养。
3. 组织了多次国际会议,包括了2009年和2012年的中丹肿瘤和水解酶国际会议,以及2013年诺和诺德-中科院国际研讨会。应邀在多个国际会议上做大会邀请报告,包括了2006年第48届美国血液学年会、2006年第18届ISFP会议、2007年第21届ISTH(国际血栓和纤溶大会)、2007年International Workshop of Plasminogen Activation国际会议、2008年和2012年的Gordon Research Conference on Plasminogen Activation。
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