2000 - 2004 , 理学博士 , 生物化学与分子生物学 , 清华大学生物科学与技术系
1996 - 2000 , 工学学士 , 环境工程 , 清华大学环境科学与工程系
2010 - 至今 , 副研究员 , 北京大学生命科学学院
2006 - 2010 , 博士后 , School of Pharmacology, University of South Carolina， USA; Department of Pharmacology, Toxicology & Therapeutics, University of Kansas Medical Center, USA 导师：朱宝亭 (Bao-Ting Zhu)
2005 - 2005 , 博士后 , Department of Botany and Plant Sciences，University of California, Riverside, USA 导师：朱健康 (Jian-Kang Zhu)
1. Identification of substrate-binding sites and substrates of small heat shock protein by in vivo photo-crosslinking. VIIth International Congress on Stress response in Biology and Medicine, Sept. 16-19, 2015, Huangshan, Anhui Province, China
2. In vivo substrate diversity and preference of small heat shock protein IbpB revealed by photo-crosslinking , The 4th Asia Pacific Protein Association (the APPA2014 Conference)，May 17-20, 2014, Jeju Island. South Korea
3. Chaperone function and mechanism of small heat shock proteins. The 4th National Protein Society Conference Oct. 12-15, 2013, Hefei, Anhui Province, China
4. Molecular mechanism of DegP-mediated thermotolerance in E. coli. Enzymology and Enzyme Engineering Symposium, Sept. 13-14, 2013. Institute of Biology, Chinese Academy of Sciences, Chengdu, Sichun Province, China
5. DegP primarily functions as a protease for the biogenesis of outer membrane proteins in cells. Symposium on Protein Folding, Post-Translational Modification & Quality Control, May 29, 2013, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
6. Defining the essential functions of DegP for the biogenesis of outer membrane proteins in cells. The 11th National Enzymology Society Conference, May 16-19, 2013, Wuxi, Jiangsu Province, China
Selected Publications (*corresponding author)
1. Yan Wang, Rui Wang, Feng Jin, Yang Liu, Jiayu Yu, Xinmiao Fu * and Zengyi Chang *. A Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-barrel Outer Membrane Proteins in Bacteria. J. Biol. Chem., 2016, in Press.
2. Liu, J, Fu, X*, Chang Z*. Hypoionic shock treatment enables aminoglycosides antibiotics to eradicate bacterial persisters. Scientific Reports, 2015, 5: 14247.
3. Zou Z, Fu X*. Abiotic regulation: a common way for proteins to modulate their functions. Curr Protein Pept Sci. 2015, 16(3):188-95. (editor-invited review)
4. Fu X* Chaperone function and mechanism of small heat shock proteins, Acta Biochimica et Biophysica Sinica, 2014, 46(5):347-56 (editor-invited review)
5. Ezemaduka A, Yu J, Shi X, Zhang K, Yin C, Fu X*, Chang Z*. A small heat shock protein enables Escherichia coli to grow at a lethal temperature of 50ºC conceivably by maintaining cell envelope integrity. J. Bacteriol., (2014) 196:2004-2011
6. Ge X, Lyu ZX, Liu Y, Wang R, Zhao XS, Fu X*, Chang Z*. Identification of FkpA as a key quality control factor for the biogenesis of outer membrane proteins under heat shock conditions, J. Bacteriol., 2014, 196: 672-680
7. Ge X, Wang R, Ma J, Liu Y, Ezemaduka A, Chen P, Fu X* and Chang Z*. DegP primarily functions as a protease for the biogenesis of β-barrel outer membrane proteins in Gram-negative bacterium Escherichia coli, FEBS J, 2014 , 281: 1226-1240
8. Fu X*, Shi X, Yan L, Zhang H, Chang Z.*, In vivo substrate diversity and preference of small heat shock protein IbpB as revealed by using a genetically incorporated photo-crosslinker, J. Biol. Chem., 2013, 288(44):31646-54.
9. Fu X*, Shi X, Yin L, Liu J, Joo K, Lee J, Chang Z.*, Small heat shock protein IbpB acts as a robust chaperone in living cells by hierarchically activating its multi-type substrate-binding residues., J Biol Chem, 2013, 288(17):11897-906.
10. Fu X, Wang P, Fukui M, Long C, Yin L, Choi HJ, Zhu BT. PDIp Is a Major Intracellular Estrogen-Storage Protein That Modulates the Tissue Levels of Estrogen in the Pancreas, Biochem. J., 2012, 447(1):115-23.
11. Fu X, Wang P, Zhu BT. Characterization of the Estradiol-Binding Site Structure of Human Protein Disulfide Isomerase (PDI), PLoS ONE, 2011, 6(11):e27185.
12. Fu X, Wang P, Zhu BT, Characterization of the Estradiol-Binding Site Structure of Human Pancreas-Specific Protein Disulfide Isomerase: Indispensable Role of the Hydrogen Bond between His278 and the Estradiol 3-Hydroxyl Group, Biochemistry, 2011, 50:106-115
13. Fu X, and Zhu BT, Human Pancreas-Specific Protein Disulfide Isomerase (PDIp) Can Function as a Chaperone Independently of Its Enzymatic Activity by Forming Stable Complexes with Denatured Substrate Proteins., Biochem. J., 2010, 429:157-69
14. Fu X, Zhang H, Zhang X, Cao Y, Jiao W, Liu C, Song Y, Abulimiti A and Chang Z, A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins., J. Biol. Chem., 2005, 280:6337-6348
15. Fu X, Jiao W and Chang Z, Phylogenetic and biochemical studies reveal a potential evolutionary origin of animal small heat shock proteins from bacterial class A, J Mol Evol., 2006, 62:257-266
16. Fu X and Chang Z, Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis, Biochem. Biophy. Res. Commun., 2004, 316:291-299
17. Abulimiti A+, Fu X+, Gu L, Feng X and Chang Z, Mycobacterium tuberculosis Hsp16.3 Nonamers are Assembled and Re-assembled via Trimer and Hexamer Intermediates., J. Mol. Biol., 2003, 326:1013-1023, +contributed equally
18. Liu JF, Fu X*, and Chang Z* (2016). A reciprocating motiong-driven rotation mechanism for the ATP synthase, Science China Life Sciences, doi: 10.1007/s11427-015-4955-0.
19. Zhang K, Ezemaduka AN, Wang Z, Hu H, Shi X, Liu C, Lu X, Fu X, Chang Z, Yin CC., A novel mechanism for small heat shock proteins to function as molecular chaperones., Scientific Reports, 2015, 5: 8811
20. Fu X, Tang Y, Dickinson BC, Chang CJ, Chang Z., An oxidative fluctuation hypothesis of aging generated by imaging H2O2 levels in live Caenorhabditis elegans with altered lifespans., Biochem Biophys Res Commun., 2015, 458(4):896-900.
21. Fu X*, Chang Z, Shi X, Bu D, Wang C. Multilevel structural characteristics for the natural substrate proteins of bacterial small heat shock proteins., Protein Sci., 2014 , 23: 229-237
22. Shi X, Yan L, Zhang H, Sun K, Chang Z, Fu X*, Differential degradation for small heat shock proteins IbpA and IbpB is synchronized in Escherichia coli: implications for their functional cooperation in substrate refolding, Biochem Biophys Res Commun, 2014, 452(3):402-7
23. Hong W, Wu YE, Fu X, Chang Z., Chaperone-dependent mechanisms for acid resistance in enteric bacteria, Trends in Microbiology, 2012, Jul;20(7):328-35.
24. Zhang M, Lin S, Song X, Liu J, Fu Y, Ge X, Fu X, Chang Z, Chen PR., genetically incorporated crosslinker reveals chaperone cooperation in acid resistance, Nature Chemical Biology, 2011, 7: 671-677
25. Fu X and Zhu BT, Both PDI and PDIp can attack the native disulfide bonds in thermally-unfolded RNase and form stable disulfide-linked complexes, BBA-PROTEINS PROTEOM, 2011, 1814(4):487-95
26. Shi X, Wang Z, Yan L, Ezemaduka AN, Fan G, Wang R, Fu X, Yin CC, and Chang Z, Small heat shock protein AgsA forms dynamic fibrils, FEBS Letters, 2011, 585(21):3396-3402.
27. Fu X and Zhu BT, Human pancreas-specific protein disulfide isomerase homolog (PDIp) is an intracellular estrogen-binding protein that modulates estrogen levels and actions in target cells, J Steroid Biochem Mol Biol., 2009, 115:20-29
28. Fu X, Dai X, Ding J, Zhu BT, Pancreas-specific protein disulfide isomerase has a cell type-specific expression in various mouse tissues and is absent in human pancreatic adenocarcinoma cells: implications for its functions, J Mol Histol., 2009, 40:189-99
29. Fu X and Zhu BT, Human pancreas-specific protein disulfide isomerase homolog (PDIp) is redox-regulated through formation of an inter-subunit disulfide bond., Arch Biochem Biophys, 2009, 485:1-9
30. Fu X, Wang P, Zhu BT, Protein disulfide isomerase is a multifunctional regulator of estrogenic status in target cells., J Steroid Biochem Mol Biol., 2008, 112:127-37
31. Jiang XR, Wang P, Fu X and Zhu BT, Chemical synthesis and biochemical characterization of biotinylated derivatives of 17β-estradiol with a long side-chain covalently attached to its C-7α position, Steroids, 2008, 73:1252-61
32. Zhu J, Fu X, Koo YD, Zhu, JK, Jenney FEJr, Adams MW, Zhu Y, Shi H, Yun, DJ, Hasegawa PM and Bressan RA, An enhancer mutant of Arabidopsis salt overly sensitive 3 mediates both ion homeostasis and the oxidative stress response., Mol. Cell. Biol., 2007, 27:5214-5224.
33. Katiyar-Agarwal S, Zhu J, Kim K, Agarwal M, Fu X, Huang A and Zhu JK, The plasma membrane Na+/H+ antiporter SOS1 interacts with RCD1 and functions in oxidative stress tolerance in Arabidopsis, Proc. Natl. Acad. Sci. USA, 2006, 103:18816-18821
34. Fu X and Chang Z, Identification of a Highly Conserved Pro-Gly Doublet in Non-animal Small Heat Shock Proteins and Characterization of Its Structural and Functional Roles in Mycobacterium tuberculosis Hsp16.3, Biochemistry (Moscow), 2006, 71 Suppl 1:S83-90
35. Feng Y, Jiao W, Fu X and Chang Z, Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein., Protein Sci., 2006, 15:1441-1448
36. Fu X and Chang Z, Identification of bis-ANS binding sites in Mycobacterium tuberculosis small heat shock protein Hsp16.3: Evidences for a two-step substrate-binding mechanism, Biochem. Biophys. Res. Commun, 2006, 349:167-171
37. Zhang H, Fu X and Chang Z, The association of small heat shock protein Hsp16.3 with the plasma membrane of Mycobacterium tuberculosis: dissociation of oligomers is a prerequisite, Biochem. Biophy. Res. Commun, 2005, 330:1055-1061
38. Hong W, Jiao W, Hu J, Zhang J, Liu C, Fu X, Shen D, Xia B and Chang Z, Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation, J. Biol. Chem., 2005, 280:27029-27034.
39. Zhang X, Fu X, Zhang H and Chang Z, chaperone-like activity of beta-casein., Int. J. Biochem. Cell. Biol., 2005, 37:1232-1240.
40. Fu X, Zhang X and Chang Z, 4,4'-dianilino-1,1'-binaphthyl-5,5'-sulfonate (bis-ANS), a novel molecule having chaperone-like activity., Biochem. Biophys. Res. Commun., 2005, 329:1087-1093.
41. Fu X, Jiao W, Abulimiti A and Chang Z, Inter-subunit cross-linking suppressed the dynamic oligomeric dissociation of Mycobacterium tuberculosis Hsp16.3 and reduced its chaperone activity, Biochemistry (Moscow), 2004, 69,552-557
42. Chen X, Fu X, Ma Y and Chang Z, Chaperone-like activity of Mycobacterium tuberculosis Hsp16.3 does not require its intact (native) structures, Biochemistry (Moscow), 2004, 70(8):913-9
43. Liu Y, Fu X, Shen J, Zhang H, Hong W and Chang Z, Periplasmic proteins of Escherichia coli are highly resistant to aggregation: revaluation for roles of molecular chaperones in periplasm., Biochem. Biophy. Res. Commun., 2004, 316:795-801.
44. Fu X, Li W, Mao Q and Chang Z, Disulfide bonds convert small heat shock protein Hsp16.3 from a chaperone to a non-chaperone: implications for the evolution of cysteine in molecular chaperones, Biochem. Biophys. Res. Commun, 2003, 308: 627-635
45. Fu X, Liu C, Liu Y, Feng X, Gu L, Chen X and Chang Z, Small heat shock protein Hsp16.3 modulates its chaperone activity by adjusting the rate of oligomeric dissociation., Biochem. Biophys. Res. Commun., 2003, 310: 412-420
46. Feng X, Huang S, Fu X, Abulimiti A and Chang Z, The reassembling process of the nonameric Mycobacterium tuberculosis small heat-shock protein Hsp16.3 occurs via a stepwise mechanism., Biochem. J., 2002, 363:329-334