Chang ZengYi received his B.S. degree in Biology in 1984 from East China Normal University (Shanghai, China). He was then accepted as a graduate student of the then Shanghai Institute of Biochemistry, Chinese Academy of Sciences before being selected as a CUSBEA (China United States Biochemistry Examination and Application) fellow to pursue his Ph.D. studies at the Department of Biochemistry, Baylor College of Medicine (Houston, USA). In 1992, he received his Ph.D. in biochemistry and afterwards did his post-doc training at the Howard Hughes Medical Institute (19921995). In 1996, he became an associate Professor at Tsinghua University (Beijing, China) and was promoted to full professorship in 1998. He moved to Peking University in 2003 where he currently serves as the director of the Center for
Protein Science (2005present), and was the Vice-Dean of the School of Life Sciences (20072013). He is currently an executive council member of the International Union of Biochemistry and Molecular Biology (IUBMB),the President of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB), the Past-President of the Asia Pacific Protein Association (APPA) and The Chief supervisor of the Chinese Society of Biochemistry and Molecular Biology. He is currently also serving as an Editor of Biochemical and Biophysical Research Communication, an Associate editor of Protein Science. He has served as an editorial board members for the Journal of Biological Chemistry and IUBMB Life,the executive vice Editor-in-Chief of Science China Life Sciences, among others. His laboratory explores the functions and mechanisms of such proteins as molecular chaperones and proteases in the quality control of proteins under stress conditions or during their biogenesis (especially membrane proteins including the ATP synthase) in living cells. His lab also seeks to understand the molecular mechanism of dormancy (e.g., bacterial persister). He has published more than 80 papers since becoming an independent PI in China.

1984 B.S., Biology, East China Normal University, Shanghai, China.
1985 Graduate Student, Shanghai Institute of Biochemistry, Chinese Academy of Sciences, Shanghai, China.
1984-1985, English Training, Guangzhou English Learning Center (GELC), Sun Yat-Sen University, Guangzhou, China.
1992 Ph.D., Biochemistry, Baylor College of Medicine, Houston, Texas, USA. Ph.D. Thesis: “Probing the Roles of the Highly Conserved Amino Acids in the Catalytic Activity of Adenosine Deaminase”, Advisor: Dr. Rodney, E. Kellems.

1996-1998 Associate Professor, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing, P. R. China.
1998-8/2003 Professor, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing, P. R. China.
Jun.-Sept., 2002 Visiting Professor, Harvard Medical School, Boston, USA.
2003-Present Professor, Department of Biochemistry and Molecular Biology, College of Life Sciences, Peking University, Beijing, P. R. China 100871.
2007-2013 Vice Dean, School of Life Sciences, Peking University, Beijing, China.

Chief Supervisor (2018-2022), The Chinese Society of Biochemistry and Molecular Biology; Chair of the education Committee.
Executive Council member (2018-2021), The International Union of Biochemistry and Molecular Biology (IUBMB)
President(2017-2019) Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB);
President (2011-2014), Asia Pacific Protein Association (APPA);
President (2011-2015), The Chinese Protein Society;
Executive Council Member (2008-2014), The Protein Society;
Vice president (2014-2018), Chinese Association of Biochemistry and Molecular Biology (CSBMB).

Vice President (2023-2027) Chinese Society of Biochemistry and Molecular Biology
Chief Supervisor (2018-2022), The Chinese Society of Biochemistry and Molecular Biology; Chair of the education Committee.
Executive Council member, the International Union of Biochemistry and Molecular Biology (IUBMB)
President (2017-2019) Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB);
President (2011-2014), Asia Pacific Protein Association (APPA);
President (2011-2015), The Chinese Protein Society;
Executive Council Member (2008-2014), The Protein Society;
Vice president (2014-2018), Chinese Association of Biochemistry and Molecular Biology (CSBMB).

2018-current，Protein Science，Associate Editor
2013至今，杂志《Biochemical and Biophysical Research Communication》（BBRC），Editor编委
2012-至今《生命的化学》，编委，常务编委
2008至今，《中国生物化学与分子生物学报》，副主编；
2009-2020，国际生物化学与分子生物学联合会（IUBMB）主办刊物《IUBMB Life》，Editorial Board member编委；
2009-2012，杂志《Acta Biochimica Et Biophysica Sinica》(ABBS)，Editor常务编委；
2008-2012，国际生物化学与分子生物学联合会（IUBMB）主办刊物《Biochemistry and Molecular Biology Education》，Editorial Board member编委；
2008-2017，《中国科学：生命科学》（Science China Life Sciences），Executive Vice Editor-in-Chief常务副主编；
2008-2011，杂志《Journal of Biological Chemistry》（JBC），Editorial Board member编委；
2003-2008, 杂志《科学通报》Associate Editor特邀编辑；
2002-2018，国际蛋白质协会主办刊物《Protein Science》，Editorial Advisory Board member编委；

The Biogenesis and Quality Control of beta-barrel Outer Membrane Proteins in Gram Negative bacteria, The Sri Lanka College of Biochemists Symposium (June 22, 2016, Colombo, Sri Lanka).

Understanding the Unusual Biological Function and Action Mechanism of the Acid Resistant Molecular Chaperone HdeA: from in vitro to in vivo, The 15th IUBMB-24th FAOBMB Conferences (Oct. 21-26, 2014, Taipei)

The functionally Active conformation of the acid resistant molecular chaperone HdeA is disordered, The 8th International Symposium of the Protein Society of Thailand (Aug. 5-7, 2013, Bangkok, Thailand).

The functionally Active conformation of the acid resistant molecular chaperone HdeA is disordered ,The 17th International Biophysics Congress (Beijing, China, Oct 30-Nov 3, 2011)

Two-tier mechanism for acid-responsive chaperone HdeA,The 1st Korean Protein Society Symposium(Seoul, Sept. 23, 2011)

Homo-oligomerization as a Common Way for Proteins to Modulate their Activties ,The third Korea-Japan Seminar in Biomolecular Sciences (Jeju Island, Korea, Feb. 27-Mar. 1, 2011)

Homo-oligomerization as a Common Way for Proteins to Modulate their Activties ,The 10th Protein Science Society of Japan Symposium (Sapporo, Japan)

The Immediate activation of bacterial stress proteins in response to stress conditions,New Frontiers in Microbiology & Biotechnology (Seoul, Korea)

The Immediate activation of stress proteins in response to stress conditions,4th International Congress on Stress Response in Biology and Medicine (October 6-9, 2009, Sapporo, Japan)

Unravelling the many roles of Sir2 in Aging,NSFC-CIHR Canada-China Joint Health Research Program Scientific Workshop , 2009.9.28

Homo-oligomerization as a Common Way for Proteins to Modulate their Activties ,The 21st IUBMB and 12th FAOBMB International Congress in Biochemistry and Molecular Biology, Aug. 4-7, 2009, Shanghai, China.

Homo-oligomerization as a Common Way for Proteins to Modulate their Activties , The 23rd Protein Society Symposium, July 25-29, 2009, Boston, USA (invited speaker).


Modulation of Protein Activities via Homo-oligomerization: a phenomenon that has been underappreciated ,The ATI International Forum (March 9, 2009,Tokai, Japan)

Modulation of protein activities via Homo-oligomerization: a phenomenon that has been underappreciated,The 2nd Pacific Rim International Conference on Protein Science, June 22-27, 2008, Cairns, Australia. , (also as a member of the organizing committee)

Protein Homo-oligomerization: The Biological Significance and Mechanism of Occurrence,10th IUBMB Conference, May 21-25, 2007，Salvador, Brazil. (invited speaker) , Invited one-hour talk

Immediate structural Transformation and Activity Enhancement for Stress Proteins in Responding to Stress Conditions, 20th Symposium of the Protein Society, Aug. 4-9, 2006, San Diego, USA (speaker).

20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress, June 17-23, 2006, Kyoto, Japan (invited speaker).

CAST/ICSU Scientific Forum-in conjunction with the 28th General Assembly of ICSU, Oct. 17, 2005, Shanghai, China (中国，invited speaker).

10th Congress of Federation of Asian and Oceanian Biochemists and Molecular Biologists, Dec 7th-11th, 2003,Bangalore, India, (invited speaker)

The World Conference on Science and Technology, September 13-16, 2001, Manila, the Philippines.

The 15th FAOBMB (Federation of Asian & Oceanian Biochemists and Molecular Biologists) Symposium, October 21-24, 2000, Beijing, China

Protein Structure, Stability, and Folding: Fundamental and Medical Aspects, June 22-26, 1998, Moscow, Russia.

Associate Editor (2018-present), Protein Science,
Editor (2013-present), Biochemical and Biophyscal Research Communication
Editorial Board member (2008-2013), Journal of Biological Chemistry
Editorial Advisory Board member (2008-2017), Protein Science
Editorial Board member (2008-2013), IUBMB Life (a publication of International Union of Biochemistry and Molecular Biology,);
Executive Vice Editor-in-Chief (2008-2018), Science China: Life Sciences
Editorial Board Member, Biochemistry and Molecular Biology Education (a publication of IUBMB);
Vice Editor-in-Chief (2011-present), Chinese Journal of Biochemistry and Molecular Biology；
Editor, Acta Biochimica et Biophysica Sinica.
Guest editor, IUBMB Life Special Issue in celebration of the 21st IUBMB and 12th FAOBMB International Congress of Biochemistry and Molecular Biology to be held in Shanghai, China, August 2-7, 2009.
Guest editor, IUBMB Life Special China Issue, November, 2016.

Chang, Z. Biogenesis of Secretory Proteins. In: Ralph A Bradshaw and Philip D Stahl (Editor-in-Chief),Encyclopedia of Cell Biology, Vol 1, Waltham, MA: Academic Press, 2016, pp. 535-544.

Chang, Z. What Do Small Heat Shock Proteins Do for Bacterial Cells. In: The Big Book on Small Heat Shock Proteins(ed. R.M. Tanguay and L.E. Hightower). Springer, 2015, pp.511-525.

1. The biogenesis and quality control of proteins, especially membrane proteins （such as ATP synthase and beta-barrel outer membrane proteins), working on molecular chaperones and proteinases (e.g., sHSPs, HdeA, DegP, etc).
2. Stress responses of living organisms: including the molecular mechanism of aging and dormancy.

119.昌增益. 谈生命科学等领域原创性基础研究成果的获得与评价[J]. 科技导报, 2024, 42(10): 65-73 https://doi.org/10.3981/j.issn.1000-7857.2024.02.00251
118.昌增益. 教育部留美博士研究生CUSBEA项目之历史回顾[J]. 中国生物化学与分子生物学报, 2023, 39(8): 1212-1228
117.Chang, Zengyi and Fu, Xinmiao (2023) Biogenesis of Secretory Proteins in Eukaryotic and Prokaryotic Cells. In: Bradshaw Ralph A., Hart Gerald W. and Stahl Philip D. (eds.) Encyclopedia of Cell Biology, Second Edition, vol. 1, pp. 689-702. Oxford: Elsevier.
116. Feng Jin and Zengyi Chang (2023) Uncovering the membrane-integrated SecAN Protein that plays a key role in translocating nascent outer membrane proteins. BBA-Protein and Proteomics, 1871(1):140865.
115.Chang Z. (2022) Some random thoughts on the life of protein molecules in living cells, Biochemical and Biophysical Research Communication, Horizons in Biochemistry and Biophysics special issue, 633:33-38.
114..Chang, Z and Fu X (2022) Biogenesis of Secretory Proteins in Eukaryotic and Prokaryotic Cells.Reference Module in Life Sciences (Book), https://doi.org/10.1016/B978-0-12-821618-7.00048-1.
113.Chang Z, Exploring proteins in living cells，2021，Science Bulletin, （Invited review），66:4524-4538.
112.Xinmiao Fu, Anastasia N Ezemaduka, Xinping Lu and Zengyi Chang (2021) The nematode worm Caenorhabditis elegans 12-kDa small heat shock proteins with little in vitro chaperone activity play crucial roles for its dauer formation, longevity and reproduction. Protein Science, 30:2170-2182.
111.Yang Liu#, Jiayu Yu#, Mengyuan Wang#, Qingfang Zeng, Xinmiao Fu, Zengyi Chang (2021) A high-throughput genetically directed protein crosslinking analysis reveals the physiological relevance of the ATP synthase “inserted” state. FEBS Journal, 288:2989-3009.doi: 10.1111/febs.15616.
110. Yanna Zhao, Fengqi Sun, Jiafeng Liu, Yan Wang, Yuanyuan Gao, Zengyi Chang and Xinmiao Fu (2020) Rapid Freezing Enables Aminoglycosides To Eradicate Bacterial Persisters via Enhancing Mechanosensitive Channel MscL-Mediated Antibiotic Uptake. mBio 11:e03239-19. https://doi.org/10.1128/mBio.03239-19.
109*. Yu, J., Liu, Y., Yin, H., and Chang, Z. (2019). Regrowth-delay body as a bacterial subcellular structure marking multidrug-tolerant persisters. Cell　Discovery, doi.org/10.1038/s41421-019-0080-3.(被Faculty 1000推荐文章“It would be hard to over
estimate the importance of this paper”）
108. Shuang Zhang, Yu Cheng, Jing Ma, Yan Wang, Zengyi Chang, and Xinmiao Fu (2019) DegP degrades a wide range of substrate proteins in Escherichia coli under stress conditions. Biochemical Journal 476 (23): 3549-3564.
107. Xinmiao Fu and Zengyi Chang (2019) Biogenesis, quality control and structural dynamics of proteins as explored in living cells via site-directed photo-crosslinking. Protein Science, 28:1194–1209. DOI 10.1002/pro.3627(invited review for the Proteins in the Cell special issue; https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.3627).
106.余家钰，刘洋，殷会佳，昌增益，复苏延迟体(regrowth-delay body)作为一种标示休眠细菌的可逆亚细胞结构，《中国生物化学与分子生物学报》,2019，35(4):349-352（邀请短文）。
105*.Xinmiao Fu, Yan Wang, Xinwen Song, Xiaodong Shi, Heqi Shao, Yang Liu, Meng Zhang and Zengyi Chang* (2019) Subunit interactions as mediated by “non-interface” residues in living cells for multiple homo-oligomeric proteins. Biochemical and Biophysical Research Communications, 512(2019):100-105. doi.org/10.1016/j.bbrc.2019.03.004.
104.Chang, Z*. (2019). The 2018 Nobel Prize in Chemistry: To engineer proteins (enzymes/peptide/antibodies) towards desired properties by constructing random libraries. SCIENCE CHINA Life Sciences, 62(5), 713-724. doi: 10.1007/s11427-019-9498-2.
103*. Xinmiao Fu, Yan Wang, Heqi Shao, Jing Ma, Xinwen Song, Meng Zhang, Zengyi Chang (2018). DegP Functions as a Critical Protease for Bacterial Acid Resistance. FEBS Journal, FEBS Journal, 285:3525-3538.
102*. Fenghui Guan, Jiayu Yu, Jie Yu, Yang Liu, Ying Li, Xin-hua Feng, Kerwyn Casey Huang, Zengyi Chang*, Sheng Ye* (2018). Lateral interactions between protofilaments of the bacterial tubulin homolog FtsZ are essential for cell division. eLife, 7:e35578.
101*.Jin, F. and Chang, Z. (2017).A Shortened Version Of SecA (SecAN) Functions As The Protein-Conducting Channel For Nascent β-Barrel Outer Membrane Proteins. BioRxiv, preprint. doi: https://doi.org/10.1101/121335.
100*. Chang, Z., Wang, C. C. and Li, L. (2016). China is catching up in life Science Research. IUBMB Life, 68(11):844-845. (Editorial for the China Special Issue).
99*. Chang, Z. (2016).The Function of the DegP (HtrA) Protein: Protease vs. Chaperone. IUBMB Life, 68(11):904-907, DOI 10.1002/iub.1561(invited review for the Special China Issue).
98*. Wang, Y., Wang, R., Jin, F., Liu, Y., Yu, J.Y., Fu, XM. and Chang, Z. (2016). A Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-barrel Outer Membrane Proteins in Bacteria. J. Biol. Chem. 291(32):16720-16729. doi: 10.1074/jbc.M115.710715.
97*. Chang Z (2016). The discovery of Qinghaosu (artemisinin) as an effective anti-malaria drug: A unique China Story. Science China Life Sciences,59:81-88. doi.10.1007/s11427-015-4988-z.
中文版：昌增益。 青蒿素作为有效抗疟药物的发现： 一个不同寻常的中国故事.中国科学：生命科学，2doi.10.1360/N052015-00358.
96*. Liu, JF, Fu, XM, and Chang Z. (2016). A reciprocating motiong-driven rotation mechanism for the ATP synthase, Science China Life Sciences, 59:44-48. doi: 10.1007/s11427-015-4955-0. online published.
中文版：刘佳峰，付新苗，昌增益。ATP合酶旋转催化的一种新机制。《中国科学：生命科学》，46（3）：269-273。
95*. Liu, JF, Fu, XM and Chang Z. (2015). Hypoionic shock treatment enables aminoglycosides antibiotics to eradicate bacterial persisters. Scientific Reports, 5:14247, DOI:10:1038/srep14247.
94. 昌增益，王志珍，美国学术不端行为监管体系的建设及其对中国的启示，《科技导报》，2015，,33(15):12-13.
93* Chang, Z. Biogenesis of Secretory Proteins. In: Ralph A Bradshaw and Philip D Stahl (Editor-in-Chief),Encyclopedia of Cell Biology, Vol 1, Waltham, MA: Academic Press, 2016, pp. 535-544.
92*. Chang, Z. What Do Small Heat Shock Proteins Do for Bacterial Cells. In: The Big Book on Small Heat Shock Proteins(ed. R.M. Tanguay and L.E. Hightower). Springer, 2015, pp.511-525.
91*. Xinmiao Fu, Yan Tang, Bryan C. Dickinson, Christopher J. Chang and Zengyi Chang (2015). An oxidative fluctuation hypothesis of aging generated by imaging H2O2 levels in live C. elegans with altered lifespans. Biochemical and Biophysical Research Communications. 458(4):896-900. doi: 10.1016/j.bbrc.2015.02.055
90*. Zhang, K., Ezemaduka, A. N., Wang, Z., Hu, H., Shi, X., Liu, C., Lu, X., Fu, X., Chang, Z. & Yin C. C. (2015). A Novel Mechanism for Small Heat Shock Proteins to Function as Molecular Chaperones, Scientific Reports, 5 : 8811 | DOI: 0.1038/srep08811.
89. 昌增益，从分子水平认识生命现象-回顾与展望，《北大讲座》精华集（科学），太阳成集团tyc7111cc出版社，2015年1月，8-21页。
88. X. Shi, L. Yan, H. Zhang, K. Sun, Z. Chang, X. Fu, (2014). Differential degradation for small heat shock proteins IbpA and IbpB is synchronized in Escherichia coli: implications for their functional cooperation in substrate refolding. Biochemical and Biophysical Research Communications, 452:402-407.doi: http://dx.doi.org/ 10.1016/j.bbrc.2014.08.084.
87*、CHANG ZengYi, GU LiangCai. (2014). Is the mission to identify all the human proteins achievable?-Commenting on the human proteome draft maps. SCIENCE CHINA Life Sciences, 2014, 57(10): 1039-1040.
86*. Li, S., Wang, R., Li, D., Ma, J., Li, H., He, X., Chang, Z., & Weng, Y., (2014). Thermal-triggerd Proteinquake Leads to Disassembly of DegP Hexamer as an Imperative Activation Step. Sci. Rep., 4:4834. (co-corresponding author)..
85*. Ezemaduka, A. N., Yu, J. Y., Shi, X. D., Zhang, K. M., Yin, C. C., Fu, X. M. and Chang, Z. (2014). A small heat shock protein enables Escherichia coli to grow at a lethal temperature of 50ºC conceivably by maintaining cell envelope integrity, Journal of Bacteriology, 196:2004-2011.
84*. Ge, X.,Wang, R., Ma, J., Liu, Y., Ezemaduka, A. N., Chen, P. R., Fu, X. and Chang, Z., (2014) DegP primarily functions as a protease for the biogenesis of β-barrel outer membrane proteins in the Gram-negative bacterium Escherichia coli, FEBS J., 281, 1226-1240.
83*. Xi Ge, Zhi-Xin Lyu, Yang Liu, Rui Wang, Xin Sheng Zhao, Xinmiao Fu, Zengyi Chang ( 2014) Identification of FkpA as a key quality control factor for the biogenesis of outer membrane proteins under heat shock conditions, Journal of Bacteriology, 196: 672-680.
82*. Fu, X., Shi, X., Yan, L., Zhang, H. and Chang, Z., (2013) In vivo substrate diversity and preference of small heat shock protein IbpB as revealed by using a genetically incorporated photo-crosslinker, J Biol Chem, , 288:31646-31654.
81*. Fu, X.,M, Shi, X.D., Yin, L. X., Liu, J. F., Joo, K. H., Lee, J. Y., and Chang, Z. （2013） 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., 288(17):11897-11906.
80. 昌增益，认识生命活动的直接执行者：神奇的蛋白质分子，《科学名家讲座》第十二辑，57-85页，中国言实出版社，2013年11月。
79*. Hong, W., Wu, Y. E., Fu, X. and Chang, Z. (2012), Chaperone-dependent mechanisms for acid resistance in enteric bacteria, Trends in Microbiology, 20:328-335 (invited review)
78*. Zhang, M., Lin, S. Song, X. Liu, J. Fu, Y. Ge, X. Fu, X. Chang, Z. Chen, P. R. (2011) A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance, Nat. Chem. Biol., 7:671-677. （co-corresponding author and cover article for the October issue）
77*. Dickinson, B. C., Tang, Y. Chang, Z. and Chang, C. J. (2011) Development of a Nuclear-Localized Fluorescent Probe for Hydrogen Peroxide and Applications to the Study of Sirtuin-Mediated Oxidative Stress Responses in vivo, Chem. Biol. , 18:943-948 (co-corresponding author)
76*. Wu, S. Ge, X. Lv Z., Zhi Z., Chang, Z. and Zhao, X. S, (2011) Interaction between Bacterial Outer Membrane Proteins and Periplasmic Quality Control Factors: A Kinetic Partitioning Mechanism , Biochem. J., 438:505-511. (co-corresponding author)
75*. Zengyi Chang and Neil Isaacs, (2011) The 2011 Joint Sino-UK Protein Symposium, Biochemical Society Transaction, 39:1311-1312 , The introduction of a special issue Edited by Zengyi Chang and Neil Isaacs. (corresponding author)
74*. Xiaodong Shi, Zhao Wang, Linxuan Yan，Anastasia N. Ezemaduka, Guizhen Fan, Rui Wang, Xin-Miao Fu, Chang-Cheng Yin, Zengyi Chang , (2011) small heat shock protein AgsA forms dynamic fibrils, FEBS Letters, 585:3396-3402.
73*. Chang, Z. (2011) Science China Life Sciences in 2010: a New name marking a new start , Progress in Biochemistry and Biophysics , 38: 804~809
72*. Feng, Y. J., Zhang, M., Hu, M., X., Zheng, J., Jiao, W. W., and Chang ,Z. (2009). Disassembly intermediates of RbsD pro tein remain oligomeric despite the loss of an intact secondary structure. Sci China Ser C-Life Sci, 52(11): 997-1002. (cover article)
71. Chang, Z (2009) “Posttranslational modulation on the Biological Activities of Molecular Chaperones”, Sci. China. Ser. C- Lif Sci.,52:515-520. (invited review)
*70. Chang, Z. (2009) “The CUSBEA Program: Twenty Years Later”, IUBMB Life, 61(6): 555-565.（feature article）
*69. Wang,Y. Ezemaduka, A. N., Tang, Y. and Chang, Z. , (2009) Understanding the Mechanism of the Dormant Dauer Formation of C. elegans: From Genetics to Biochemistry , IUBMB Life , 61(6):607-612. (Invited critical review)
*68. Jiang J, Zhang X, Chen Y, Wu Y, Zhou ZH, Chang Z, Sui SF.(2008) “Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins” Proc Natl Acad Sci U S A, 105(33):11939-11944.
*67. Wu, Y., Hong, W., Zhang, L., and Chang, Z. (2008) “Conserved Amphiphilic Feature Is Essential for Periplasmic Chaperone HdeA to Support Acid Resistance in Enteric Bacteria”, Biochem. J.,412:389-397.
*66. Liu, C., Mao, K., Zhang, M., Sun, Z., Hong, W., Li, C., Peng, B., and Chang, Z. (2008) “The SH3-Like Domain Switches Its Interaction Partners to Modulate the Repression Activity of Mycobacterial Iron-Dependent TranscrIption Regulator (IdeR) in Response to Metal Ion Fluctuations”, J. Biol. Chem., 283(4):2439-2453.
*65. Jiao, W., Hong, W., Li, P., Sun, S., Ma, J., Qian, M., Hu, M., and Chang, Z. (2008) “The Dramatically Increased Chaperone Activity of Small Heat Shock Protein IbpB is Retained for an Extended Period of Time after the Stress Condition is Removed”, Biochem. J., 410(1):63-70.
*64、张萌，昌增益 “认识真核生物细胞内使基因转录的蛋白质分子机器-2006年诺贝尔化学奖评述” 《2007科学发展报告》，科学出版社，2007年3月。
*63、马静， 葛熙、昌增益 “蛋白质功能研究：历史、现状和将来”，生命科学， 2007， 19（3）：294-300。
*62、秦焱，王慧，昌增益 “线虫中的小分子热休克蛋白HSP12.1具有分子伴侣活性”生物化学与生物物理进展，2007， 34（6）：620-624。
*61、Fu, X., and Chang, Z*. (2006) “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., 349:169-171.
*60、Feng, Y., Jiao, W., Fu, X., and Chang, Z. (2006) “Stepwise Disassembly and Apparent Non-stepwise Reassembly for the Oligomeric RbsD Protein “, Protein Science, 15(6):1441-1448.
*59、Zhang, X., Zheng, Y., and Chang, Z. (2006) “Peptide Induced Conformational Changes of E. coli DegP (HtrA) Protease”, Progress in Biochemistry and Biophysics, 33(2):183-189.
58、Fedurkina, N.V., Belousova, L.V., Mitskevich, L.G., Zhou, H.-M., Chang, Z., and Kurganov, B.I. (2006) “The change in the kinetic regime of protein aggregation with temperature increase: Thermal aggregation of rabbit muscle creatine kinase”, Biochemistry-Moscow, 71(3):325-331.
*57、Fu, X. and Chang ,Z. (2006) “Phylogenetic and biochemical studies reveal a potential evolutionary origin of animal small heat shock proteins from bacterial class A” J. Mol. Evol., 62:257-266.)
*56、Chen, X., Fu, X., Ma, Y., and Chang, Z. (2005) “Chaperone-like activity of Mycobacterium tuberculosis Hsp16.3 does not require its intact (native) structures”, Biochemistry-Moscow,70(8):913-919.
*55、Jiao, W., Li, P., Zhang, J., Zhang, H., Chang, Z. (2005) “Small Heat Shock Proteins Function in the Insoluble Protein Complex”, Biochem Biophys Res Commun,335(1):227-231.
*54、Hong, W., Jiao, W., Hu, J., Zhang, J., Liu, C., Fu, X., Shen, D., Xia, B., and Chang, Z. (2005) “Periplasmic Protein HdeA Exhibits Chaperone-like Activity Exclusively within Stomach pH Range by Transforming into Disordered Conformation”, J. Biol. Chem., 280(29):27029-27034.
*53、Fu, X. and Chang , Z (2005) “Identification of a highly conserved Pro-Gly in non-animal small heat shock proteins and characterization of its structural and functional roles in Mycobacterium tuberculosis Hsp16.3” Biochemistry-Moscow, 69(5)：678-685.
*52、Fu, X., Zhang, H., Zhang, X., Cao, Y., Jiao, W., Liu, C., Song, Y., Abulimiti, A., and Chang, Z. (2005) “A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins” J. Biol. Chem., 280 (8) :6337-6348.
*51、Zhang, H. Fu, X. Jiao, W., Zhang, X., Liu, C., and Chang, Z. (2005) “The association of small heat shock protein Hsp16.3 with the plasma membrane of Mycobacterium tuberculosis: dissociation of oligomers is a prerequisite” Biochem Biophys Res Commun, 330:1055-1061.
*50、Jiao，W., Qian, M., Li, P., Zhao, L., and Chang, Z. (2005) “The essential role of the flexible termini in the temperature-responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli” J. Mol. Biol., 347(4):871-884.
*49、Fu, X., Zhang, X., and Chang, Z. (2005) “4`-dianilino-1,1`-binaphthyl-5,5`-sulfonate (bis-ANS), a novel molecule having chaperone-like activity”, Biochem Biophys Res Commun,329:1087-1093.
*48、Zhang, X.,Fu, X., Zhang, H., Liu, C. Jiao, W., and Chang, Z. (2005) “Chaperone-like Activity of β-Casein”, Interna. J. Biochem. Cell Biol., 37:1232-1240.
47、叶子坚，刘冲，陈效友，昌增益 “分枝杆菌中表达重组蛋白的新载体pMSL的构建”， 江西农业大学学报，2005年第27卷5期，753-758。
*46、昌增益，焦旺旺 “细胞内一种耗能蛋白质降解途径的发现：2004年诺贝尔化学奖工作介绍”，生物物理学报，2004年，第20卷第6期,第421－425页。
*45、陈效友，李传友，马王与，刘冲，王敬慧，张雪峰，昌增益 “卡介苗菌MDP1基因敲除技术的研究” 中国结核和呼吸杂志，2004年，第27卷第3期，第183-187页。
*44、Liu, C. He., Y. and Chang Z. (2004) Truncated hemoglobin of Mycobacterium tuberculosis: The oligomeric state change and the interaction with membrane components” Biochem Biophys Res Commun. 316:1163-1172.
*43、Liu Y., Fu, X., Shen, J., Zhang, H., Hong, W., and Chang, Z. (2004) “Periplasmic proteins of Escherichia coli are highly resistant to aggregation: A reappraisal for roles of molecular chaperones in periplasm” Biochem Biophys Res Commun. 316(3):795-801.
*42、Fu, X. and Chang, Z. (2004) “Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis” Biochem Biophys Res Commun. 316:291-299.
*41、Zhang, X. and Chang Z. (2004) “Temperature-dependent protease activity and structural properties of human HtrA2 protease” Biochemistry-Moscow, 69(6):687-692.
*40、Fu, X., Jiao, W., Abulimiti, A. and Chang, Z. (2004) “Inter-subunit cross-linking suppressed the dynamic oligomeric dissociation of Mycobacterium tuberculosis Hsp16.3 and reduced its chaperone activity” Biochemistry-Moscow, 69(5)：552-557.
*39、Fu X, Li W, Mao Q, Chang Z. (2003) “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. 308(3):627-635.
*38、Fu, X. Liu, C., Liu, Y., Feng, X., Gu, L., Chen, X., and Chang, Z.（2003）“Small Heat Shock Protein Hsp16.3 Modulates Its Chaperone Activity by Adjusting the Rate of Oligomeric Dissociation”. Biochem Biophys Res Commun. 310(2):412-420.
*37、Abulimiti, A., Fu, X., Gu., L., Feng, X., and Chang, Z. (2003) ` Mycobacterium tuberculosis Hsp16.3 Nonamers are Assembled and Re-assembled via Trimer and Hexamer Intermediates ` J. Mol. Biol. 326(4):1013-1023.
*36、Abulimiti, A., Qiu, X., Chen, J., Liu, Y., and Chang, Z. (2003) “Reversible methionine sulfoxidation of Mycobacterium tuberculosis small heat shock protein Hsp16.3 and its possible role in scavenging oxidants” Biochem. Biophys. Res. Commun., 305(1):87-93.
*35、Abulimiti, A. and Chang, Z. (2003) `Alpha-crystallin promotes the assembly of trimeric form of the Mycobacterium tuberculosis Hsp16.3 in cell free system` Biochemistry (Moscow), 68（3）：269-274.
34、Chen Y, Lu YJ, Wang HW, Quan S, Chang Z, Sui SF. (2003) “Two-dimensional crystallization of a small heat shock protein HSP16.3 on lipid layer” Biochem Biophys Res Commun. 310(2):360-6.
*33、Gu, L., Abulimiti, A., Li, W., and Chang, Z. (2002) `Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisit for chaperone-like activity` J. Mol. Biol. 319（2）：517-526.
*32、Feng, X., Huang, S. Fu, X., Abulimiti, A. and Chang, Z. (2002) `The reassembling process of the nonameric Mycobacterium tuberculosis small heat shock protein Hsp16.3 occurs via a stepwise mechanism` Biochem. J., 363:329-334
*31、毛启龙，冯修光，昌增益“结核杆菌小分子热休克蛋白Hsp16.3的高效自发再折叠和再组装”生物化学与生物物理进展，2002年，29（1）：87-90。1
*30、黄素芳，古良才，毛启龙，昌增益“Leu122对 Hsp16.3组装过程中亚基相互作用的影响” 中国生物化学与分子生物学报，2002年，18（1）：99-104。
29、Xiu, Z., Chang, Z., Zeng, A. (2002) `Nonlinear Dynamics of Regulations of Bacterial trp operon: Model Analysis of Integrated Effects of Repression, Feedback Inhibition, and Attenuation` Biochnol. Prog. 18:686-693.
28、Pan, G. J., Chang, Z.Y., Scholer, H.R., and Pei, D. Q. (2002) “Stem cell pluripotency and transcrIption factor Oct4” Cell Research 12(5-6):321-329.
*27、Mao, Q., Ke, D., Feng, X. and Chang, Z. (2001) “Preheat Treatment for Mycobacterium tuberculosis Hsp16.3: Correlation Between a Structural Phase Change at 60oC and a Dramatic Increase in Chaperone-like Activity” Biochem. Biophys. Res. Commun., 284:942-947.
*26、Mao, Q., Chang, Z. (2001) “Site-directed Mutation on the only Universally Conserved Residue Leu122 of Small Heat Shock Protein Hsp16.3” Biochem. Biophys. Res. Commun., 289(5):1257-1261.
*25、Mao, Q., Ke, D., Chang, Z. (2001) “Electrostatic interaction plays an essential role for Mycotacterium tuberculosis Hsp16.3 to interact with substrate proteins” Biochemistry (Moscow), 66(8):904-908.
*24、Mao, Q., Ke, D., and Chang, Z. (2001) `Heat treatment of small heat shock proteins alpha-crystallin and Hsp16.3: Structure changes vs. Chaperone like activity` Tsinghua Science and Technology, 6(5):406-409.
23、Chen, Y., An, J., Ding, Y., Dai, H., Mao, Q., Feng, L., Liu, B., Chang, Y., Chen, F., He, H., Tang, H., Chang, Z., and Rao, ZH (2001) “Preliminary X-ray crystallographic studies of the Mycobacterium tuberculosis Hsp16.3 molecular chaperone” Protein and Peptide letters, 8(6):499-502.
*22、Dai, H., Mao, Q., Yang, H., and Chang, Z. (2000) “Probing the Roles of the Only Universally Conserved Leucine Residue in the Oligomerization and Chaperone-like Activity of Mycobacterium tuberculosis Small Heat Shock Protein Hsp16.3”, J. Protein Chem., 19(4):319-326.
21、Wang, L., Duan, M., Zhang, Y. Lin S., and Chang, Z. (2000)“Translocation of P53-regulated laminin receptors in pro-apoptotic microcircustance of human vasculogenesis inhibition”, Cell Biology International, 24(10):745-748
20、修志龙，昌增益，苏志国“20世纪生物技术回顾与21世纪展望”，自然杂志，2000，22（219）：233－240。
18、Yang, H., Huang, S., Dai, H., Gong, Y., Zheng, C., and Chang, Z. (1999), “The Mycobacterium tuberculosis small heat shock protein HSP16.3 Exposes Hydrophobic Surfaces at Mild Conditions: Conformational Flexibility and Molecular Chaperone Activity”, Protein Science, 8（1）:174－179.
*13、杨红梅，毛启龙，薛涛，昌增益，“结核杆菌小分子热休克蛋白Hsp16.3一高度保守亮氨酸的定点突变研究”，清华大学学报（自然科学版），1999年36(6):42-45。
*12、昌增益，戴红政，毛启龙，余冰滨 （1999）“克隆的概念，意义与进展”生物学通报，34(11):3-6。
7、Chang, Z., Wilson, D.K., Kellems, R.E., and Quiocho, F.A. (1997) “Cysteine not Required for the Catalytic Activity of Adenosine Deaminase” Tsinghua Science and Technology (published in English), 2(1):441-446.
6、Chang, Z., Primm, T.P., Jakana, J., Lee, I.H., Chiu, W., Gilb ert, H.F., and Quiocho, F.A. (1996) “Mycobacterium tuberculosis 16-kDa Antigen (HSP16.3) Functions as an Oligomeric Structure in Vitro to Suppress Thermal Aggregation” J. Biol. Chem., 271(12):7218-7223
5、Sideraki, V., Mohamedali, K.A.,Wilson, D.K., Chang, Z., Kellems, R.E., Quiocho, F.A., and Rudolph, F.B. (1996) “Probing the Functional Role of Two Conserved Active Site Aspartates in Mouse Adenosine Deaminase” Biochemistry, 35(4):7862-7872.
4、Chang, Z., Choudhary, A. Lathigra, R. and Quiocho, F.A. (1994) “The Immunodominant 38-kDa Lipoprotein Antigen of Mycobacterium tuberculosis Is a Phosphate-binding Protein” J. Biol. Chem., 269(3):1956-1958.
3、Chouhary, A., Vyas, M. N. Vyas, N. K. Chang, Z. and Quiocho, F.A. (1994) “Crystallization and Preliminary X-ray Crystallographic Analysis of the 38-kDa Immunodominant Antigen of Mycobacterium tuberculosis”Protein Science, 3(12):2450-2451.
2、Sharff, A. J., Wilson, D. K., Chang, Z. and Quiocho, F. A. (1992) “Refined 2.5 A Structure of Murine Adenosine Deaminase at pH 6.0” J. Mol. Biol., 226(4):917-921.
1、Chang, Z., Nygaard, P., Chinault, A. C., and Kellems, R. (1991)“Deduced Amino Acid Sequence of Escherichia coli Adenosine Deaminase Reveals Evolutionarily Conserved Amino Acid Residues: Implications for Catalytic Function” Biochemistry, 30(8):2273-2280.

Teaching the undergraduate course Biochemistry since 1996.

Laboratory Introduction