個人介紹:

昌增益1965年出生于江西省萍鄉市，1984年畢業于華東師範大學生物系，獲學士學位，同年考取中國科學院上海生物化學研究所碩士研究生，之後通過教育部CUSBEA（中美聯合招收生物化學與分子生物學博士研究生）項目遴選赴美國留學，1992年獲美國貝勒醫學院生物化學博士學位。于1996年回國，在清華大學生物科學與技術系任副教授，1997年獲得“國家傑出青年科學基金”，1998年破格晉升為清華大學教授。于2003年調beat365官方网站工作，曾任副院長一職（2007-2013）。曾為國家973項目首席科學家主持十二五項目，回國至今發表學術論文100多篇，研究成果涉及蛋白質的功能、活性調控機制、質量控制、膜蛋白生成的分子機制和生物休眠的分子機制等多方面，特别側重于對活細胞中蛋白質的研究；我們對于在目标蛋白質中通過遺傳手段引入可以誘發光交聯的非天然氨基酸技術體系進行了諸多改進：如建立了随機引入方法體系，也構建出了特定用于引入非天然氨基酸的細菌細胞體系，還建立了一種用于檢測交聯結果的高通量SDS-PAGE電泳體系（一塊膠可同時分析384種蛋白質樣品）等。代表性的發現包括：揭示了一種參與細菌外膜蛋白生成的超分子複合體；揭示了一種全新的細菌亞細胞結構-複蘇延遲體（隻在停止生長和分裂的細胞中形成，在細胞複蘇時發生解聚，其中的蛋白質被重新利用）；揭示了ATP合酶的兩種功能狀态并提出了該酶活性的換擋調控機制。這些工作得到了國際同行的高度關注。

教育經曆:

1992 - 1995，博士後，美國休斯醫學研究所 (Howard Hughes Medical Institute, Huston)；
1985 - 1992，理學博士，生物化學，美國貝勒醫學院（Baylor College of Medicine)（通過教育部CUSBEA項目留學美國）；
1984 - 1985，碩士研究生，生物化學，中國科學院上海生物化學研究所,赴廣州進行英語培訓；
1980 - 1984，理學學士，生物學，上海華東師範大學。

工作經曆:

2003.9開始　　 beat365官方网站教授、博士生導師。
2002.7-2002.10 哈佛大學醫學院 訪問教授。
1998-2003.8　　 清華大學生物系 教授、博士生導師（生物化學與分子生物學）。
1996-1998　　　　清華大學生物系 副教授。

社會服務工作:

（1）2003-至今，歐美同學會留美分會 理事
（2）教育部高等學校生物科學專業教學指導分委員會 委員（2006-2010）
（3）科技部“蛋白質研究”重大科學研究計劃專家組 成員（2006-2010年）
（4）國際科學理事會中國委員會(ICSU-China)委員 (2003-2018)
（5）國家中長期（2006-2020）科學與技術發展規劃戰略研究 骨幹研究員 （2003-2004）

榮譽獎勵:

（1）獲2020年國家自然科學二等獎（第三完成人）
（2）獲2019年教育部自然科學獎一等獎（第三完成人）
（3）北京市教學名師獎，2009
（4）主持并主講的全英文本科生課程《生物化學》獲教育部國家精品課程，2005
（5）“國家中長期科學和技術發展規劃領導小組辦公室” 頒發榮譽證書，2004
（6）北京市先進科普工作者，2002
（7）美國哈佛醫學院訪問教授，2002
（8）國家傑出青年科學基金獲得者，1997
（9）中國教育部CUSBEA（中美聯合招收生物化學研究生項目）獎學金赴美國留學，1985

學術任職:

2023-2027，中國生物化學與分子生物學會 副理事長
2018-2022，中國生物化學與分子生物學會 監事長；教育專業委員會 主任委員
2018-2024，國際生物化學及分子生物學聯盟(IUBMB) 執委（出版委員會主席）
2017-2019，亞洲及大洋洲生物化學家及分子生物學家聯盟（FAOBMB) 主席
2014-2017,2022-，第五屆中國科協國際科聯工作協調委員會（ICSU-CHINA） 委員
2014-2018，中國生物化學與分子生物學會 副理事長、黨委書記
2014-2018，亞太地區蛋白質學會（APPA） 主席
2011-2015，中國生物化學與分子生物學會蛋白質專業委員會 主任委員
2009-2017，中國生物物理學會 理事
2008-2014，國際蛋白質學會 執委
2003-至今，歐美同學會留美分會 理事

雜志任職:

2018-至今 Protein Science刊物 副主編（Associate Editor）
2013至今，雜志《Biochemical and Biophysical Research Communication》（BBRC），Editor編委
2012-至今《生命的化學》，編委，常務編委
2008至今，《中國生物化學與分子生物學報》，副主編；
2008-至今，國際蛋白質協會主辦刊物《Protein Science》，Associate Editor 副主編2002至今，
2009-2020，國際生物化學與分子生物學聯合會（IUBMB）主辦刊物《IUBMB Life》，Editorial Board member編委；
2009-2012，雜志《Acta Biochimica Et Biophysica Sinica》(ABBS)，Editor常務編委；
2008-2012，國際生物化學與分子生物學聯合會（IUBMB）主辦刊物《Biochemistry and Molecular Biology Education》，Editorial Board member編委；
2008-2017，《中國科學：生命科學》（Science China Life Sciences），Executive Vice Editor-in-Chief常務副主編；
2008-2011，雜志《Journal of Biological Chemistry》（JBC），Editorial Board member編委；
2003-2008, 雜志《科學通報》Associate Editor特邀編輯；
2002-2018，國際蛋白質協會主辦刊物《Protein Science》，Editorial Advisory Board member編委；

評審任職:

國家自然科學基金委評審專家（1999年2008年）

會議發言與組織:

Learning about proteins: from in test tubes to in living cells (International Conference of Punjab University, “Recent Innovations in Molecular Sciences”, Nov. 6-8, Lahore, Pakistan; Plenary talk)

The biogenesis and quality control of b-barrel outer membrane proteins as explored in living cells (Sino-Germany Conference, Oct. 7-10, 2019, Beijing, China)

Exploring proteins in living cells: Uncovering the regrowth-delay body and a novel protein translocon (2018 World Life Science Conference, Oct. 27-29, 2018, Beijing, China; Session c0-chair)

Discovery of the Quiescent Body that Functions as a Biological Timer for Growth Resumption of Non-growing Bacterial Cells（Sino-UK Life Science and Medicine Summit, Sep. 26-28, 2017, Beijing)

The biogenesis and quality control of b-barrel outer membrane proteins as explored in living cells (2017 Gordon Research Conference on Membrane Protein Folding, Jun. 4-9, 2017, Easton, USA)


The biogenesis and quality control of beta-barrel outer membrane proteins as explored in living cells (2016 World Life Science Conference, Nov. 1-2, 2016, Beijing, China)


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 (中國，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.

雜志編輯:

2018-至今 Protein Science 副主編 (Associate Editor)
2013至今，Biochemical and Biophysical Research Communication(BBRC) 執行編委(Editor)
2012-至今《生命的化學》，編委，常務編委
2008至今，《中國生物化學與分子生物學報》，副主編；
2008-2016，國際蛋白質協會主辦刊物《Protein Science》編委
2009-2020，國際生物化學與分子生物學聯合會（IUBMB）主辦刊物《IUBMB Life》，Editorial Board member編委；
2009-2012，雜志《Acta Biochimica Et Biophysica Sinica》(ABBS)，Editor常務編委；
2008-2012，國際生物化學與分子生物學聯合會（IUBMB）主辦刊物《Biochemistry and Molecular Biology Education》，Editorial Board member編委；
2008-2017，《中國科學：生命科學》（Science China Life Sciences），Executive Vice Editor-in-Chief常務副主編；
2008-2011，雜志《Journal of Biological Chemistry》（JBC），Editorial Board member編委；
2003-2008, 雜志《科學通報》Associate Editor特邀編輯；
2002-2018，國際蛋白質協會主辦刊物《Protein Science》，Editorial Advisory Board member編委；

書籍編撰:

（1）《中國大百科全書》生物科學輯，生物化學與分子生物學科學 副主編 （2）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. （3）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, .511-525. （4）昌增益 “從分子水平認識生命現象--回顧與展望”，《北大講座》第十輯，2006年1月，北京大學出版社，302-318頁。 （5）昌增益（譯者）《蛋白質、酶和基因-化學與生物學的交互作用》(原著：Fruton, J. S.)，2005年1月出版，清華大學出版社（701頁）。 （6）昌增益（譯者）《二十世紀生物學的分子革命--分子生物學所走過的路》（原著：Morange, M.），2002年2月，科學出版社（256頁）。（該書2020年被教育部選擇為中學生課外讀物。） （7）付立傑，陳克勤，昌增益《生物技術世紀》（原著：Rifkin J.），上海科技教育出版社，2000年。

教材編撰:

（1）王鏡岩，朱聖庚，徐長法，張庭芳，昌增益，秦詠梅 《生物化學》（上、下冊），2017年1月出版，高等教育出版社。（本人為編者之一，共同編寫了多章，獨立撰寫了第36章“基因組學與蛋白質組學”。）
（2）昌增益，江凡，孟安明，常智傑，餘冰賓《Lehninger生物化學原理》(原著：Nelson, D. L. and Cox, M. M.)（第三版），2005年6月出版，高等教育出版社（本人翻譯第1、16、17、18、19、20章）。
（3）查錫良（主編）《醫學分子生物學》，醫學院校研究生教材（複旦大學），2003年11月，人民衛生出版社；本人撰寫有關蛋白質部分的三章：“第九章，蛋白質的研究曆史與方法”；“第十章，蛋白質分子的折疊、組裝細胞定位及降解”；“第十一章，蛋白質的結構與功能”；245-299頁（大約9萬字）。

執教課程:

1996-現在：《生物化學》（上）、《生物化學》（下） , 主持、主講 , 國家精品課程（2005年）、教育部雙語教學示範課程（2007年）。
生物化學與分子生物學進展 , 主講 , 北京大學 , 2003起 , 研究生課程

      本實驗室主要興趣在于：1.　　生物體内蛋白質，特别是膜蛋白(如ATP合酶,beta桶外膜蛋白等）的生成、質量控制、組裝、調控、作用機制等等；2.生物的脅迫響應,包括衰老和休眠現象的分子機制
　　任何生命形式都不可避免地要經曆像高溫、極端pH值、活性氧等有毒物質的存在等脅迫條件。在這樣的條件下，生物體内的大分子，如DNA、RNA、蛋白質等由非共價弱相互作用維持的空間結構都将受到影響。這其中可能以蛋白質分子受到的威脅最大，蛋白質分子的去折疊往往會導緻聚集的發生，而這将意味着蛋白質分子功能的喪失。過去的研究表明，各種生物的基因組都編碼了一類被稱為分子伴侶（或熱休克蛋白、或脅迫蛋白等）的蛋白質分子。這些蛋白質的角色就是保護生物體内那些容易發生去折疊和聚集的蛋白質。這些“保镖”蛋白質，參與了對體内其它蛋白質分子的“生、老、病、死”等過程。我們關注的一些問題包括：脅迫蛋白質是如何在生物體内發揮其功能的？脅迫蛋白質分子的結構如何對脅迫條件發生瞬時響應而導緻生物學活性順時性提高的？部分生命個體以休眠方式應對極端脅迫條件的分子機制是什麼？與此相關的衰老現象和休眠現象的分子機制是什麼？等等。
　　蛋白質在生物體内發揮作用是通過與其它分子發生相互作用而完成的。大量的蛋白質分子自身或相互之間也發生着大量的相互作用。自身的相互作用，形成同源寡聚體，不同蛋白質分子之間的相互作用即形成異源寡聚體。盡管過去的體外或體内研究已經揭示了大量特異的蛋白質之間的相互作用，但大量發生于生物體内的動态的或弱的相互作用目前還難以鑒定和深入研究。我們關注的一些問題包括：很多通過體外研究被鑒定為以單亞基形式存在的蛋白質，在體内是否能夠形成同源寡聚體？能夠在活細胞條件下鑒定出與特異蛋白質發生相互作用的蛋白質？這樣的以同源或異源寡聚形式發生的蛋白質-蛋白質相互作用如何完成特定的生物學功能？等等。
　　3. 革蘭氏陰性細菌内外膜蛋白的生成轉運、降解、質量控制、組裝及生物活性調控等。主要通過活細胞體系開展研究，利用非天然氨基酸為探針對特定蛋白質進行遺傳标記。
　　E-mail：changzy（AT）pku.edu.cn

119.昌增益. 談生命科學等領域原創性基礎研究成果的獲得與評價[J]. 科技導報, 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項目之曆史回顧[J]. 中國生物化學與分子生物學報, 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.昌增益，蛋白質之活細胞探究，2021，科學通報（邀請綜述），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推薦文章“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.餘家钰，劉洋，殷會佳，昌增益，複蘇延遲體(regrowth-delay body)作為一種标示休眠細菌的可逆亞細胞結構，《中國生物化學與分子生物學報》，2019，35(4):349-352.（邀請短文）
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, 512:100-105. 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, 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).Discovery of a Shortened Version Of SecA (SecAN) that conceivably functions As a Protein-Conducting Channe. BioRxiv, preprint. doi: https://doi.org/10.1101/121335. (online March 28, 2017)
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 China Special 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。 青蒿素作為有效抗瘧藥物的發現： 一個不同尋常的中國故事.中國科學：生命科學，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：劉佳峰，付新苗，昌增益。ATP合酶旋轉催化的一種新機制。《中國科學：生命科學》，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，美國學術不端行為監管體系的建設及其對中國的啟示，《科技導報》，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，從分子水平認識生命現象-回顧與展望，《北大講座》精華集（科學），北京大學出版社，2015年1月，8-21頁。
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，認識生命活動的直接執行者：神奇的蛋白質分子，《科學名家講座》第十二輯，57-85頁，中國言實出版社，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、張萌，昌增益 “認識真核生物細胞内使基因轉錄的蛋白質分子機器-2006年諾貝爾化學獎評述” 《2007科學發展報告》，科學出版社，2007年3月。
*63、馬靜， 葛熙、昌增益 “蛋白質功能研究：曆史、現狀和将來”，生命科學， 2007， 19（3）：294-300。
*62、秦焱，王慧，昌增益 “線蟲中的小分子熱休克蛋白HSP12.1具有分子伴侶活性”生物化學與生物物理進展，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、葉子堅，劉沖，陳效友，昌增益 “分枝杆菌中表達重組蛋白的新載體pMSL的構建”， 江西農業大學學報，2005年第27卷5期，753-758。
*46、昌增益，焦旺旺 “細胞内一種耗能蛋白質降解途徑的發現：2004年諾貝爾化學獎工作介紹”，生物物理學報，2004年，第20卷第6期,第421－425頁。
*45、陳效友，李傳友，馬王與，劉沖，王敬慧，張雪峰，昌增益 “卡介苗菌MDP1基因敲除技術的研究” 中國結核和呼吸雜志，2004年，第27卷第3期，第183-187頁。
*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、毛啟龍，馮修光，昌增益“結核杆菌小分子熱休克蛋白Hsp16.3的高效自發再折疊和再組裝”生物化學與生物物理進展，2002年，29（1）：87-90。1
*30、黃素芳，古良才，毛啟龍，昌增益“Leu122對 Hsp16.3組裝過程中亞基相互作用的影響” 中國生物化學與分子生物學報，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、修志龍，昌增益，蘇志國“20世紀生物技術回顧與21世紀展望”，自然雜志，2000，22（219）：233－240。
19、張代佳，劉傳斌，修志龍，昌增益“微波技術在植物細胞内有效成分提取中的應用”，中草藥，2000， 31（9）：5－6。
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、楊紅梅，毛啟龍，薛濤，昌增益，“結核杆菌小分子熱休克蛋白Hsp16.3一高度保守亮氨酸的定點突變研究”，清華大學學報（自然科學版），1999年36(6):42-45。
*12、昌增益，戴紅政，毛啟龍，餘冰濱 （1999）“克隆的概念，意義與進展”生物學通報，34(11):3-6。
11、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.

本實驗室主要開展活細胞中的蛋白質研究，涉及蛋白質生成、組裝、質量控制，調控和作用機制等，以及細胞休眠的分子機制等方面。

實驗室成員：
資深技術員：劉洋；
秘書：于春燕：
研究生： 殷會佳（本科山東大學）、曾慶芳（本科蘭州大學）、王夢媛（本科北京化工大學）、李春辰（本科中國藥科大學），李鴻飛、陳佩甯，趙志義，趙瑩。實驗室電話62758056