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个人简历
个人介绍文字
昌增益1965年出生于江西省萍乡市，1984年毕业于华东师范大学生物系，获学士学位，同年考取中国科学院上海生物化学研究所硕士研究生，之后通过教育部CUSBEA（中美联合招收生物化学与分子生物学博士研究生）项目遴选赴美国留学，1992年获美国贝勒医学院生物化学博士学位。于1996年回国，在清华大学生物科学与技术系任副教授，1997年获得“国家杰出青年科学基金”，1998年破格晋升为清华大学教授。于2003年调北京大学生命科学学院工作，曾任副院长一职（2007-2013）。曾为国家973项目首席科学家主持十二五项目，回国至今发表学术论文100多篇，研究成果涉及蛋白质的功能、活性调控机制、质量控制、膜蛋白生成的分子机制和生物休眠的分子机制等多方面，特别侧重于对活细胞中蛋白质的研究；我们对于在目标蛋白质中通过遗传手段引入可以诱发光交联的非天然氨基酸技术体系进行了诸多改进：如建立了随机引入方法体系，也构建出了特定用于引入非天然氨基酸的细菌细胞体系，还建立了一种用于检测交联结果的高通量SDS-PAGE电泳体系（一块胶可同时分析384种蛋白质样品）等。代表性的发现包括：揭示了一种参与细菌外膜蛋白生成的超分子复合体；揭示了一种全新的细菌亚细胞结构-复苏延迟体（只在停止生长和分裂的细胞中形成，在细胞复苏时发生解聚，其中的蛋白质被重新利用）；揭示了ATP合酶的两种功能状态并提出了该酶活性的换挡调控机制。这些工作得到了国际同行的高度关注。
教育经历
1992 - 1995，博士后，美国休斯医学研究所 (Howard Hughes Medical Institute, Huston)；
1985 - 1992，理学博士，生物化学，美国贝勒医学院（Baylor College of Medicine)（通过教育部CUSBEA项目留学美国）；
1984 - 1985，硕士研究生，生物化学，中国科学院上海生物化学研究所,赴广州进行英语培训；
1980 - 1984，理学学士，生物学，上海华东师范大学。
1985 - 1992，理学博士，生物化学，美国贝勒医学院（Baylor College of Medicine)（通过教育部CUSBEA项目留学美国）；
1984 - 1985，硕士研究生，生物化学，中国科学院上海生物化学研究所,赴广州进行英语培训；
1980 - 1984，理学学士，生物学，上海华东师范大学。
工作经历
2003.9开始 北京大学生命科学学院教授、博士生导师。
2002.7-2002.10 哈佛大学医学院 访问教授。
1998-2003.8 清华大学生物系 教授、博士生导师（生物化学与分子生物学）。
1996-1998 清华大学生物系 副教授。
2002.7-2002.10 哈佛大学医学院 访问教授。
1998-2003.8 清华大学生物系 教授、博士生导师（生物化学与分子生物学）。
1996-1998 清华大学生物系 副教授。
社会服务工作
（1）2003-至今，欧美同学会留美分会 理事
（2）教育部高等学校生物科学专业教学指导分委员会 委员（2006-2010）
（3）科技部“蛋白质研究”重大科学研究计划专家组 成员（2006-2010年）
（4）国际科学理事会中国委员会(ICSU-China)委员 (2003-2018)
（5）国家中长期（2006-2020）科学与技术发展规划战略研究 骨干研究员 （2003-2004）
（2）教育部高等学校生物科学专业教学指导分委员会 委员（2006-2010）
（3）科技部“蛋白质研究”重大科学研究计划专家组 成员（2006-2010年）
（4）国际科学理事会中国委员会(ICSU-China)委员 (2003-2018)
（5）国家中长期（2006-2020）科学与技术发展规划战略研究 骨干研究员 （2003-2004）
荣誉奖励
（1）获2020年国家自然科学二等奖（第三完成人）
（2）获2019年教育部自然科学奖一等奖（第三完成人）
（3）北京市教学名师奖，2009
（4）主持并主讲的全英文本科生课程《生物化学》获教育部国家精品课程，2005
（5）“国家中长期科学和技术发展规划领导小组办公室” 颁发荣誉证书，2004
（6）北京市先进科普工作者，2002
（7）美国哈佛医学院访问教授，2002
（8）国家杰出青年科学基金获得者，1997
（9）中国教育部CUSBEA（中美联合招收生物化学研究生项目）奖学金赴美国留学，1985
（2）获2019年教育部自然科学奖一等奖（第三完成人）
（3）北京市教学名师奖，2009
（4）主持并主讲的全英文本科生课程《生物化学》获教育部国家精品课程，2005
（5）“国家中长期科学和技术发展规划领导小组办公室” 颁发荣誉证书，2004
（6）北京市先进科普工作者，2002
（7）美国哈佛医学院访问教授，2002
（8）国家杰出青年科学基金获得者，1997
（9）中国教育部CUSBEA（中美联合招收生物化学研究生项目）奖学金赴美国留学，1985
学术任职
2023-2027，中国生物化学与分子生物学会 副理事长
2018-2022，中国生物化学与分子生物学会 监事长；教育专业委员会 主任委员
2018-2024，国际生物化学及分子生物学联盟(IUBMB) 执委（出版委员会主席）
2017-2019，亚洲及大洋洲生物化学家及分子生物学家联盟（FAOBMB) 主席
2014-2017,2022-，第五届中国科协国际科联工作协调委员会（ICSU-CHINA） 委员
2014-2018，中国生物化学与分子生物学会 副理事长、党委书记
2014-2018，亚太地区蛋白质学会（APPA） 主席
2011-2015，中国生物化学与分子生物学会蛋白质专业委员会 主任委员
2009-2017，中国生物物理学会 理事
2008-2014，国际蛋白质学会 执委
2003-至今，欧美同学会留美分会 理事
2018-2022，中国生物化学与分子生物学会 监事长；教育专业委员会 主任委员
2018-2024，国际生物化学及分子生物学联盟(IUBMB) 执委（出版委员会主席）
2017-2019，亚洲及大洋洲生物化学家及分子生物学家联盟（FAOBMB) 主席
2014-2017,2022-，第五届中国科协国际科联工作协调委员会（ICSU-CHINA） 委员
2014-2018，中国生物化学与分子生物学会 副理事长、党委书记
2014-2018，亚太地区蛋白质学会（APPA） 主席
2011-2015，中国生物化学与分子生物学会蛋白质专业委员会 主任委员
2009-2017，中国生物物理学会 理事
2008-2014，国际蛋白质学会 执委
2003-至今，欧美同学会留美分会 理事
杂志任职
2018-至今 Protein Science刊物 副主编（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；
2008-至今，国际蛋白质协会主办刊物《Protein Science》，Associate Editor 副主编2002至今，
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；
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；
2008-至今，国际蛋白质协会主办刊物《Protein Science》，Associate Editor 副主编2002至今，
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；
评审任职
国家自然科学基金委评审专家（1999年2008年）
会议发言与组织
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.
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.
杂志编辑
2018-至今 Protein Science 副主编 (Associate Editor)
2013至今，Biochemical and Biophysical Research Communication(BBRC) 执行编委(Editor)
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；
2008-2016，国际蛋白质协会主办刊物《Protein Science》编委
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；
2013至今，Biochemical and Biophysical Research Communication(BBRC) 执行编委(Editor)
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；
2008-2016，国际蛋白质协会主办刊物《Protein Science》编委
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；
书籍编撰
（1）《中国大百科全书》生物科学辑，生物化学与分子生物学科学 副主编
（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 “从分子水平认识生命现象--回顾与展望”，《北大讲座》第十辑，2006年1月，北京大学出版社，302-318页。
（5）昌增益（译者）《蛋白质、酶和基因-化学与生物学的交互作用》(原著：Fruton, J. S.)，2005年1月出版，清华大学出版社（701页）。
（6）昌增益（译者）《二十世纪生物学的分子革命--分子生物学所走过的路》（原著：Morange, M.），2002年2月，科学出版社（256页）。（该书2020年被教育部选择为中学生课外读物。）
（7）付立杰，陈克勤，昌增益《生物技术世纪》（原著：Rifkin J.），上海科技教育出版社，2000年。
（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 “从分子水平认识生命现象--回顾与展望”，《北大讲座》第十辑，2006年1月，北京大学出版社，302-318页。
（5）昌增益（译者）《蛋白质、酶和基因-化学与生物学的交互作用》(原著：Fruton, J. S.)，2005年1月出版，清华大学出版社（701页）。
（6）昌增益（译者）《二十世纪生物学的分子革命--分子生物学所走过的路》（原著：Morange, M.），2002年2月，科学出版社（256页）。（该书2020年被教育部选择为中学生课外读物。）
（7）付立杰，陈克勤，昌增益《生物技术世纪》（原著：Rifkin J.），上海科技教育出版社，2000年。
教材编撰
（1）王镜岩，朱圣庚，徐长法，张庭芳，昌增益，秦咏梅 《生物化学》（上、下册），2017年1月出版，高等教育出版社。（本人为编者之一，共同编写了多章，独立撰写了第36章“基因组学与蛋白质组学”。）
（2）昌增益，江凡，孟安明，常智杰，余冰宾《Lehninger生物化学原理》(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（本人翻译第1、16、17、18、19、20章）。
（3）查锡良（主编）《医学分子生物学》，医学院校研究生教材（复旦大学），2003年11月，人民卫生出版社；本人撰写有关蛋白质部分的三章：“第九章，蛋白质的研究历史与方法”；“第十章，蛋白质分子的折叠、组装细胞定位及降解”；“第十一章，蛋白质的结构与功能”；245-299页（大约9万字）。
（2）昌增益，江凡，孟安明，常智杰，余冰宾《Lehninger生物化学原理》(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（本人翻译第1、16、17、18、19、20章）。
（3）查锡良（主编）《医学分子生物学》，医学院校研究生教材（复旦大学），2003年11月，人民卫生出版社；本人撰写有关蛋白质部分的三章：“第九章，蛋白质的研究历史与方法”；“第十章，蛋白质分子的折叠、组装细胞定位及降解”；“第十一章，蛋白质的结构与功能”；245-299页（大约9万字）。
科研领域描述
本实验室主要兴趣在于：1. 生物体内蛋白质，特别是膜蛋白(如ATP合酶,beta桶外膜蛋白等）的生成、质量控制、组装、调控、作用机制等等；2.生物的胁迫响应,包括衰老和休眠现象的分子机制
任何生命形式都不可避免地要经历像高温、极端pH值、活性氧等有毒物质的存在等胁迫条件。在这样的条件下，生物体内的大分子，如DNA、RNA、蛋白质等由非共价弱相互作用维持的空间结构都将受到影响。这其中可能以蛋白质分子受到的威胁最大，蛋白质分子的去折叠往往会导致聚集的发生，而这将意味着蛋白质分子功能的丧失。过去的研究表明，各种生物的基因组都编码了一类被称为分子伴侣（或热休克蛋白、或胁迫蛋白等）的蛋白质分子。这些蛋白质的角色就是保护生物体内那些容易发生去折叠和聚集的蛋白质。这些“保镖”蛋白质，参与了对体内其它蛋白质分子的“生、老、病、死”等过程。我们关注的一些问题包括：胁迫蛋白质是如何在生物体内发挥其功能的？胁迫蛋白质分子的结构如何对胁迫条件发生瞬时响应而导致生物学活性顺时性提高的？部分生命个体以休眠方式应对极端胁迫条件的分子机制是什么？与此相关的衰老现象和休眠现象的分子机制是什么？等等。
蛋白质在生物体内发挥作用是通过与其它分子发生相互作用而完成的。大量的蛋白质分子自身或相互之间也发生着大量的相互作用。自身的相互作用，形成同源寡聚体，不同蛋白质分子之间的相互作用即形成异源寡聚体。尽管过去的体外或体内研究已经揭示了大量特异的蛋白质之间的相互作用，但大量发生于生物体内的动态的或弱的相互作用目前还难以鉴定和深入研究。我们关注的一些问题包括：很多通过体外研究被鉴定为以单亚基形式存在的蛋白质，在体内是否能够形成同源寡聚体？能够在活细胞条件下鉴定出与特异蛋白质发生相互作用的蛋白质？这样的以同源或异源寡聚形式发生的蛋白质-蛋白质相互作用如何完成特定的生物学功能？等等。
3. 革兰氏阴性细菌内外膜蛋白的生成转运、降解、质量控制、组装及生物活性调控等。主要通过活细胞体系开展研究，利用非天然氨基酸为探针对特定蛋白质进行遗传标记。
E-mail：changzy（AT）pku.edu.cn
任何生命形式都不可避免地要经历像高温、极端pH值、活性氧等有毒物质的存在等胁迫条件。在这样的条件下，生物体内的大分子，如DNA、RNA、蛋白质等由非共价弱相互作用维持的空间结构都将受到影响。这其中可能以蛋白质分子受到的威胁最大，蛋白质分子的去折叠往往会导致聚集的发生，而这将意味着蛋白质分子功能的丧失。过去的研究表明，各种生物的基因组都编码了一类被称为分子伴侣（或热休克蛋白、或胁迫蛋白等）的蛋白质分子。这些蛋白质的角色就是保护生物体内那些容易发生去折叠和聚集的蛋白质。这些“保镖”蛋白质，参与了对体内其它蛋白质分子的“生、老、病、死”等过程。我们关注的一些问题包括：胁迫蛋白质是如何在生物体内发挥其功能的？胁迫蛋白质分子的结构如何对胁迫条件发生瞬时响应而导致生物学活性顺时性提高的？部分生命个体以休眠方式应对极端胁迫条件的分子机制是什么？与此相关的衰老现象和休眠现象的分子机制是什么？等等。
蛋白质在生物体内发挥作用是通过与其它分子发生相互作用而完成的。大量的蛋白质分子自身或相互之间也发生着大量的相互作用。自身的相互作用，形成同源寡聚体，不同蛋白质分子之间的相互作用即形成异源寡聚体。尽管过去的体外或体内研究已经揭示了大量特异的蛋白质之间的相互作用，但大量发生于生物体内的动态的或弱的相互作用目前还难以鉴定和深入研究。我们关注的一些问题包括：很多通过体外研究被鉴定为以单亚基形式存在的蛋白质，在体内是否能够形成同源寡聚体？能够在活细胞条件下鉴定出与特异蛋白质发生相互作用的蛋白质？这样的以同源或异源寡聚形式发生的蛋白质-蛋白质相互作用如何完成特定的生物学功能？等等。
3. 革兰氏阴性细菌内外膜蛋白的生成转运、降解、质量控制、组装及生物活性调控等。主要通过活细胞体系开展研究，利用非天然氨基酸为探针对特定蛋白质进行遗传标记。
E-mail：changzy（AT）pku.edu.cn
代表性论文
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.昌增益，蛋白质之活细胞探究，2021，科学通报（邀请综述），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, 512:100-105. 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），北京大学出版社，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。
19、张代佳，刘传斌，修志龙，昌增益“微波技术在植物细胞内有效成分提取中的应用”，中草药，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、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。
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.
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.昌增益，蛋白质之活细胞探究，2021，科学通报（邀请综述），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, 512:100-105. 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），北京大学出版社，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。
19、张代佳，刘传斌，修志龙，昌增益“微波技术在植物细胞内有效成分提取中的应用”，中草药，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、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。
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.
执教课程
1996-现在：《生物化学》（上）、《生物化学》（下） , 主持、主讲 , 国家精品课程（2005年）、教育部双语教学示范课程（2007年）。
生物化学与分子生物学进展 , 主讲 , 北京大学 , 2003起 , 研究生课程
生物化学与分子生物学进展 , 主讲 , 北京大学 , 2003起 , 研究生课程
实验室简介
本实验室主要开展活细胞中的蛋白质研究，涉及蛋白质生成、组装、质量控制，调控和作用机制等，以及细胞休眠的分子机制等方面。
