1. Han L, Zheng J, Wang Y, Yang X, Liu Y, Sun C, Cao B, Zhou H, Ni D, Lou J, Zhao Y, Huang Y*（2016）Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins.Nat Struct Mol Biol. Mar; 23（3）:192-6 .
2. Ni D, Huang Y*（2015）The Expression, Purification, and Structure Determination of BamA from E. coli.Methods Mol Biol. 1329:169-78.
3. Cao B, Zhao Y, Kou Y, Ni D, Zhang XC and Huang Y*(2014) Structure of the nonameric bacterial amyloid secretion channel. Proc Natl Acad Sci USA. Dec 16;111(50):E5439-44.
4. Qiao S, Luo Q, Zhao Y, Zhang XC and Huang Y* (2014) Structural basis for lipopolysaccharide insertion in the bacterial outer membrane Nature Jul 3; 511(7507):108-11.
5. Ni D, Yang K and Huang Y* (2014) Refolding, crystallization and preliminary X-ray crystallographic studies of the β-barrel domain of BamA, a membrane protein essential for outer membrane protein biogenesis. Acta Crystallogr F Struct Biol Commun 70(Pt 3):362-5.
6. Ni D, Wang Y, Yang X, Zhou H, Hou X, Cao B, Lu Z, Zhao X, Yang K and Huang Y* (2014) Structural and functional analysis of the β-barrel domain of BamA from Escherichia coli. FASEB J 28(6):2677-2685.
7. Huang Y*, Smith B., Chen L, Baxter R & Deisenhofer J* (2009) Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC. Proc Natl Acad Sci USA, 106(18): 7403-7.
8. Huang Y, Baxter R, Smith BS, Partch CL, Colbert CL and Deisenhofer J (2006) Crystal structure of cryptochrome 3 from Arabidopsis thaliana and its implication for photolyase activity. Proc Natl Acad Sci USA, 103(47): 17701-6
9. Huang Y, Park YC, Rich RL, Segal D, Myszka D. G. and Wu H (2001). Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain. Cell, 104: 781-790.
10.Huang Y, Rich R., Myszkat D. and Wu H. (2003) Requirement of both the second and third BIR domains for the relief of X-linked inhibitor of apoptosis protein (XIAP)-mediated caspase inhibition by Smac. J. Biol. Chem. 278(49): 49517-22
11.Huang Y, Lu M. and Wu H. (2004) Antagonizing XIAP-mediated caspase-3 inhibition: Achilles' heel of cancers? Cancer Cell. 5(1): 1-2
12.Xu G, Cirilli M, Huang Y, Rich RL, Myszka DG, and Wu H (2001). Covalent inhibition revealed by the crystal structure of the p35/caspase-8 complex. Nature, 410: 494-497.
13.Lin SC, Huang Y, Lo YC, Lu M, and Wu H (2007) Crystal structure of the BIR1 domain of XIAP In two crystal forms. Journal of Molecular Biology
14.Lu M Lin S, Huang Y, Kang YJ, Rich R, Lo YC, Myszka D, Han J and Wu H (2007) XIAP induces NF-κB activation via the BIR1/TAB1 interaction and BIR1 dimerization. Molecular Cell 26: 1-14
15.Xu G, Rich RL, Steegborn C, Min T, Huang Y, Myszka DG and Wu H (2003). Mutational analysis of the p35-caspase interaction: A bowstring kinetic model of caspase inhibition by p35. J. Biol. Chem. 278 (7): 5455-61.
16.Wang S, Huang Y, and Zhou Z (1997). Calcium dependence of myocardial hypothermial tolerance on sources of activator. Cryobiology 35 (3): 193-200.
发表论文
[1] Weiwei Bei, Qingshan Luo, Huigang Shi, Haizhen Zhou, Min Zhou, Xinzheng Zhang, Yihua Huang. Cryo-EM structures of LolCDE reveal the molecular mechanism of bacterial lipoprotein sorting in Escherichia coli. PLOS Biology[J]. 2022, 20(10): https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9595528/.[2] 黄亿华. Structures of the BAM complex and its recognition of the β-barrel outer membrane protein (β-OMP) substrates. FASEB J. 2020, [3] 黄亿华. Cryo-EM structure of the nonameric CsgGCsgF. Plos Biology. 2020, [4] 黄亿华. Structure of Yidc from Thermotoga maritima and its implications for Yidc-midiated membrane protein insertion. FASEB J. 2018, [5] Wang, Yan, Pannuri, Archana Andole, Ni, Dongchun, Zhou, Haizhen, Cao, Xiou, Lu, Xiaomei, Romeo, Tony, Huang, Yihua. Structural Basis for Translocation of a Biofilm-supporting Exopolysaccharide across the Bacterial Outer Membrane. JOURNAL OF BIOLOGICAL CHEMISTRY[J]. 2016, 291(19): 10046-10057, http://dx.doi.org/10.1074/jbc.M115.711762.[6] Han, Long, Zheng, Jiangge, Wang, Yan, Yang, Xu, Liu, Yanqing, Sun, Chuanqi, Cao, Baohua, Zhou, Haizhen, Ni, Dongchun, Lou, Jizhong, Zhao, Yongfang, Huang, Yihua. Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins. NATURE STRUCTURAL & MOLECULAR BIOLOGY[J]. 2016, 23(3): 192-196, http://dx.doi.org/10.1038/nsmb.3181.[7] 黄亿华. Structural and functional analysis of the β-barrel domain of BamA from Escherichia coli.. FASEB J. 2014, [8] Ni, Dongchun, Wang, Yan, Yang, Xu, Zhou, Haizhen, Hou, Xiaomin, Cao, Baohua, Lu, Zhixin, Zhao, Xinsheng, Yang, Kun, Huang, Yihua. Structural and functional analysis of the beta-barrel domain of BamA from Escherichia coli. FASEB JOURNAL[J]. 2014, 28(6): 2677-2685, http://dx.doi.org/10.1096/fj.13-248450.[9] Qiao, Shuai, Luo, Qingshan, Zhao, Yan, Zhang, Xuejun Cai, Huang, Yihua. Structural basis for lipopolysaccharide insertion in the bacterial outer membrane. NATURE[J]. 2014, 511(7507): 108-U523, http://dx.doi.org/10.1038/nature13484.[10] Dongchun Ni, Kun Yang, Yihua Huang. Refolding, crystallization and preliminary X-ray crystallographic studies of the β-barrel domain of BamA, a membrane protein essential for outer membrane protein biogenesis. Acta Crystallographica. Section F, Structural Biology Communications. 2014, 70(Pt 3): 362-365, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3944703/.[11] Cao, Baohua, Zhao, Yan, Kou, Yongjun, Ni, Dongchun, Zhang, Xuejun Cai, Huang, Yihua. Structure of the nonameric bacterial amyloid secretion channel. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA[J]. 2014, 111(50): E5439-E5444, http://dx.doi.org/10.1073/pnas.1411942111.[12] Ni, Dongchun, Yang, Kun, Huang, Yihua. Refolding, crystallization and preliminary X-ray crystallographic studies of the beta-barrel domain of BamA, a membrane protein essential for outer membrane protein biogenesis. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS[J]. 2014, 70: 362-365, http://dx.doi.org/10.1107/S2053230X14003008.[13] Huang, Yihua, Smith, Barbara S, Chen, Lucy X, Baxter, Richard H G, Deisenhofer, Johann. Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA[J]. 2009, 106(18): 7403-7407, https://www.webofscience.com/wos/woscc/full-record/WOS:000265783600027.[14] Miao Lu, Su-Chang Lin, Yihua Huang, Young Jun Kang, Rebecca Rich, Yu-Chih Lo, David Myszka, Jiahuai Han, Hao Wu. XIAP Induces NF-κB Activation via the BIR1/TAB1 Interaction and BIR1 Dimerization. Molecular Cell. 2007, 26(5): 689-702, http://dx.doi.org/10.1016/j.molcel.2007.05.006.[15] Lin, SuChang, Huang, Yihua, Lo, YuChih, Lu, Miao, Wu, Hao. Crystal structure of the BIR1 domain of XIAP in two crystal forms. JOURNAL OF MOLECULAR BIOLOGY[J]. 2007, 372(4): 847-854, http://dx.doi.org/10.1016/j.jmb.2007.07.019.[16] 黄亿华. Crystal structure of cryptochrome 3 from Arabidopsis thaliana and its implication for photolyase activity. Proc Natl Acad Sci USA. 2006, [17] Huang, YH, Lu, M, Wu, H. Antagonizing XIAP-mediated caspase-3 inhibition: Achilles' heel of cancers?. CANCER CELL[J]. 2004, 5(1): 1-2, http://dx.doi.org/10.1016/S1535-6108(03)00340-4.[18] 黄亿华. Smac dimer relieves effector caspase inhibition by binding to the BIR2 and BIR3 domains within each XIAP molecule. J. Biol. Chem. 2003, [19] Xu, GZ, Cirilli, M, Huang, YH, Rich, RL, Myszka, DG, Wu, H. Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex. NATURE[J]. 2001, 410(6827): 494-497, https://www.webofscience.com/wos/woscc/full-record/WOS:000167583800048.[20] Huang, YH, Park, YC, Rich, RL, Segal, D, Myszka, DG, Wu, H. Structural basis of caspase inhibition by XIAP: Differential roles of the linker versus the BIR domain. CELL[J]. 2001, 104(5): 781-790, http://dx.doi.org/10.1016/S0092-8674(01)00273-2.[21] Wang Yan, Andole Pannuri Archana, Ni Dongchun, Zhou Haizhen, Cao Xiou, Lu Xiaomei, Romeo Tony, Huang Yihua. Structural Basis for Translocation of a Biofilm-supporting Exopolysaccharide across the Bacterial Outer Membrane *. The Journal of Biological Chemistry. 291(19): 10046-10057, http://dx.doi.org/10.1074/jbc.M115.711762.
