陆珺霞
武汉科技大学, 化学与化工学院, 教授，博士生导师
出生年月：1977-06
研究领域：生物核磁、神经退行性疾病、生物矿化
电话：+86 13601975620 │ 邮箱：ljx@wust.edu.cn
地址：湖北省武汉市青山区和平大道947号
教育经历
2002-08至2007-08, 美国迈阿密大学, 生物化学, 博士, 导师: Gary Lorigan
1999-9至2002-06, 复旦大学, 化学系, 硕士, 导师: 王韵华
1995-09至1999-06, 复旦大学, 化学系, 学士
工作经历
2015.4-2023.7 上海科技大学，生命科学与技术学院，课题组长，研究员，
2013.7-2015.4 美国国家健康研究所，研究员
2012.3-2013.4 美国西北太平洋国家研究所，研究助理
2007.7-2011.7 美国国家健康研究所，博士后
研究概况
主要研究方向为利用固态核磁研究神经退行性疾病相关淀粉样蛋白结构，功能性纤维蛋白结构，生物矿化蛋白等。在国际高水平期刊，包括Cell, PNAS, Nature Communication, J. Am. Chem. Soc.等著名杂志发表论文近40篇。主持国家自然科学基金（2项）、国家重点研发（1项）等项目。
具体研究方向如下：
1） 细胞坏死程序性调控中重要信号传导蛋白的结构变化和互作机制
2） 神经退行性疾病ALS相关蛋白TDP-43相分离和聚合过程中瞬时动态中间体研究
3） 神经退行性疾病ALS相关蛋白TDP-43的药物筛选
4） 生物矿化和材料的研究，研究牙釉蛋白对牙釉质形成和骨质生成的调控，牙釉蛋白功能性高聚物结构，设计新型仿生材料。
5） 多肽纤维材料
代表性论文
[1] Wu, X. L. #; Hu, H. #; Dong, X. Q.; Zhang, J.; Wang, J.; Schwieters, C. D.; Liu, J.; Wu, G.X.; Li, B.; Lin, J. Y.; Wang, H. Y.* and Lu, J. X.* (2021) The amyloid structure of mouse RIPK3 (Receptor interacting protein kinase 3) in cell necroptosis. Nat Commun. 12:1627 doi.org/10.1038/s41467-021-21881-2
[2] Wu, X. L.#; Ma, Y.#; Zhao, K.#; Zhang, J.; Sun, Y.; Li, Y.; Dong, X.Q.; Hu, H.; Liu, J.; Wang, J.; Zhang, X.; Li, B.; Wang, H.; Li, D.; Sun, B.; Lu, J.X. * and Liu, C. * (2021) The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3. Proc. Natl. Acad. Sci. USA April 6, 2021 118 (14) e2022933118; https://doi.org/10.1073/pnas.2022933118
[3] Zhuo, X. F.; Wang, J.; Zhang J.; Jiang L. L.; Hu, H. Y*. and Lu, J. X*. (2020) Solid-state NMR reveals the structural transformation of the TDP-43 amyloidogenic region upon fibrillation. J. Am. Chem. Soc. 142, 7, 3412-3421.
[4] Hu, H. #; Wu, X.L. #; Wu, G. X.; Nan, N.; Zhang J.; Zhu, X. X.; Zhang Y.; Shu Z. Q.; Liu, J.; Liu, X.Y.; Lu, J. X*. and Wang, H. Y.* (2020) RIP3-mediated necroptosis is regulated by inter-filament assembly of RIP homotypic interaction motif, Cell Death Differ. Jul 31. doi: 10.1038/s41418-020-0598-9
[5] Song, R. #; Wu, X. #; Xue, B.; Yang, Y.; Huang, W.; Zeng, G.; Wang, J.; Li, W.; Cao, Y.; Wang, W*.; Lu, J. X.* and Dong, H.* (2019) Principles governing catalytic activity of self-assembled short peptides. J. Am. Chem. Soc. 141, 223-231.
[6] Lu, J.X.; Qiang, W.; Yau W.M.; Schwieters, C. D.; Meredith, S.C. and Tycko R.* (2013) Molecular structure of β-amyloid fibrils in Alzheimer’s disease brain tissue Cell 154,1257-1268 (with video paperflick)
[7] Qiang,W.; Yau, W.M.; Lu, J.X.; Collinge, J.; and Tycko, R. *, (2017) Structural Variation in Amyloid-β Fibrils from Alzheimer's Disease Clinical Subtypes Nature 541, 217-221
[8] Jing Liu, Xia-lian Wu, Yu-teng Zeng, Zhi-heng Hu and Jun-xia Lu* Solid-state NMR studies of amyloids (2023) Structure Cell Press. 10.1016/j.str.2023.01.005 Review
[9] Jing Zhang, Yushi Bai, Jian Wang, Bing Li, Stefan Habelitz and Jun-xia Lu* (2022) Calcium interactions in amelogenin-derived peptide assembly Front. Physiol. 13:1063970
[10] Yu-Teng Zeng, Lu-Lu Bi, Xiao-Feng Zhuo, Ling-Yun Yang, Bo Sun and Jun-xia Lu* (2022) Different Intermolecular Interactions Drive NonpathogenicLiquid–Liquid Phase Separation and Potentially Pathogenic Fibril Formation by TDP-43 Int. J. Mol. Sci. 23,15227.
[11] Jing-Yu Lin, Ming-Hui Sun, Jing Zhang, Meng Hu, Yu-Teng Zeng, Qian-Qian Yi, Jian Wang, Yun Bai, Yifeng Zhang*, Jun-Xia Lu* (2022) Solid-state NMR (SSNMR) Characterization of Osteoblast from Mesenchymal Stromal Cell Differentiation to Osteoblast Mineralization. Journal of bone and mineral research plus, Oct; 6(10): e10662
[12] Dong, X. Q.; Lin, J. Y.; Wang, P. F.; Li, Y.; Wang, J.; Li, B.; Liao, J. and Lu, J. X.* (2021) Solid-State NMR Studies of the Succinate-Acetate Permease from Citrobacter Koseri in Liposomes and Native Nanodiscs. Life, 11, 908.
[13] Yi, C. Y. #; Xia, J. #; He, L#; Ling, Z. Y.; Wang, X. S.; Yan, Y.; Wang J. J.; Zhao, X. H.; Fan, W. G.; Sun, X. Y.; Zhang R. H.; Ye, S.; Zhang, R. G.; Ma, L. Y.; Zhang, Y.G.; Zhou, H. L.; Huang, Z.; Niu, J. Q.; Long, G*.; Lu, J. X*.; Zhong, J*.and Sun B*. (2020) Junctional and somatic hypermutation-induced CX4C motif is critical for the recognition of a highly conserved epitope on HCV E2 by a human broadly neutralizing antibody, Cell Mol. Immunol. Mar 31:1-11
[14] Zhang, J.; Wang J.; Ma, C. W. and Lu, J. X.* (2020) Hydroxyapatite formation coexists with amyloid-like self-assembly of human amelogenin. Int. J. Mol. Sci. 21, 8, 2946.
[15] Chu, Y. #; Dong, X. #; Kang, Y. J.; Liu, J.; Zhang, T.; Yang, C.; Wang, Z.; Shen, W.; Huo, H.; Zhuang, M.; Lu, J. X.* and Liu, Y.* (2020) The Chaperone BAG6 Regulates Cellular Homeostasis between Autophagy and Apoptosis by Holding LC3B. iscience, Oct 21; 23(11):101708.
[16] Ma, C.W.; Zhang, J.; Dong, X.Q. and Lu, J. X*. (2019). Amyloid structure of high-order assembly of Leucine-rich amelogenin revealed by solid-state NMR. J. Struct. Biol. 206, 29-35.
[17] Arachchige, R. J.; Burton, S. D.; Lu, J. X.; Ginovska, B. Harding, L.K.; Taylor, M.E.; Tao, J.; Dohnalakova, A.; Tarasevich, B.; Bucko, G.W. and Shaw, W. J* (2018) Solid-state NMR identification of intermolecular interactions in amelogenin bound to hydroxyapatite, Biophys. J., Nov 6; 115(9):1666-1672 doi. 10.1016/j-bpj.2018.08.027
[18] He, L.; Gu, W.; Wang, M.; Chang, X.; Sun, X.; Zhan,g Y.; Lin, X.; Yan, C.; Fan, W.; Su, P.; Wang, Y.; Yi, C.; Lin, G.; Li, L.; Jiang, Y.; Lu, J.X; Dong, C.; Wang, H.; Sun, B.*. (2018) Extracellular Matrix Protein 1 promotes follicular helper T cells differentiation and antibody production, Proc. Natl. Acad. Sci. USA 115(34):8621-8626. doi: 10.1073/pnas.1801196115,
[19] Lu, J.X.*; Dong, X.Q. and Zhang, J.J. (2017) Solid-State Structure of Abeta (A beta) in Alzheimer's Disease Protein & Peptide Letters, 24(4), 322-330 Review
[20] Lu, J.X.; Bayro, M.J. and Tycko, R*. (2016) Major Variations in HIV-1 Capsid Assembly Morphologies Involve Minor Variations in Molecular Structures of Structurally Ordered Protein Segments, J. Biol. Chem. vol 291, No. 25, pp. 13098-13112
[21] Scherpelz, K. P.; Lu, J.X.; Tycko R. and Meredith, S.C.* （2016）Preparation of Amyloid Fibrils Seeded from Brain and Meninges, Protein Amyloid Aggregation: Methods and Protocols, Methods in Molecular Biology, David Eliezer (ed.), vol. 1345, 299-311
[22] Lu, J.X.; Burton, S.D.; Xu, Y.M.; Buchko G.W. and Shaw, W.J.* (2014) The flexible structure of the K24S28 region of Leucine-Rich Amelogenin Protein (LRAP) bound to apatites as a function of surface type, calcium, mutation, and ionic strength Front. Physiol. 5, 254, 1-8
[23] Lu, J.X.; Xu, Y.M. and Shaw, W.J.* (2013) Mineral Association Changes the Secondary Structure and Dynamics of Amelogenin J. Dent. Res. 92, 1000-1004 (IF8.94)
[24] Lu, J.X.; Xu, Y.M. and Shaw, W.J.* (2013) Phosphorylation and Ionic Strength Alter the LRAP-HAP interface in the N-terminus Biochemistry. 52, 2196-2205
[25] Lu, J.X.; Sharpe S.; Yau, W.Y. and Tycko R.* (2010) Oligomerization State and Supramolecular Structure of the HIV-1 Vpu Protein Transmembrane Segment in Phospholipid Bilayers Protein Sci. 19, 1877-1896
[26] Lu, J.X.; Yau, W.Y. and Tycko R.* (2010) Evidence from solid state NMR for non-helical conformations in the transmembrane domain of the amyloid precursor protein Biophys. J. 100, 711-719
[27] Chu, S. D., Abu-Baker, S., Lu, J.X. and Lorigan, G.A.* (2010) N-15 Solid-state NMR spectroscopic studies on phospholamban at its phosphorylated form at Ser-16 in aligned phospholipid bilayers Biochim. Biophys. Acta.-biomembranes 1798 312-317
[28] Abu-Baker, S. #, Lu, J.X. #, Chu, S.D., Shetty, K.K., Gor’kov, P.L., and Lorigan, G.A.* (2007) The structural topology of wild-type phospholamban in oriented lipid bilayers using N-15 solid-state NMR spectroscopy Protein Sci. 16, 2345-2349
[29] Abu-Baker, S., Lu, J.X., Chu, S.D., Brinn, C.C., Makaroff, C.A., and Lorigan, G.A.* (2007) Side chain and backbone dynamics of phospholamban in phospholipid bilayers utilizing H-2 and N-15 solid-state NMR spectroscopy Biochemsitry. 46, 11695-11706.
[30] Lu, J.X., Blazyk J. and Lorigan, G. A.* (2006) Exploring membrane selectivity of the antimicrobial peptide KIGAKI using Solid-State NMR spectroscopy Biochim. Biophys. Acta. 1758, 1303-1313.
[31] Lu, J.X., Damodaran, K. and Lorigan, G. A.* (2006) “Probing Membrane Topology by 1H-13C Heteronuclear Dipolar Solid-State NMR Spectroscopy” J. Magn. Reson. 178, 283-287.
[32] Lu, J.X., Damodaran, K., Blazyk, J. and Lorigan, G. A.* “Solid-State NMR Relaxation Studies of the Interaction Mechanism of Antimicrobial Peptides with Phospholipid Bilayer Membranes” Biochemistry. (2005) 44, 10208-10217.
[33] Lu, J.X., Caporini, M. A. and Lorigan, G. A. (2004) “The Effects of Cholesterol on Magnetically Aligned Phospholipid Bilayers: A Solid-State NMR and EPR Spectroscopy Study” J. Magn. Reson. 168: 18-30.
[34] Li, S., Lu, J.X., Gan, J. H., Wang, Y. H., Huang Z. X.* and Xia Z. X.* (2005) Structure of the F58W mutant of cytochrome b5: the mutation leads to multiple conformations and weakens stacking interactions Acta Crystallogr., Sect. D: Biol. Crystallogr. D61(2), 180-189.
[35] Su, H., Lu, J.X., Wang, Y. H., Ren, Y., Xie, Y. and Huang Z. X.* (2004) Study on the DME-cytochrome b(5) and its mutants at site of F58 Chinese Sci. Bull. 49, 18, 1914-1919
[36] Wang, W. H., Lu, J.X., Yao P., Xie, Y. and Huang Z. X.* (2003) The distinct heme coordination environments and heme-binding stabilities of His39Ser and His39Cys mutants of cytochrome b(5) Protein Eng. 16,12 1047-1054
[37] Wang, Y. H., Lu, J.X., Wang, W. H., Ren, Y., Xie, Y. and Huang Z. X.* (2002) Roles of Phe58 in Stabilizing Structure of Cytochrome b5 Chinese Sci. Bull. 47, 24, 2063-2066.
