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姚天明
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- 姓名：姚天明
- 目前身份：
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- 学位：
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学术头衔：
博士生导师
- 职称：-
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学科领域：
生物化学
- 研究兴趣：
姚天明，同济大学化学系教授，博士生导师。 1994年南京大学配位化学研究所博士研究生毕业，获理学博士学位。同年被分配到同济大学化学系任教。1996年元月任同济大学化学系副教授，无机化学教研室主任。1997年被评为上海市优秀高校青年教师。1999年3月赴台湾中山大学访问研究，博士后研究员,从事有机金属无水无氧操作。2000年入选首批教育部高校骨干教师资助计划，从事功能配合物超分子组装研究。2000年3月获教育部国家重点实验室高级访问学者专项资助，赴南京大学配位化学国家重点实验室，从事杯芳烃超分子化学与模拟生物催化研究。2001年7月获日本学术振兴会资助，赴日本大阪药科大学，从事tau蛋白分子结构与AD病理及相关药物设计的研究，外国人特别研究员。2002年7月被评为同济大学化学系教授。2003年7月回国，同济大学大学化学系任教，教授，博士生导师。承担国家自然科学基金课题"Tau蛋白异常聚集的分子机制与Alzheimer病新药设计的化学基础"等项目的研究工作。在国内外主要刊物上发表的学术论文（只列10篇） 1．Koji Tomoo, Tian-Ming Yao et al, Possible Role of Each Repeat Structure of the Microtubule-Binding Domain of the Tau Protein in In Vitro Aggregation, J.Biochem., 2005, 138 ,413（通讯作者） 2． Tian-Ming Yao et al , Conformational Transition State Is Responsible for Assembly of Microtuble-binding Domain of Tau Protein，Biochemical Biophysical Research Communications, 2004, 315, 659（通讯作者，第二） 3． Tian-Ming Yao et al , Different Associational and Conformational Behavior between the Second and Third Repeat Fragments in Tau MBD，Eur.J.Biochem., 2004, 271,544.（通讯作者，第二） 4． Tian-Ming Yao et al , Aggregation Analysis of MBD Domain in Tau Protein by Spectroscopic Method,，J.Biochem., 2003, 134 ,91（通讯作者，第一） 5. Tian-Ming Yao et al , Supramolecular Interaction between Water-soluble Calix [4] arene and ATP，The Catalysis of Calix[4]arene for hydrolysis of ATP，Spect.Chem.Acta. A, 2002, 58, 3033（通讯作者，第一） 6. Tian-Ming Yao et al , Syntheses, characterization and non-linear optical properties of nickel complexes of multi-sulfur 1,2-dithiolene with strong near-IR absorption, J.Mater.Chem., 1996, 6, 1633.（第二） 7. Tian-Ming Yao et al , Syntheses, properties and crystal structures of a serieses of mixtures of dmit and dmise metal complexes, Polyhedron, 1996,15, 3547. （第二） 8. Tian-Ming Yao et al , Syntheses,crystal structure and properties of [Bu4N][Ni(pddt)2],, Polyhedron, 1995,14, 483. （第一） 9. Tian-Ming Yao et al , Syntheses and properties of the nickel complexes of the new 1,2-dithiolenes: MEDT and PHDT. The crystal structure of [Bu4N][Ni(MEDT)2], Polyhedron, 1995,14,1487.（第二） 10. Tian-Ming Yao et al , Preparation and properties of the [Pt(NN)(SS)] type complexes and their iodine-doped analogures, Tran.Met.Chem., 19,614,1994 （第一）
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6
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2006-08-07
姚天明， JING-LIN ZUO， TIAN-MING YAO， XIAO-ZENG YOU*， HOONG-KUN FUN， SIVAKUMAR KANDASAMY
，-0001，（）：
-1年11月30日
A series of mixtures of symmetric metal complexes of C3S22 and C3S4Se2 ligands (C3S22=1.3-dithiole-2-thione-4.5-dithiolate, DMIT; C3S4Se2=1.3-dithiole-2-selone-4-5-dithiolate，DMISE)，LBu4N]2[M(C3S4.4Seo.6)2](M=Ni,1; M-Cu, 2), [Bu4N] [Ni(C3S4.4Seo.6)2]，3，[Bu4N]2[Ni(C3S4.7Seo.3)2], 4, and[Bu4N][Ni(C3S4.7Se0.3)2], 5．have been prepared．Oxidation reactions of 1 with excess iodine afrorded the neutral complex [Ni(C3S4.4Seo.6)2]，6，which exhibited electrical conductivity of 0．29 S cm-1 at 25℃ for a compacted pellet. Single-crystal X-ray analysis of 1 revealed that the anion structure as a whole is planar．Both 3 and 5 form a one-dimensional arrangement through the inter-molecular sulfur-sulfur contacts．The S and Se at the terminal positions of the ligand are disordered．A single-crystal ESR study on[BuN1]2[Cu/Ni(C3S4.4SeO.6)2] demonstrated that the M-S coordination bond in the complex has a strong covalent o-bond character．
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2006-08-07
姚天明， Yao Tian-Ming a， b， Ye Zhi-Feng a， Wang Li a， Gu Jin-Ying a， Yao Si-De c， Shi Xian-Fa a， *
Spectrochimica Acta Part A 58(2002)3033-3038，-0001，（）：
-1年11月30日
The catalysis effect of water-soluble calix[4]arene C[4] (calix[4]arene-5,11,17,23-tetrasulfonate) on hydrolysis of ATP in aqueous solution was studied by HPLC. Using laser photolysis and pulse radiolysis, the supramolecular interaction between water-soluble calix[4]arene and ATP was investigated.
Supramolecular interaction， Calixarene， Hydrolysis of ATP， Laser photolysis， Pulse radiolysis
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2006-08-07
姚天明， Shuko Hiraoka， a Tian-Ming Yao， b Katsuhiko Minoura， a Koji Tomoo， a， * Miho Sumida， cTaizo Taniguchi， c， d and Toshimasa Ishidaa
Biochemical and Biophysical Research Communications 315(2004)659-663，-0001，（）：
-1年11月30日
In the brains of Alzheimer's disease patients, the tau protein dissociates from the axonal microtubule and abnormally aggregates to form a paired helical filament (PHF). One of the priorities in Alzheimer research is to clarify the mechanism of PHF formation. Although several reports on the regulation of tau assembly have been published, it is not yet clear whether in vivo PHFs are composed of b-structures or a-helices. Since the four-repeat microtubule-binding domain (4RMBD) of the tau protein has been considered to play an essential role in PHF formation, its heparin-induced assembly propensity was investigated by the thioflavin fluorescence method to clarify what conformation is most preferred for the assembly. We analyzed the assembly propensity of 4RMBD in Tris-HCl buffer with different trifluoroethanol (TFE) contents, because TFE reversibly induces the transition of the random structure to the a-helical structure in an aqueous solution. Consequently, it was observed that the 4RMBD assembly is most significantly favored to proceed in the 10-30% TFE solution, the concentration of which corresponds to the activated transition state of 4RMBD from a random structure to an a-helical structure, as determined from the circular dichroism (CD) spectral changes. Since such an assembly does not occur in a buffer containing TFE of<10% or>40%, the intermediate conformation between the random and a-helical structures could be most responsible for the PHF formation of 4RMBD. This is the first report to clarify that the non-native a-helical intermediate in transition from random coil is directly associated with filament formation at the start of PHF formation.
Tau protein， Microtubule-binding domain， Assembly， Conformational transition
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2006-06-21
姚天明， Koji Tomoo， *， Tian-Ming Yao， Katsuhiko Minoura， Shuko Hiraoka， Miho Sumida， Taizo Taniguchi and Toshimasa Ishida
J. Biochem. 138, 413～423 (2005)，-0001，（）：
-1年11月30日
Although one of the priorities in Alzheimer's research is to clarify the filament formation mechanism of the tau protein, it is currently unclearhowit is transformed from a normal structure in a neuron. To examine which part and what structural change in
aggregation,， fluorescence,， light scattering,， microtubule-binding domain,， repeat structure,， solution conformation,， tau protein.，
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2006-06-21
姚天明， Katsuhiko Minoura， Tian-Ming Yao， Koji Tomoo， Miho Sumida， Masahiro Sasaki， Taizo Taniguchi， and Toshimasa Ishida
Eur. J. Biochem. 271, 545～552 (2004)，-0001，（）：
-1年11月30日
The third repeat fragment (R3) in the four-repeat microtubule-binding domain of the water-soluble tau protein has been considered to play an essential role in the protein's filamentous assembly. To clarify the associational and conformational features tha
tau protein， microtubule-binding domain， repeated fragment， self-assembly， amphipathic structure.，
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2006-06-21
【期刊论文】Aggregation Analysis of the Microtubule Binding Domain in Tau Protein by Spectroscopic Methods
姚天明， Tian-Ming Yao*， ， Koji Tomoo*， Toshimasa Ishida， Hiroshi Hasegawa， Masahiro Sasaki and Taizo Taniguchi
Aggregation Analysis of Microtubule Binding Domain in Tau Vol. 134, No.1, 2003, 91～99，-0001，（）：
-1年11月30日
The microtubule-associated protein tau is a highly soluble protein that shows hardly any tendency to assemble under physiological conditions. In the brains of Alzheimer's disease (AD) patients, however, tau dissociates from the axonal microtubule and abno
aggregation,， tau protein,， spectroscopic analysis.，
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