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| 1 | Structure of the human activated spliceosome in three conformational states显示文摘在拼接的 pre-mRNA 的每个周期期间, pre 催化的 spliceosome (B 建筑群) 被变换成激活的 spliceosome (B 行为 建筑群) ,它有一个合法活跃地点但是不能继续到分叉的反应。这里,我们在场人的 B 处于三个不同 conformational 状态的行为 建筑群。他们地图允许将近所有的原子建模 U2 小原子 ribonucleoprotein (snRNP ) 的蛋白质部件,包括三 SF3a 建筑群和七 SF3b 建筑群。人的 B 行为 建筑群包含 52 蛋白质, U2, U5,和 U6 小原子 RNA (snRNA ) ,和 pre-mRNA。三不同符合构造被捕获了,代表人的 B 行为 建筑群。这些建筑群在开关环的取向不同 Prp8,拼接的因素 RNF113A 和 NY-CO-10,和十九建筑群(NTC ) 和 NTC 相关的建筑群的大多数部件。有 B 和 C 建筑群的这三建筑群和比较的分析在 B-to-B 行为 和 B 行为 -to-B* 转移,它最终为分叉的反应告知活跃地点。 | Xiaofeng Zhang, Chuangye Yan, Xiechao Zhan, Lijia Li, Jianlin Lei, Yigong Shi Jianlin Lei Yigong Shi | 2018 | Cell Research2018，28，3： | 4 |
| 2 | Structures of the human pre-catalytic spliceosome and its precursor spliceosome显示文摘The pre-catalytic spliceosome (B complex) is preceded by its precursor spliceosome (pre-B complex) and followed by the activated spliceosome (Bact complex). The pre-B-to-B and B-to-Bact transitions are driven by the ATPase/helicases Prp28 and Brr2,respectively. In this study,we report the cryo-electron microscopy structures of the human pre-B complex and the human B complex at an average resolution of 5.7 and 3.8 A,respectively. In the pre-B complex,U1 and U2 small nuclear ribonucleoproteins (snRNPs) associate with two edges of the tetrahedron-shaped U4/U6.U5 tri-snRNP. The pre-mRNA is yet to be recognized by U5 or U6 small nuclear RNA (snRNA),and loop I of U5 snRNA remains unengaged. In the B complex,U1 snRNP and Prp28 are dissociated,the 5’-exon is anchored to loop I of U5 snRNA,and the 5’-splice site is recognized by U6 snRNA through duplex formation. In sharp contrast to S. cerevisiae,most components of U2 snRNP and tri-snRNP,exemplified by Brr2,undergo pronounced rearrangements in the human pre-B-to-B transition. Structural analysis reveals mechanistic insights into the assembly and activation of the human spliceosome. | Xiechao Zhan Chuangye Yan Xiaofeng Zhang Jianlin Lei Yigong Shi | 2018 | Cell Research2018，28，12： | 4 |
| 3 | Properties of TiO_2-SiO_2 Mixed Oxides and Photocatalytic Oxidation of Heptane and Sulfur Dioxide显示文摘A series of TiO 2-XSiO 2[X denotes the molar fraction(%) of silica in the mixed oxides] with different \{n(Ti)\}/n(Si) ratios was prepared with ammonia water as a hydrolysis catalyst. The photocatalysts prepared were characterized by XRD, thermal analysis, FTIR, UV-Vis and SPS. The characterization results of FTIR and UV-Vis spectra show that Ti atoms were gradually changed from octahedral coordination to tetrahedral coordination with the addition of silica, which is not beneficial for obtaining strong Brnsted acidity and higher photocatalytic activity. The photocatalytic activity experiments, which were conducted by using heptane(or SO 2) as the model reactant, showed that TiO 2-SiO 2 containing a suitable amount of silica can exhibit much higher photocatalytic activity than pure TiO 2. The enhanced photocatalytic activity can be attributed to three following factors: (1) smaller crystalline size; (2) higher thermal stability; (3) the new strong Brnsted acidity. | XIEChao XUZi-li YANGQiu-jing LINa WANGDe-bao DUYao-guo | 2005 | Chemical Research in Chinese Universities2005，21，1： | 3 |
| 4 | Cryo-EM structure of the inner ring from the Xenopus laevis nuclear pore complex显示文摘Nuclear pore complex(NPC)mediates nucleocytoplasmic shuttling.Here we present single-particle cryo-electron microscopy structure of the inner ring(IR)subunit from the Xenopus laevis NPC at an average resolution of 4.2Å.A homo-dimer of Nup205 resides at the center of the IR subunit,flanked by two molecules of Nup188.Four molecules of Nup93 each places an extended helix into the axial groove of Nup205 or Nup188,together constituting the central scaffold.The channel nucleoporin hetero-trimer of Nup62/58/54 is anchored on the central scaffold.Six Nup155 molecules interact with the central scaffold and together with the NDC1–ALADIN hetero-dimers anchor the IR subunit to the nuclear envelope and to outer rings.The scarce inter-subunit contacts may allow sufficient latitude in conformation and diameter of the IR.Our structure reveals the molecular basis for the IR subunit assembly of a vertebrate NPC. | Gaoxingyu Huang Xiechao Zhan Chao Zeng Ke Liang Xuechen Zhu Yanyu Zhao Pan Wang Qifan Wang Qiang Zhou Qinghua Tao Minhao Liu Jianlin Lei Chuangye Yan Yigong Shi | 2022 | Cell Research2022，32，5： | 1 |
| 5 | Computer simulation of unsymmetry of the melt-spinning hollow fiber 显示文摘 | Wang Huaping Yu Xiaowei Hu Xiechao | 1999 | J China Text Univ1999，16，2： | 1 |
| 6 | Cryo-EM structure of the nuclear ring from Xenopus laevis nuclear pore complex显示文摘Nuclear pore complex(NPC)shuttles cargo across the nuclear envelope.Here we present single-particle cryo-EM structure of the nuclear ring(NR)sub unit from Xenopus laevis NPC at an average resoluti on of 5.6 A.The NR sub unit comprises two 10-membered Y complexes,each with the nucleoporin ELYS closely associating with Nup160 and Nup37 of the long arm.Unlike the cytoplasmic ring(CR)or inner ring(IR),the NR sub unit contains only one molecule each of Nup205 and Nup93.Nup205 binds both arms of the Y complexes and in teracts with the stem of inner Y complex from the n eighboring subunit.Nup93 conn ects the stems of inner and outer Y complexes within the same NR sub unit,and places its N-terminal extended helix i nto the axial groove of Nup205 from the n eighboring subunit.Together with other structural in formation,we have gen erated a composite atomic model of the cen tral ring scaffold that includes the NR,IR,and CR.The IR is connected to the two outer rings mainly through Nup155.This model facilitates functional understanding of vertebrate NPC. | Gaoxingyu Huang Xiechao Zhan Chao Zeng Xuechen Zhu Ke Liang Yanyu Zhao Pan Wang | 2022 | Cell Research2022，32，4： | 1 |
| 7 | CNVseq,anewmethodtodetectcopynumbervariationusinghighthroughputsequencing显示文摘 | XIEChao TAMMIM T | 2009 | BMCBioinformatics2009，10，： | 1 |
| 8 | 显示文摘 | XIEChao MAILian-dao DUZhi-hui etal(谢超 麦联叨 都志辉 等) | | 计算机工程与应用0，，： | 1 |
| 9 | Inducing dopaminergic differentiation of expanded rat mesencephalic neural stem cells by ascorbic acid in vitro显示文摘Ascorbic acid (AA) induced differentiation of neural stem cells (NSCs) into dopaminergic (DAergic) neurons is reported. NSCs derived from rat mesencephalon were maintained and expanded in a defined medium containing mitogens of basic fibroblast growth factor (bFGF) and epidermal growth factor (EGF). Compared with the control, ascorbic acid treatment led to more DAergic neuronal differentiation as indicated by the expression of tyrosine hydroxylase (TH) and dopamine transporter (DAT), which are specific markers of dopamine neurons. AA induction also enhanced expression of Nurr1 and Shh. PD98059, an inhibitor of mitogen activated protein kinase/extracellular signal regulated kinase (MAPK/ERK) pathway, could block AA induced Nurr1, TH and DAT mRNA expression. The results might suggest a new strategy to provide enough dopaminergic cells for the therapy of Parkinson’s disease (PD), and Nurr1 and ERK signaling pathway might participate in the AA induced DAergic differentiation. | ZHENGMin WANGDongmei HOULingling LIHaimin XIEChao JIAOWencang BAICixian WANGYaping PEIXuetao | 2004 | Progress in Natural Science:Materials International2004，14，1： | 0 |
| 10 | Structures of the human spliceosomes before and after release of the ligated exon显示文摘Pre-mRNA splicing is executed by the spliceosome,which has eight major functional states each with distinct composition.Five of these eight human spliceosomal complexes,all preceding exon ligation,have been structurally characterized.In this study,we report the cryo-electron microscopy structures of the human post-catalytic spliceosome(P complex)and intron lariat spliceosome(ILS)at average resolutions of 3.0 and 2.9??,respectively.In the P complex,the ligated exon remains anchored to loop I of U5 small nuclear RNA,and the 3′-splice site is recognized by the junction between the 5′-splice site and the branch point sequence.The ATPase/helicase Prp22,along with the ligated exon and eight other proteins,are dissociated in the P-to-ILS transition.Intriguingly,the ILS complex exists in two distinct conformations,one with the ATPase/helicase Prp43 and one without.Comparison of these three late-stage human spliceosomes reveals mechanistic insights into exon release and spliceosome disassembly. | Xiaofeng Zhang Xiechao Zhan Chuangye Yan Wenyu Zhang Dongliang Liu Jianlin Lei Yigong Shi | 2019 | Cell Research2019，29，4： | 0 |
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