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| 1 | L_-glutamine provides acid resistance for Escherichia coil through enzymatic release of ammonia显示文摘 | Peilon Lu | 2013 | Cell Research2013，23，5： | 23 |
| 2 | Crystal structure and biochemical analyses reveal Beclin 1 as a novel membrane binding protein显示文摘Beclin 1 基因是 haplo 不够的肿瘤 suppressor 并且在 autophagy 起一个必要作用。然而, Beclin 1 由工作的分子的机制仍然保持大部分未知。这里,我们在 1.6 Å 报导 Beclin 1 的 evolutionarily 保存的领域(ECD ) 的水晶结构;分辨率。Beclin 1 ECD 展览一以前 unreported 褶层,与在中央轴附近相称性地安排的三次结构的重复。Beclin 1 ECD 定义膜绑定领域的一个新奇的类,与为与 cardiolipin 充实的类脂化合物膜的强壮的偏爱。在 Beclin 1 ECD 的一个表面环的尖端,包括三芳香的氨基酸,与类脂化合物膜充当一根恐水病的手指到伙伴,因而导致膜和 liposomes 的变丑。这些芳香的残余的变化使 Beclin 1 变为不能稳定地在 vitro 与类脂化合物膜联系并且不能充分在 vivo 在 Beclin 1-knockdown 房间救 autophagy。这些观察为译解形成一个重要框架 Beclin 1 的生物功能。 | Weljlao Huang Wooyoung Chol Wanqiu Hu Na Mi Qiang Guo Meisheng Ma Mei Liu Yuan Tian Peilong Lu Feng-Liang Wang Haiteng Deng Lei Liu Ning Gao Li Yu Yigong Shi | 2012 | Cell Research2012，22，3： | 21 |
| 3 | Apoptosome and inflammasome: conserved machineries for caspase activation显示文摘Apoptosome and inlammasome are multimeric protein complexes that mediate the activation of speciic caspases at the onset of apoptosis and inlammation.he central component of apoptosome or inlammasome is a tripartite scafold protein,exempliied by Apaf-1 and NLRC4,which contains an amino-terminal homotypic interaction motif,a central nucleotide-binding oligomerization domain and a carboxyl-terminal ligand-sensing domain.In the absence of death cue or an inlammatory signal,Apaf-1 or NLRC4 exists in an auto-inhibited,monomeric state,which is stabilized by adenosine diphosphate(ADP).Binding to an apoptosis-or inlammation-inducing ligand,together with replacement of ADP by adenosine triphosphate(ATP),results in the formation of a multimeric apoptosome or inlammasome.he assembled apoptosome and inlammasome serve as dedicated machineries to facilitate the activation of speciic caspases.In this review,we describe the structure and functional mechanisms of mammalian inlammasome and apoptosomes from three representative organisms.Emphasis is placed on the molecular mechanism of caspase activation and the shared features of apoptosomes and inlammasomes. | Jijie Chai Yigong Shi | 2014 | National Science Review2014，1，1： | 6 |
| 4 | Mechanisms of TGF-β Signaling from Cell Membrane to the Nucleus显示文摘 | Yigong Shi Joan Massagué | 2003 | Cell2003，，6： | 5 |
| 5 | 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 |
| 6 | Molecular architecture of the luminal ring of the Xenopus laevis nuclear pore complex显示文摘The nuclear pore complex(NPC)mediates the flow of substances between the nucleus and cytoplasm in eukaryotic cells.Here we report the cryo-electron tomography(cryo-ET)structure of the luminal ring(LR)of the NPC from Xenopus laevis oocyte.The observed key structural features of the LR are independently confirmed by single-particle cryo-electron microscopy(cryo-EM)analysis.The LR comprises eight butterfly-shaped subunits,each containing two symmetric wings.Each wing consists of four elongated,tubular protomers.Within the LR subunit,the eight protomers form a Finger domain,which directly contacts the fusion between the inner and outer nuclear membranes and a Grid domain,which serves as a rigid base for the Finger domain.Two neighboring LR subunits interact with each other through the lateral edges of their wings to constitute a Bumper domain,which displays two major conformations and appears to cushion neighboring NPCs.Our study reveals previously unknown features of the LR and potentially explains the elastic property of the NPC. | Yanqing Zhang Sai Li Chao Zeng Gaoxingyu Huang Xuechen Zhu Qifan Wang Kunpeng Wang Qiang Zhou Chuangye Yan Wusheng Zhang Guangwen Yang Minhao Liu Qinghua Tao Jianlin Lei Yigong Shi | 2020 | Cell Research2020，30，6： | 4 |
| 7 | 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 |
| 8 | Mechanisms of TGF-β Signaling from Cell Membrane to the Nucleus显示文摘 | Yigong Shi Joan Massagué | 2003 | Cell2003，，6： | 4 |
| 9 | Functional characterization of humar equilibrative nucleoside transporter 1显示文摘 | Weiyun Huang Xin Zeng Yigong Shi Minhao Liu | 2017 | Protein & Cell2017，8，4： | 3 |
| 10 | Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex by cryo-electron microscopy single particle analysis显示文摘The nuclear pore complex(NPC)exhibits structural plasticity and has only been characterized at local resolutions of up to 15 A for the cytoplasmic ring(CR).Here we present a single-particle cryo-electron microscopy(cryo-EM)structure of the CR from Xenopus laevis NPC at average resolutions of 5.5-7.9A,with local resolutions reaching 4.5 A.Improved resolutions allow identification and placement of secondary structural elements in the majority of the CR components.The two Y complexes in each CR subunit interact with each other and associate with those from flanking subunits,forming a circular scaffold.Within each CR subunit,the Nup358-containing region wraps around the stems of both Y complexes,likely stabilizing the scaffold.Nup205 connects the short arms of the two Y complexes and associates with the stem of a neighboring Y complex.The Nup214-containing region uses an extended coiled-coil to link Nup85 of the two Y complexes and protrudes into the axial pore of the NPC.These previously uncharacterized structural features reveal insights into NPC assembly. | Gaoxingyu Huang Yanqing Zhang Xuechen Zhu Chao Zeng Qifan Wang Qiang Zhou Qinghua Tao Minhao Liu Jianlin Lei Chuangye Yan Yigong Shi | 2020 | Cell Research2020，30，6： | 2 |
| 11 | 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 |
| 12 | Mechanisms of TGF-β Signaling from Cell Membrane to the Nucleus显示文摘 | Yigong Shi Joan Massagué | 2003 | Cell2003，，6： | 1 |
| 13 | Serine/threonine phosphatases:mechanism through structure显示文摘 | Yigong Shi | 2009 | Cell2009，139，： | 1 |
| 14 | China Research Culture 显示文摘 | Yigong Shi Yi Rao | 2010 | Science2010，329，5996： | 1 |
| 15 | A structural view of mitochondria-mediated apoptosis显示文摘 | Yigong Shi | 2001 | Nature Struct Biol2001，18，： | 1 |
| 16 | Caspase Activation显示文摘 | Yigong Shi | 2004 | Cell2004，，7： | 1 |
| 17 | Mechertisms of caspase activation and inhibition during apoptosis显示文摘 | Yigong Shi | 2002 | Mol Cell2002，9，： | 1 |
| 18 | The galvsnization of biology a growing appreciation for the roles of Zine显示文摘 | JEREMY M BERG YIGONG SHI | 1996 | Science1996，，271： | 1 |
| 19 | A structural basis for mutational inactivation of the tumour suppressor Smad4 显示文摘 | Shi Yigong Hata A Lo RS | 1997 | Nature1997，388，6637： | 1 |
| 20 | Structure of a Protein Phosphatase 2A Holoenzyme: Insights into B55-Mediated Tau Dephosphorylation显示文摘 | Yanhui Xu Yu Chen Ping Zhang Philip D. Jeffrey Yigong Shi | 2008 | Molecular Cell2008，，6： | 1 |
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