Хайлтын үр дүнгүүд - Xuejun C. Zhang

Үр дүнг сайжруулах
  1. 1
    Energy coupling mechanisms of <scp>MFS</scp> transporters

    Energy coupling mechanisms of <scp>MFS</scp> transporters -н Xuejun C. Zhang, Yan Zhao, Jie Heng, Daohua Jiang

    Хэвлэсэн 2015
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    Revisão
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  2. 2
    Crystal structure of lipid phosphatase <i>Escherichia coli</i> phosphatidylglycerophosphate phosphatase B

    Crystal structure of lipid phosphatase <i>Escherichia coli</i> phosphatidylglycerophosphate phosphatase B -н Junping Fan, Daohua Jiang, Yan Zhao, Jianfeng Liu, Xuejun C. Zhang

    Хэвлэсэн 2014
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    Artigo
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  3. 3
    The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism

    The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism -н Xiaoqiang Wang, Chi-Sun Wang, Jordan Tang, Fred Dyda, Xuejun C. Zhang

    Хэвлэсэн 1997
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    Artigo
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  4. 4
    Crystal Structure of the E. coli Peptide Transporter YbgH

    Crystal Structure of the E. coli Peptide Transporter YbgH -н Yan Zhao, Guotao Mao, Min Liu, Laixing Zhang, Xianping Wang, Xuejun C. Zhang

    Хэвлэсэн 2014
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    Artigo
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  5. 5
    Structure of the nonameric bacterial amyloid secretion channel

    Structure of the nonameric bacterial amyloid secretion channel -н Baohua Cao, Yan Zhao, Yongjun Kou, Dongchun Ni, Xuejun C. Zhang, Yihua Huang

    Хэвлэсэн 2014
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    Artigo
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  6. 6
    Crystal structure of cytotoxin protein suilysin from Streptococcus suis

    Crystal structure of cytotoxin protein suilysin from Streptococcus suis -н Lingfeng Xu, Bo Huang, Huamao Du, Xuejun C. Zhang, Jianguo Xu, Xuemei Li, Zihe Rao

    Хэвлэсэн 2010
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    Artigo
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  7. 7
    Substrate-bound structure of the E. coli multidrug resistance transporter MdfA

    Substrate-bound structure of the E. coli multidrug resistance transporter MdfA -н Jie Heng, Yan Zhao, Ming Liu, Yue Liu, Junping Fan, Xianping Wang, Yongfang Zhao, Xuejun C. Zhang

    Хэвлэсэн 2015
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    Artigo
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  8. 8
    Crystallography of a Lewis-Binding Norovirus, Elucidation of Strain-Specificity to the Polymorphic Human Histo-Blood Group Antigens

    Crystallography of a Lewis-Binding Norovirus, Elucidation of Strain-Specificity to the Polymorphic Human Histo-Blood Group Antigens -н Yutao Chen, Ming Tan, Ming Xia, Ning Hao, Xuejun C. Zhang, Pengwei Huang, Xi Jiang, Xuemei Li, Zihe Rao

    Хэвлэсэн 2011
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    Artigo
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  9. 9
    Crystal structure of E. coli lipoprotein diacylglyceryl transferase

    Crystal structure of E. coli lipoprotein diacylglyceryl transferase -н Guotao Mao, Yan Zhao, Xusheng Kang, Zhijie Li, Yan Zhang, Xianping Wang, Fei Sun, Krishnan Sankaran, Xuejun C. Zhang

    Хэвлэсэн 2016
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    Artigo
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  10. 10
    Structure and mechanism of the human NHE1-CHP1 complex

    Structure and mechanism of the human NHE1-CHP1 complex -н Yanli Dong, Yiwei Gao, Alina Ilie, Dusik Kim, Annie Boucher, Bin Li, Xuejun C. Zhang, John Orlowski, Yan Zhao

    Хэвлэсэн 2021
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    Artigo
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  11. 11
    Structural Basis for the Recognition of Blood Group Trisaccharides by Norovirus

    Structural Basis for the Recognition of Blood Group Trisaccharides by Norovirus -н Sheng Cao, Zhiyong Lou, Ming Tan, Yutao Chen, Yijin Liu, Zhushan Zhang, Xuejun C. Zhang, Xi Jiang, Xuemei Li, Zihe Rao

    Хэвлэсэн 2007
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    Artigo
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  12. 12
    Bcl-2 and Bax Interact via the BH1–3 Groove-BH3 Motif Interface and a Novel Interface Involving the BH4 Motif

    Bcl-2 and Bax Interact via the BH1–3 Groove-BH3 Motif Interface and a Novel Interface Involving the BH4 Motif -н Jingzhen Ding, Zhi Zhang, G. Jane Roberts, Mina Falcone, Yiwei Miao, Yuanlong Shao, Xuejun C. Zhang, David W. Andrews, Jialing Lin

    Хэвлэсэн 2010
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    Artigo
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  13. 13
    Dodecamer Structure of Severe Acute Respiratory Syndrome Coronavirus Nonstructural Protein nsp10

    Dodecamer Structure of Severe Acute Respiratory Syndrome Coronavirus Nonstructural Protein nsp10 -н Dan Su, Zhiyong Lou, Fei Sun, Yujia Zhai, Haitao Yang, Rongguang Zhang, A. Joachimiak, Xuejun C. Zhang, Mark Bartlam, Zihe Rao

    Хэвлэсэн 2006
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    Artigo
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  14. 14
    Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5

    Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5 -н Guangyu Zhu, Jia Chen, Jay Liu, J.S. Brunzelle, Bo Huang, Nancy Wakeham, S. Terzyan, Xuemei Li, Zihe Rao, Guangpu Li, Xuejun C. Zhang

    Хэвлэсэн 2007
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    Artigo
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  15. 15
    New Antiviral Target Revealed by the Hexameric Structure of Mouse Hepatitis Virus Nonstructural Protein nsp15

    New Antiviral Target Revealed by the Hexameric Structure of Mouse Hepatitis Virus Nonstructural Protein nsp15 -н Xiaoling Xu, Yujia Zhai, Fei Sun, Zhiyong Lou, Dan Su, Yuanyuan Xu, Rongguang Zhang, A. Joachimiak, Xuejun C. Zhang, Mark Bartlam, Zihe Rao

    Хэвлэсэн 2006
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    Artigo
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  16. 16
    Structure of the YajR transporter suggests a transport mechanism based on the conserved motif A

    Structure of the YajR transporter suggests a transport mechanism based on the conserved motif A -н Daohua Jiang, Yan Zhao, Xianping Wang, Junping Fan, Jie Heng, Xuehui Liu, Wei Feng, Xusheng Kang, Bo Huang, Jianfeng Liu, Xuejun C. Zhang

    Хэвлэсэн 2013
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    Artigo
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  17. 17
    After Embedding in Membranes Antiapoptotic Bcl-XL Protein Binds Both Bcl-2 Homology Region 3 and Helix 1 of Proapoptotic Bax Protein to Inhibit Apoptotic Mitochondrial Permeabilization

    After Embedding in Membranes Antiapoptotic Bcl-XL Protein Binds Both Bcl-2 Homology Region 3 and Helix 1 of Proapoptotic Bax Protein to Inhibit Apoptotic Mitochondrial Permeabiliza... -н Jingzhen Ding, Blaine H. M. Mooers, Zhi Zhang, Justin Kale, Domina Falcone, Jamie Mcnichol, Bo Huang, Xuejun C. Zhang, Chengguo Xing, David W. Andrews, Jialing Lin

    Хэвлэсэн 2014
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    Artigo
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  18. 18
    Structure of human lanthionine synthetase C-like protein 1 and its interaction with Eps8 and glutathione

    Structure of human lanthionine synthetase C-like protein 1 and its interaction with Eps8 and glutathione -н Wenchi Zhang, Liang Wang, Yijin Liu, Ji-Wei Xu, Guangyu Zhu, Huaixing Cang, Xuemei Li, Mark Bartlam, Kenneth Hensley, Guangpu Li, Zihe Rao, Xuejun C. Zhang

    Хэвлэсэн 2009
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    Artigo
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  19. 19
    Closed-state inactivation and pore-blocker modulation mechanisms of human CaV2.2

    Closed-state inactivation and pore-blocker modulation mechanisms of human CaV2.2 -н Yanli Dong, Yiwei Gao, Shuai Xu, Yuhang Wang, Zhuoya Yu, Yue Li, Bin Li, Yuan Tian, Bei Yang, Xuejun C. Zhang, Daohua Jiang, Zhuo Huang, Yan Zhao

    Хэвлэсэн 2021
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    Artigo
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  20. 20
    Structural basis for modulation of human NaV1.3 by clinical drug and selective antagonist

    Structural basis for modulation of human NaV1.3 by clinical drug and selective antagonist -н Xiaojing Li, Feng Xu, Hao Xu, Shuli Zhang, Yiwei Gao, Hongwei Zhang, Yanli Dong, Yanchun Zheng, Bei Yang, Jianyuan Sun, Xuejun C. Zhang, Yan Zhao, Daohua Jiang

    Хэвлэсэн 2022
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    Artigo
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