Результаты поиска - Wei‐Jen Tang

Отмена результатов
  1. 1
    Targeting Insulin-Degrading Enzyme to Treat Type 2 Diabetes Mellitus

    Targeting Insulin-Degrading Enzyme to Treat Type 2 Diabetes Mellitus по Wei‐Jen Tang

    Опубликовано 2015
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  2. 2
    The adenylyl cyclase activity of anthrax edema factor

    The adenylyl cyclase activity of anthrax edema factor по Wei‐Jen Tang, Qing Guo

    Опубликовано 2009
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  3. 3
    Expression and characterization of calmodulin-activated (type I) adenylylcyclase

    Expression and characterization of calmodulin-activated (type I) adenylylcyclase по Wei‐Jen Tang, Jerzy Krupiński, Alfred G. Gilman

    Опубликовано 1991
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    Artigo
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  4. 4
    Amyloid β-degrading cryptidases: insulin degrading enzyme, presequence peptidase, and neprilysin

    Amyloid β-degrading cryptidases: insulin degrading enzyme, presequence peptidase, and neprilysin по E. Malito, Raymond E. Hulse, Wei‐Jen Tang

    Опубликовано 2008
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  5. 5
    Two Cytoplasmic Domains of Mammalian Adenylyl Cyclase Form a GSα- and Forskolin-activated Enzyme in Vitro

    Two Cytoplasmic Domains of Mammalian Adenylyl Cyclase Form a GSα- and Forskolin-activated Enzyme in Vitro по Shui-Zhong Yan, David Hahn, Zhihui Huang, Wei‐Jen Tang

    Опубликовано 1996
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    Artigo
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  6. 6
    Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism

    Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism по Yuequan Shen, A. Joachimiak, Marsha Rich Rosner, Wei‐Jen Tang

    Опубликовано 2006
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    Artigo
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  7. 7
    Distinct patterns of bidirectional regulation of mammalian adenylyl cyclases.

    Distinct patterns of bidirectional regulation of mammalian adenylyl cyclases. по Ronald Taussig, Wei‐Jen Tang, John R. Hepler, Alfred G. Gilman

    Опубликовано 1994
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    Artigo
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  8. 8
    Structure of the dynein-1 outer arm in sea urchin sperm flagella. I. Analysis by separation of subunits.

    Structure of the dynein-1 outer arm in sea urchin sperm flagella. I. Analysis by separation of subunits. по Wei‐Jen Tang, Christopher W. Bell, Winfield S. Sale, I. R. Gibbons

    Опубликовано 1982
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  9. 9
    Molecular Basis for the Recognition and Cleavages of IGF-II, TGF-α, and Amylin by Human Insulin-Degrading Enzyme

    Molecular Basis for the Recognition and Cleavages of IGF-II, TGF-α, and Amylin by Human Insulin-Degrading Enzyme по Qing Guo, Marika Manolopoulou, Yao Bian, Alexander Schilling, Wei‐Jen Tang

    Опубликовано 2009
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    Artigo
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  10. 10
    Molecular Basis of Catalytic Chamber-assisted Unfolding and Cleavage of Human Insulin by Human Insulin-degrading Enzyme

    Molecular Basis of Catalytic Chamber-assisted Unfolding and Cleavage of Human Insulin by Human Insulin-degrading Enzyme по Marika Manolopoulou, Qing Guo, E. Malito, Alexander Schilling, Wei‐Jen Tang

    Опубликовано 2009
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    Artigo
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  11. 11
    Calcium-independent calmodulin binding and two-metal–ion catalytic mechanism of anthrax edema factor

    Calcium-independent calmodulin binding and two-metal–ion catalytic mechanism of anthrax edema factor по Yuequan Shen, Natalia L. Zhukovskaya, Qing Guo, Jan Florián, Wei‐Jen Tang

    Опубликовано 2005
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    Artigo
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  12. 12
    Phylogeny and expression of axonemal and cytoplasmic dynein genes in sea urchins.

    Phylogeny and expression of axonemal and cytoplasmic dynein genes in sea urchins. по Barbara Gibbons, David J. Asai, Wei‐Jen Tang, T S Hays, I. R. Gibbons

    Опубликовано 1994
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    Artigo
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  13. 13
    Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin

    Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin по Qing Guo, Yuequan Shen, Young-Sam Lee, Craig S. Gibbs, Milan Mrksich, Wei‐Jen Tang

    Опубликовано 2005
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    Artigo
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  14. 14
    Degradation of Alzheimer’s Amyloid-β by a Catalytically Inactive Insulin-Degrading Enzyme

    Degradation of Alzheimer’s Amyloid-β by a Catalytically Inactive Insulin-Degrading Enzyme по Bikash R. Sahoo, Pritam Kumar Panda, Wenguang Liang, Wei‐Jen Tang, Rajeev Ahuja, Ayyalusamy Ramamoorthy

    Опубликовано 2021
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    Artigo
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  15. 15
    Photosensitized cleavage of dynein heavy chains. Cleavage at the V2 site by irradiation at 365 NM in the presence of oligovanadate.

    Photosensitized cleavage of dynein heavy chains. Cleavage at the V2 site by irradiation at 365 NM in the presence of oligovanadate. по I. R. Gibbons, A. Lee-Eiford, Gábor Mócz, C. A. Phillipson, Wei‐Jen Tang, Barbara Gibbons

    Опубликовано 1987
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    Artigo
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  16. 16
    Molecular Bases for the Recognition of Short Peptide Substrates and Cysteine-Directed Modifications of Human Insulin-Degrading Enzyme

    Molecular Bases for the Recognition of Short Peptide Substrates and Cysteine-Directed Modifications of Human Insulin-Degrading Enzyme по E. Malito, Luis A. Ralat, Marika Manolopoulou, Julie L. Tsay, Natasha L. Wadlington, Wei‐Jen Tang

    Опубликовано 2008
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    Artigo
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  17. 17
    Anthrax Edema Toxin Inhibits Endothelial Cell Chemotaxis via Epac and Rap1

    Anthrax Edema Toxin Inhibits Endothelial Cell Chemotaxis via Epac and Rap1 по Jia Hong, Robert C. Doebele, Mark W. Lingen, Lawrence A. Quilliam, Wei‐Jen Tang, Marsha Rich Rosner

    Опубликовано 2007
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    Artigo
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  18. 18
    Molecular Basis of Substrate Recognition and Degradation by Human Presequence Protease

    Molecular Basis of Substrate Recognition and Degradation by Human Presequence Protease по John V. Lin King, Wenguang Liang, Kathryn P. Scherpelz, Alexander Schilling, Stephen C. Meredith, Wei‐Jen Tang

    Опубликовано 2014
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    Artigo
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  19. 19
    Insulin-degrading Enzyme Modulates the Natriuretic Peptide-mediated Signaling Response

    Insulin-degrading Enzyme Modulates the Natriuretic Peptide-mediated Signaling Response по Luis A. Ralat, Qing Guo, Min Ren, T. Funke, Deborah M. Dickey, Lincoln R. Potter, Wei‐Jen Tang

    Опубликовано 2010
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  20. 20
    Antiinflammatory cAMP signaling and cell migration genes co-opted by the anthrax bacillus

    Antiinflammatory cAMP signaling and cell migration genes co-opted by the anthrax bacillus по Chun Kim, Sarah A. Wilcox‐Adelman, Yasuyo Sano, Wei‐Jen Tang, R. John Collier, Jin Mo Park

    Опубликовано 2008
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