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    Structural Studies of MAP Kinase Cascade Components

    MAPK cascade components have been the subject of structural analysis, advancing our understanding of how these enzymes are activated and how they interact. A surprising finding has been that unique inactive co...

    Elizabeth J. Goldsmith, **aoshan Min, Haixia He in MAP Kinase Signaling Protocols (2010)

  2. Article

    WNK1: analysis of protein kinase structure, downstream targets, and potential roles in hypertension

    The WNK kinases are a recently discovered family of serine-threonine kinases that have been shown to play an essential role in the regulation of electrolyte homeostasis. Intronic deletions in the WNK1 gene result...

    Bing-e XU, Byung-Hoon LEE, **aoshan MIN, Lisa LENERTZ, Charles J HEISE in Cell Research (2005)

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    Structure of MAPKs

    Mitogen-activated protein kinases (MAPKs) are protein-serine/threonine kinases activated by signaling pathways triggered by developmental stages, cell-surface receptors, cell stresses and other environmental c...

    Elizabeth J. Goldsmith, Melanie H. Cobb, Chung-I Chang in MAP Kinase Signaling Protocols (2004)

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    Article

    The structure of a Michaelis serpin–protease complex

    Serine protease inhibitors (serpins) regulate the activities of circulating proteases. Serpins inhibit proteases by acylating the serine hydroxyl at their active sites. Before deacylation and complete proteoly...

    Sheng Ye, Amy L. Cech, Ricardo Belmares, Robert C. Bergstrom in Nature Structural Biology (2001)

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    Article

    Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition

    Mutational studies of a serine proteinase inhibitor (serpin) reveal determinants of its structural rearrangements.

    H. Michael Tucker, James Mottonen, Elizabeth J. Goldsmith in Nature Structural Biology (1995)

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    Article

    Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution

    The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to a resolution of 2.3 A. The two domai...

    Faming Zhang, Arne Strand, David Robbins, Melanie H. Cobb, Elizabeth J. Goldsmith in Nature (1994)

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    Article

    Structural basis of latency in plasminogen activator inhibitor-1

    HUMAN plasminogen activator inhibitor-1 (PAI-1)1,2 is the fast-acting inhibitor of tissue plasminogen activator and urokinase3 and is a member of the serpin family of protease inhibitors4. Serpins normally form c...

    James Mottonen, Arne Strand, **drich Symersky, Robert M. Sweet, Dennis E. Danley in Nature (1992)

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    Article

    Serpin-resistant mutants of human tissue-type plasminogen activator

    TISSUE-type plasminogen activator (t-PA) converts the inactive zymogen, plasminogen, into the powerful protease, plasmin, which then degrades the fibrin meshwork of thrombi1–3. To prevent systemic activation of p...

    Edwin L. Madison, Elizabeth J. Goldsmith, Robert D. Gerard, Mary-Jane H. Gething in Nature (1989)