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  1. Article ; Online: VEXAS Syndrome and Thrombosis: Findings of Inflammation, Hypercoagulability, and Endothelial Dysfunction.

    Fan, Bingwen E / Sum, Christina L L / Leung, Bernard P L / Ang, Mui K / Lim, Xin R / Lee, Samuel S M / Koh, Li W / Goh, Liuh L / Chan, Wee L / Wang, Liang D / Wong, Siu L / Tay, Sen H

    Seminars in thrombosis and hemostasis

    2024  

    Language English
    Publishing date 2024-01-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 196901-8
    ISSN 1098-9064 ; 0094-6176
    ISSN (online) 1098-9064
    ISSN 0094-6176
    DOI 10.1055/s-0043-1778105
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: VEXAS Syndrome and Thrombosis: Findings of Inflammation, Hypercoagulability, and Endothelial Dysfunction

    Fan, Bingwen E. / Sum, Christina L.L. / Leung, Bernard P.L. / Ang, Mui K. / Lim, Xin R. / Lee, Samuel S.M. / Koh, Li W. / Goh, Liuh L. / Chan, Wee L. / Wang, Liang D. / Wong, Siu L. / Tay, Sen H.

    Seminars in Thrombosis and Hemostasis

    (Recent advances in Thrombosis and Hemostasis - Part X)

    2024  

    Series title Recent advances in Thrombosis and Hemostasis - Part X
    Language English
    Publishing date 2024-01-05
    Publisher Thieme Medical Publishers, Inc.
    Publishing place Stuttgart ; New York
    Document type Article
    ZDB-ID 196901-8
    ISSN 1098-9064 ; 0094-6176
    ISSN (online) 1098-9064
    ISSN 0094-6176
    DOI 10.1055/s-0043-1778105
    Database Thieme publisher's database

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  3. Article ; Online: An in cellulo-derived structure of PAK4 in complex with its inhibitor Inka1.

    Baskaran, Yohendran / Ang, Khay C / Anekal, Praju V / Chan, Wee L / Grimes, Jonathan M / Manser, Ed / Robinson, Robert C

    Nature communications

    2015  Volume 6, Page(s) 8681

    Abstract: PAK4 is a metazoan-specific kinase acting downstream of Cdc42. Here we describe the structure of human PAK4 in complex with Inka1, a potent endogenous kinase inhibitor. Using single mammalian cells containing crystals 50 μm in length, we have determined ... ...

    Abstract PAK4 is a metazoan-specific kinase acting downstream of Cdc42. Here we describe the structure of human PAK4 in complex with Inka1, a potent endogenous kinase inhibitor. Using single mammalian cells containing crystals 50 μm in length, we have determined the in cellulo crystal structure at 2.95 Å resolution, which reveals the details of how the PAK4 catalytic domain binds cellular ATP and the Inka1 inhibitor. The crystal lattice consists only of PAK4-PAK4 contacts, which form a hexagonal array with channels of 80 Å in diameter that run the length of the crystal. The crystal accommodates a variety of other proteins when fused to the kinase inhibitor. Inka1-GFP was used to monitor the process crystal formation in living cells. Similar derivatives of Inka1 will allow us to study the effects of PAK4 inhibition in cells and model organisms, to allow better validation of therapeutic agents targeting PAK4.
    MeSH term(s) Adenosine Triphosphate ; Animals ; COS Cells ; Catalytic Domain ; Cell Line, Tumor ; Chlorocebus aethiops ; Crystallization ; Crystallography, X-Ray ; Escherichia coli ; HEK293 Cells ; HeLa Cells ; Humans ; Immunoprecipitation ; In Vitro Techniques ; Intracellular Signaling Peptides and Proteins/chemistry ; Intracellular Signaling Peptides and Proteins/metabolism ; Microscopy, Confocal ; Protein Binding ; Protein Structure, Tertiary ; p21-Activated Kinases/chemistry ; p21-Activated Kinases/metabolism
    Chemical Substances Inka1 protein, human ; Intracellular Signaling Peptides and Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; PAK4 protein, human (EC 2.7.1.11) ; p21-Activated Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2015-11-26
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/ncomms9681
    Database MEDical Literature Analysis and Retrieval System OnLINE

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