Search Results - "Amann, Kurt J."

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  1. 1

    The Structural Basis of Actin Filament Branching by the Arp2/3 Complex by Rouiller, Isabelle, Xu, Xiao-Ping, Amann, Kurt J., Egile, Coumaran, Nickell, Stephan, Nicastro, Daniela, Li, Rong, Pollard, Thomas D., Volkmann, Niels, Hanein, Dorit

    Published in The Journal of cell biology (10-03-2008)
    “…The actin-related protein 2/3 (Arp2/3) complex mediates the formation of branched actin filaments at the leading edge of motile cells and in the comet tails…”
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  2. 2

    Direct Real-Time Observation of Actin Filament Branching Mediated by Arp2/3 Complex Using Total Internal Reflection Fluorescence Microscopy by Amann, Kurt J., Pollard, Thomas D.

    “…Existing methods for studying actin filament dynamics have allowed analysis only of bulk samples or individual filaments after treatment with the drug…”
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  3. 3

    Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins by Pollard, Thomas D, Blanchoin, Laurent, Amann, Kurt J, Higgs, Henry N, Marchand, Jean-Baptiste, Kaiser, Donald A

    Published in Nature (London) (27-04-2000)
    “…Most nucleated cells crawl about by extending a pseudopod that is driven by the polymerization of actin filaments in the cytoplasm behind the leading edge of…”
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  4. 4

    The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments by Pollard, Thomas D, Amann, Kurt J

    Published in Nature cell biology (01-03-2001)
    “…Regulated assembly of actin-filament networks provides the mechanical force that pushes forward the leading edge of motile eukaryotic cells and intracellular…”
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  5. 5

    EPLIN Regulates Actin Dynamics by Cross-Linking and Stabilizing Filaments by Maul, Raymond S., Song, Yuhong, Amann, Kurt J., Gerbin, Sachi C., Pollard, Thomas D., Chang, David D.

    Published in The Journal of cell biology (03-02-2003)
    “…Epithelial protein lost in neoplasm (EPLIN) is a cytoskeleton-associated protein encoded by a gene that is down-regulated in transformed cells. EPLIN increases…”
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  6. 6

    Structure of Arp2/3 Complex in Its Activated State and in Actin Filament Branch Junctions by Volkmann, Niels, Amann, Kurt J., Stoilova-McPhie, Svetla, Egile, Coumaran, Winter, Dirk C., Hazelwood, Larnele, Heuser, John E., Li, Rong, Pollard, Thomas D., Hanein, Dorit

    “…The seven-subunit Arp2/3 complex choreographs the formation of branched actin networks at the leading edge of migrating cells. When activated by…”
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  7. 7

    Polymerization Properties of the Thermotoga maritima Actin MreB:  Roles of Temperature, Nucleotides, and Ions by Bean, Greg J, Amann, Kurt J

    Published in Biochemistry (Easton) (15-01-2008)
    “…MreB is a bacterial orthologue of actin that affects cell shape, polarity, and chromosome segregation. Although a significant body of work has explored its…”
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  8. 8

    Proteolysis of cortactin by calpain regulates membrane protrusion during cell migration by Perrin, Benjamin J, Amann, Kurt J, Huttenlocher, Anna

    Published in Molecular biology of the cell (01-01-2006)
    “…Calpain 2 regulates membrane protrusion during cell migration. However, relevant substrates that mediate the effects of calpain on protrusion have not been…”
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    Journal Article
  9. 9

    A Cluster of Basic Repeats in the Dystrophin Rod Domain Binds F-actin through an Electrostatic Interaction by Amann, Kurt J., Renley, Brian A., Ervasti, James M.

    Published in The Journal of biological chemistry (23-10-1998)
    “…The dystrophin rod domain is composed of 24 spectrin-like repeats and was thought to act mainly as a flexible spacer between the amino-terminal actin binding…”
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  10. 10

    A New Model for the Interaction of Dystrophin with F-Actin by Rybakova, Inna N., Amann, Kurt J., Ervasti, James M.

    Published in The Journal of cell biology (01-11-1996)
    “…The F-actin binding and cross-linking properties of skeletal muscle dystrophin-glycoprotein complex were examined using high and low speed cosedimentation…”
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  11. 11

    Assembly properties of the Bacillus subtilis actin, MreB by Mayer, Joshua A., Amann, Kurt J.

    Published in Cell motility and the cytoskeleton (01-02-2009)
    “…The bacterial actin MreB has been implicated in a variety of cellular roles including cell shape determination, cell wall synthesis, chromosome condensation…”
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  12. 12

    Utrophin Lacks the Rod Domain Actin Binding Activity of Dystrophin by Amann, K J, Guo, A W, Ervasti, J M

    Published in The Journal of biological chemistry (10-12-1999)
    “…We previously identified a cluster of basic spectrin-like repeats in the dystrophin rod domain that binds F-actin through electrostatic interactions (Amann, K…”
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  13. 13

    Polymerization Properties of the Thermotoga maritima Actin MreB: Roles of Temperature, Nucleotides, and Ions by Bean, Greg J, Amann, Kurt J

    Published in Biochemistry (Easton) (01-01-2008)
    “…MreB is a bacterial orthologue of actin that affects cell shape, polarity, and chromosome segregation. Although a significant body of work has explored its…”
    Get full text
    Journal Article
  14. 14

    POLYMERIZATION PROPERTIES OF THE T. MARITIMA ACTIN, MreB: ROLES OF TEMPERATURE, NUCLEOTIDES AND IONS by Bean, Greg J., Amann, Kurt J.

    Published in Biochemistry (Easton) (21-12-2007)
    “…MreB is a bacterial ortholog of actin that affects cell shape, polarity and chromosome segregation. Although a significant body of work has explored its…”
    Get full text
    Journal Article
  15. 15

    Proteolysis of Cortactin by Calpain Regulates Membrane Protrusion during Cell MigrationD by Perrin, Benjamin J., Amann, Kurt J., Huttenlocher, Anna

    Published in Molecular biology of the cell (01-01-2006)
    “…Calpain 2 regulates membrane protrusion during cell migration. However, relevant substrates that mediate the effects of calpain on protrusion have not been…”
    Get full text
    Journal Article
  16. 16
  17. 17

    Dystrophin binding to nonmuscle actin by Renley, Brian A., Rybakova, Inna N., Amann, Kurt J., Ervasti, James M.

    “…We purified actin from bovine brain by DNase I affinity chromatography in order to compare the binding of dystrophin to muscle actin with its binding to…”
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