Search Results - "Weeds, A. G."

Structure of gelsolin segment 1-actin complex and the mechanism of filament severing by McLaughlin, P. J, Gooch, J. T, Mannherz, H.-G, Weeds, A. G

“…The structure of the segment 1 domain of gelsolin, a protein that fragments actin filaments in cells, is reported in complex with actin. Segment 1 binds…”
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Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments by Hawkins, M, Pope, B, Maciver, S. K, Weeds, A. G

“…ADF (actin depolymerizing factor) is an M(r) 19,000 actin-binding protein present in many vertebrate tissues and particularly abundant in neuronal cells. We…”
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Evidence for Functional Homology in the F-Actin Binding Domains of Gelsolin and α-Actinin: Implications for the Requirements of Severing and Capping by Way, M., Pope, B., Weeds, A. G.

“…The F-actin binding domains of gelsolin and α-actinin compete for the same site on actin filaments with similar binding affinities. Both contain tandem repeats…”
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Identification of a region in segment 1 of gelsolin critical for actin binding by Way, M., Pope, B., Gooch, J., Hawkins, M., Weeds, A. G.

“…The actin severing and capping protein gelsolin contains three distinct actin binding sites. The smallest actin binding domain of approximately 15,000 Mr was…”
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Expression of Human Plasma Gelsolin in Escherichia coli and Dissection of Actin Binding Sites by Segmental Deletion Mutagenesis by Way, M., Gooch, J., Pope, B., Weeds, A. G.

“…Human plasma gelsolin has been expressed in high yield and soluble form in Escherichia coli. The protein has nucleating and severing activities identical to…”
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Ser6 in the maize actin‐depolymerizing factor, ZmADF3, is phosphorylated by a calcium‐stimulated protein kinase and is essential for the control of functional activity by Smertenko, Andrei P., Jiang, Chang‐Jie, Simmons, Nicola J., Weeds, Alan G., Davies, Dewi R., Hussey, Patrick J.

“…Summary Maize actin‐depolymerizing factor, ZmADF, binds both G‐ and F‐actin and enhances in vitro actin dynamics. Evidence from studies on vertebrate…”
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The maize actin‐depolymerizing factor, ZmADF3, redistributes to the growing tip of elongating root hairs and can be induced to translocate into the nucleus with actin by Jiang, Chang‐Jie, Weeds, Alan G., Hussey, Patrick J.

“…Summary The maize actin depolymerizing factor, ZmADF3, binds G‐and F‐actin, and increases in vitro actin dynamics. Polyclonal antibodies have been raised…”
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Expression of the N-terminal domain of dystrophin in E. coli and demonstration of binding to F-actin by Way, M., Pope, B., Cross, R.A., Kendrick-Jones, J., Weeds, A.G.

“…The N-terminal head domain of human dystrophin has been expressed in soluble form and high yield in E. coli, allowing us to test the previously unconfirmed…”
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Pollen specific expression of maize genes encoding actin depolymerizing factor-like proteins by Lopez, I. (Universidad Nacional Autonoma de Mexico, Mexico, Mexico.), Anthony, R.G, Maciver, S.K, Jiang, C.J, Khan, S, Weeds, A.G, Hussey, P.J

“…In pollen development, a dramatic reorganization of the actin cytoskeleton takes place during the passage of the pollen grain into dormancy and on activation…”
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Are the Conserved Sequences in Segment 1 of Gelsolin Important for Binding Actin? by Way, M., Pope, B., Weeds, A. G.

“…The minimal region required for actin binding in the smallest of the three domains of gelsolin (termed Segment 1 or S1) was previously defined by deletion…”
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Direct visualization by electron microscopy of the weakly bound intermediates in the actomyosin adenosine triphosphatase cycle by Pollard, T.D., Bhandari, D., Maupin, P., Wachsstock, D., Weeds, A.G., Zot, H.G.

“…We used a novel stopped-flow/rapid-freezing machine to prepare the transient intermediates in the actin-myosin adenosine triphosphatase (ATPase) cycle for…”
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Variant plasma gelsolin responsible for familial amyloidosis (Finnish type) has defective actin severing activity by Weeds, A.G., Gooch, John, McLaughlin, P., Maury, C.P.J.

“…Familial amyloidosis, Finnish type is caused by a single base mutation in gelsolin, an actin filament severing and capping protein that is present in most…”
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Two of the three actin-binding domains of gelsolin bind to the same subdomain of actin Implications for capping and severing mechanisms by Pope, B., Way, M., Weeds, A.G.

“…Gelsolin binds two monomers in the nucleating complex with G-actin in calcium and caps actin filaments. However, 3 actin-binding domains have been identified…”
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Molecular and mutational analysis of a gelsolin-family member encoded by the flightless I gene of Drosophila melanogaster by De Couet, H.G. (University of Hawaii, Honolulu, HI.), Fong, K.S.K, Weeds, A.G, McLaughlin, P.J, Miklos, G.L.G

“…The flightless locus of Drosophila melanogaster has been analyzed at the genetic, molecular, ultrastructural and comparative crystallographic levels. The gene…”
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Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin by WEEDS, A. G, TAYLOR, R. S

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Role of actin-binding proteins in cytoskeletal dynamics by Weeds, A G, Gooch, J, Hawkins, M, Pope, B, Way, M

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Crystallization of the complex of actin with gelsolin segment 1 by Mannherz, H G, Gooch, J, Way, M, Weeds, A G, McLaughlin, P J

“…Crystals of a 1:1 complex between human gelsolin segment 1 and actin have been grown from solutions containing polyethylene glycol 6000. The crystals are…”
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Primary, secondary and tertiary myotubes in developing skeletal muscle: a new approach to the analysis of human myogenesis by Draeger, A, Weeds, A G, Fitzsimons, R B

“…Monoclonal antibodies to myosins have been used to describe and define the appearance and maturation of 3 different classes of myotube in developing human…”
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Uncoupling actin filament fragmentation by cofilin from increased subunit turnover by Pope, Brian J, Gonsior, Sabine M, Yeoh, Sharon, McGough, Amy, Weeds, Alan G

“…The actin depolymerizing factor (ADF)/cofilin family of proteins interact with actin monomers and filaments in a pH-sensitive manner. When ADF/cofilin binds…”
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Loss of calcium sensitivity of plasma gelsolin is associated with the presence of calcium ions during preparation by Pope, B., Gooch, J., Hinssen, H., Weeds, A.G.

“…Gelsolin is a calcium-dependent actin severing and capping protein. Calcium ‘opens’ the molecule to make actin binding sites accessible, but removal of calcium…”
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