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Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MALCrystal structures of the vitamin D-binding protein and its complex with actin: structural basis of the actin-scavenger system.The state of the filament.Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAFVisualizing the Ca2+-dependent activation of gelsolin by using synchrotron footprintingMolecular basis for the dual function of Eps8 on actin dynamics: bundling and cappingStructure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coatStructure of an F-actin trimer disrupted by gelsolin and implications for the mechanism of severingThe structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanismCrystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamicsActivation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actinFrom the first to the second domain of gelsolin: a common path on the surface of actin?Structural basis and evolutionary origin of actin filament capping by twinfilin.Helix Straightening as an Activation Mechanism in the Gelsolin Superfamily of Actin Regulatory ProteinsThe expanding superfamily of gelsolin homology domain proteinsStructural analysis of gelsolin using synchrotron protein footprinting.Yersinia effector protein (YopO)-mediated phosphorylation of host gelsolin causes calcium-independent activation leading to disruption of actin dynamics.Single-molecule force spectroscopy reveals force-enhanced binding of calcium ions by gelsolinDestabilization of Ca2+-free gelsolin may not be responsible for proteolysis in Familial Amyloidosis of Finnish Type.Visual insight into how low pH alone can induce actin-severing ability in gelsolin under calcium-free conditions.Calcium-sensitive activity and conformation of Caenorhabditis elegans gelsolin-like protein 1 are altered by mutations in the first gelsolin-like domain.Mechanical stimulation induces formin-dependent assembly of a perinuclear actin rimType IV pilus structure and bacterial pathogenicity.Decoding Ca2+ signals in plants.Calcium-controlled conformational choreography in the N-terminal half of adseverinRegulatory role of the second gelsolin-like domain of Caenorhabditis elegans gelsolin-like protein 1 (GSNL-1) in its calcium-dependent conformation and actin-regulatory activities.Elucidating the mechanism of familial amyloidosis- Finnish type: NMR studies of human gelsolin domain 2.New approaches to targeting the actin cytoskeleton for chemotherapy.Gelsolin amyloidosis: genetics, biochemistry, pathology and possible strategies for therapeutic intervention.Gelsolin: the tail of a molecular gymnast.The proteome of the differentiating mesencephalic progenitor cell line CSM14.1 in vitro.Essential role for calcium waves in migration of human vascular smooth muscle cells.The disintegration of a molecule: the role of gelsolin in FAF, familial amyloidosis (Finnish type).The effect of cathodic electrochemical potential of Ti-6Al-4V on cell viability: voltage threshold and time dependence.Ca-dependent binding of actin to gelsolin.Molecular dynamics study of a gelsolin-derived peptide binding to a lipid bilayer containing phosphatidylinositol 4,5-bisphosphate.Identification of a functional switch for actin severing by cytoskeletal proteins.The polymerization of actin: structural changes from small-angle neutron scattering.A gelsolin-like protein from Papaver rhoeas pollen (PrABP80) stimulates calcium-regulated severing and depolymerization of actin filaments.A vertebrate slow skeletal muscle actin isoform.
P2860
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P2860
description
article publié dans la revue scientifique Science
@fr
im Dezember 1999 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published in Science
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в грудні 1999
@uk
name
Domain Movement in Gelsolin: A Calcium-Activated Switch
@en
Domain Movement in Gelsolin: A Calcium-Activated Switch
@nl
type
label
Domain Movement in Gelsolin: A Calcium-Activated Switch
@en
Domain Movement in Gelsolin: A Calcium-Activated Switch
@nl
prefLabel
Domain Movement in Gelsolin: A Calcium-Activated Switch
@en
Domain Movement in Gelsolin: A Calcium-Activated Switch
@nl
P2093
P1433
P1476
Domain movement in gelsolin: a calcium-activated switch
@en
P2093
P304
P356
10.1126/SCIENCE.286.5446.1939
P407
P577
1999-12-01T00:00:00Z