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Molecular architecture of glideosome and nuclear F-actin inPlasmodium falciparum
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Dynamics of F-actin and F-actin complexes
Journal of Molecular Biology, 1974Abstract Intensity fluctuation autocorrelation measurements of laser light scattered from solutions of F-actin and F-actin complexes with myosin subfragments were made in order to estimate the flexibility and other dynamic characteristics of these molecules. F-actin behaves as an unbound diffusing particle.
F D, Carlson, A B, Fraser
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Natural F-actin II. Natural F-actin and its transformation to Straub F-actin
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1967Abstract 1. 1. F-actin component isolated directly from myofibrils, i.e. “natural F-actin”, slowly loses its flow birefringence in 0.1 M KCl. 2. 2. Various nucleotides have a protective effect on the birefringence properties of natural F-actin; ATP or ADP together with Mg 2+ was most effective. 3. 3. Acetone treatment converted natural
H, Hama, K, Maruyama, H, Noda
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Viscoelasticity of F-actin and F-actin/gelsolin complexes
Biochemistry, 1988Actin is the major protein of eukaryote peripheral cytoplasm where its mechanical effects could determine cell shape and motility. The mechanical properties of purified F-actin, whether it is a viscoelastic fluid or an elastic solid, have been a subject of controversy. Mainstream polymer theory predicts that filaments as long as those found in purified
P A, Janmey +5 more
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Current Opinion in Cell Biology, 1993
Recent research on F-actin capping proteins has concentrated on three main areas. The discovery that controlled actin polymerization is the driving force for intracellular movement suggests an important role for capping proteins in regulating filament number and length. A capping protein from Dictyostelium (related to heat-shock protein HSP70) has been
A, Weeds, S, Maciver
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Recent research on F-actin capping proteins has concentrated on three main areas. The discovery that controlled actin polymerization is the driving force for intracellular movement suggests an important role for capping proteins in regulating filament number and length. A capping protein from Dictyostelium (related to heat-shock protein HSP70) has been
A, Weeds, S, Maciver
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Biomimetic F‐Actin Cortex Models
ChemPhysChem, 2009AbstractSince its first production from muscle tissue more than 65 years ago, our knowledge about actin has come a long way. While at the beginning it was identified as a muscle protein, nowadays actin is considered as one of the most important components of the cytoskeleton, playing a crucial role in cell motility, adhesion, morphology and ...
Haraszti, T., Clemen, A., Spatz, J.
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Rheology of F-actin I. Network of F-actin in solution
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1974Abstract The structural viscosity of an F-actin solution of a very low protein concentration was measured at velocity gradients ranging from 0.0005 to 5 s −1 . An F-actin solution of 0.033 mg/ml showed a viscosity value of 44 000 cP at a velocity gradient of 0.0005 s −1 . The viscosity value times the velocity gradient gave a constant value under the
K, Maruyama, M, Kaibara, E, Fukada
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Transiently crosslinked F-actin bundles
European Biophysics Journal, 2010F-actin bundles are prominent cytoskeletal structures in eukaryotes. They provide mechanical stability in stereocilia, microvilli, filopodia, stress fibers and the sperm acrosome. Bundles are typically stabilized by a wide range of specific crosslinking proteins, most of which exhibit off-rates on the order of 1s(-1).
Dan, Strehle +6 more
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Journal of the Mechanical Behavior of Biomedical Materials, 2010
We use the existing data of force-extension experiments on F-actin molecules tied into knots to compute a value of 0.15 for the static friction coefficient for contact between different parts of the same molecule with itself. This estimate for protein-protein friction is relevant for the stabilization of the 273 known proteins with knots, one percent ...
Helmut O, Kirchner, Sebastien, Neukirch
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We use the existing data of force-extension experiments on F-actin molecules tied into knots to compute a value of 0.15 for the static friction coefficient for contact between different parts of the same molecule with itself. This estimate for protein-protein friction is relevant for the stabilization of the 273 known proteins with knots, one percent ...
Helmut O, Kirchner, Sebastien, Neukirch
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