Results 211 to 220 of about 622,719 (265)
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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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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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Interaction of troponin components with F-actin and F-actin-tropomyosin complex
Biochimica et Biophysica Acta (BBA) - Protein Structure, 19751. Both TN-T and TN-I components of troponin interact with F-actin, causing its precipitation at 0.1 M KC1 and neutral pH in a form of highly ordered paracrystals, although the ability of TN-I component to precipitate of F-actin is much weaker. 2. F-actin paracrystals obtained in the presence of both TN-T and TN-I components consist of parallel arrays ...
R, Dabrowska +3 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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Journal of Muscle Research and Cell Motility, 1985
Recent progress in actin structural studies may give us new insight into the role of actin in muscle and cell motility. The crystallographic structure of complexes of actin and profilin (Carlsson et aI., I976; C. Schutt, personal communication) and actin and DNAase I (Suck et al., 198I; Sakabe et al., 1983) is being solved by three different groups ...
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Recent progress in actin structural studies may give us new insight into the role of actin in muscle and cell motility. The crystallographic structure of complexes of actin and profilin (Carlsson et aI., I976; C. Schutt, personal communication) and actin and DNAase I (Suck et al., 198I; Sakabe et al., 1983) is being solved by three different groups ...
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On the interaction of F-actin with fibrin
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1974Abstract It was found that F-actin combined with fibrin but not with fibrinogen. At saturating concentrations, two actin molecules were found to combine with one fibrin molecule. These experiments also revealed that under certain conditions thrombin was capable of fragmenting actin.
K, Laki, L, Muszbek
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Supercoiling of f-Actin filaments
Journal of Structural Biology, 1990In the X-ray diffraction pattern from oriented gels of actin-containing filaments sampling of layer lines indicating the development of a well-ordered pseudo-hexagonal lattice within the gels at interfilament spacings as large as 13 nm is observed. This value exceeds by 3 nm the largest estimate of an external diameter of pure f-actin.
V V, Lednev, D, Popp
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Nature Cell Biology, 2017
After mitosis, the nucleus must be rebuilt and chromatin decondensed to permit interphase genomic functions, but decondensation mechanisms are poorly understood. Now, the traditional cytoskeletal protein actin is shown to form transient nuclear filaments that are required for chromatin decondensation and nuclear expansion at mitotic exit.
Moore Henna M., Vartiainen Maria K.
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After mitosis, the nucleus must be rebuilt and chromatin decondensed to permit interphase genomic functions, but decondensation mechanisms are poorly understood. Now, the traditional cytoskeletal protein actin is shown to form transient nuclear filaments that are required for chromatin decondensation and nuclear expansion at mitotic exit.
Moore Henna M., Vartiainen Maria K.
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Polymorphism of F-Actin Assembly. 1. A Quantitative Phase Diagram of F-Actin
Biochemistry, 1996We have made the first quantitative phase diagram of actin filament (F-actin) assembly represented by the concentration of F-actin and the chi parameter which characterizes solvent-solute interaction energy. We manipulated the chi value of F-actin by adding a high molecular weight poly- (ethylene glycol) with average molecular weight 6000 (PEG 6K). The
A, Suzuki, M, Yamazaki, T, Ito
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Diphasic transformations of F-Actin. Effects of urea and MgCl2 on F-actin
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1976Asakura, Taniguchi and Oosawa [1]proposed that muscle actin polymer under sonic vibration is in a different state from that of the ordinary double stranded helical structure (F-actin), characterised by partially interrupted structures of F-actin, a state of "f-actin".
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