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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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Current Opinion in Structural Biology, 1998
The study of proteins that bind filamentous actin (F-actin) is entering an exciting stage as more and more structures are determined. After more than 50 years in which the focus was on muscle proteins, emphasis has recently shifted towards understanding the complex interplay among actin-binding molecules in non-muscle cells.
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The study of proteins that bind filamentous actin (F-actin) is entering an exciting stage as more and more structures are determined. After more than 50 years in which the focus was on muscle proteins, emphasis has recently shifted towards understanding the complex interplay among actin-binding molecules in non-muscle cells.
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Natural F-actin III. Natural F-actin as inactive polymer
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1969Abstract 1. 1. Natural F-actin was found to be short in length, and the length distribution was not changed by storage demonstrating that an end-to-end interaction between natural F-actins was lacking. 2. 2. Natural F-actin never accelerated the G-F transformation of Straub G-actin, but a great acceleration was produced by sonic treatment ...
Michiki Kasai, Hiroko Hama
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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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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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Resolving the cadherin–F-actin connection
Nature Cell Biology, 2016Cadherin adhesion complexes have recently emerged as sensors of tissue tension that regulate key developmental processes. Super-resolution microscopy experiments now unravel the spatial organization of the interface between cadherins and the actin cytoskeleton and reveal how vinculin, a central component in cadherin mechanotransduction, is regulated by
Han, Mitchell K L, de Rooij, Johan
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Journal of Theoretical Biology, 1985
The equipartition theorem is used to calculate the mode amplitudes for F-actin thermal torsion. The amplitudes phi n are found to scale as n-1, (EI)-1/2, and L1/2, where n is mode number, EI is actin bending stiffness, and L is filament length. Depending on conditions, the amplitude can be as large as 15 degrees; this is discussed briefly in terms of ...
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The equipartition theorem is used to calculate the mode amplitudes for F-actin thermal torsion. The amplitudes phi n are found to scale as n-1, (EI)-1/2, and L1/2, where n is mode number, EI is actin bending stiffness, and L is filament length. Depending on conditions, the amplitude can be as large as 15 degrees; this is discussed briefly in terms of ...
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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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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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Removal of nucleotides from F-actin
Biochimica et Biophysica Acta, 1963Abstract A partially nucleotide-free F-actin was obtained by a prolonged dialysis of a normal F-actin having bound ADP, but which maintained its polymer structure. The removal of ADP seemed to happen with equal probability everywhere in the F-actin. There was no appreciable difference in optical and rheological properties between the nucleotide-free ...
M, KASAI, F, OOSAWA
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