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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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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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Modeling of the F-Actin Structure
2007Actin has been a major target for structural studies in biology since F. B. Straub discovered it in 1942.1 This is probably because actin is one of the most abundant proteins in the eukaryotic cell as well as a key player in many physiological events, ranging from genetics to motility.
Oda, T. +4 more
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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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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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