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Autoinhibition and relief mechanisms for MICAL monooxygenases in F-actin disassembly. [PDF]

Nat Commun
Lin L, Dong J, Xu S, Xiao J, Yu C, Niu F, Wei Z.   +6 more
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Dynamics of F-actin and F-actin complexes

Journal of Molecular Biology, 1974
Abstract 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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Viscoelasticity of F-actin and F-actin/gelsolin complexes

Biochemistry, 1988
Actin 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, S, Hvidt, J, Peetermans, J, Lamb, J D, Ferry, T P, Stossel   +5 more
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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, 1967
Abstract 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, 1974
Abstract 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, 1975
1. 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, E, Nowak, Z, Podlubnaya, W, Drabikowski   +3 more
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F-actin capping proteins

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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The structure of F-actin

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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