Results 251 to 260 of about 125,465 (286)
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Hydrostatic pressure studies of native and synthetic thick filaments: II. native thick filaments from rabbit skeletal muscle

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
Native thick filaments isolated from freshly prepared rabbit psoas muscle were found to be resistant to pressure-induced dissociation. With increasing pressure application and release, a bimodal distribution of filament lengths was observed. The shorter filament length is associated with filament breakage at the center of the bare zone, while the ...
S J, Tumminia, J F, Koretz, J V, Landau
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Structure of Limulus and Other Invertebrate Thick Filaments

1984
We have demonstrated remarkable similarity among the skeletal muscles of chelicerate arthropods with respect to the cross-bridge arrangement on the surface of their thick filaments. The latter, gently isolated from the muscles of three representative species (Limulus telson , tarantula leg and scorpion leg and tail) have been examined by electron ...
Levine, R.   +5 more
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[Thick filament shortening as a result of filament sliding].

Biofizika, 1994
It is usually accepted that the phenomenon of thick filament shortening contradicts the sliding filament theory and cross-bridge mechanism of force generation. However, some peculiarity of experimental data indicate the thick filament shortening can be a corollary of the interaction of myosin cross-bridges with the actin filaments "wrong" polarities in
N P, Sidorenko, A A, Klimov
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Visualization of myosin exchange between synthetic thick filaments

Journal of Muscle Research and Cell Motility, 1991
Exchange of myosin molecules between synthetic thick filaments was examined by fluorescence energy transfer and visualized by electron microscopy using streptavidin-gold to detect exchanged biotinylated myosin molecules. N-hydroxysuccinimido-biotin (NHS-biotin) was covalently linked to purified adult chicken pectoralis myosin to obtain assembly ...
A D, Saad   +3 more
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Assembly Processes In Vertebrate Skeletal Thick Filament Formation

Annual Review of Biophysics and Biomolecular Structure, 1988
PERSPECTIVES AND OVERVIEW 217 GENERAL MODES OF ASSEMBLy 2 1 8 THE MYOSIN SUBUNIT ........ ....... ....... ....... ....
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PACKING OF MYOSIN MOLECULES IN MUSCLE THICK FILAMENTS

Cell Biology International, 2000
AbstractThe backbone of the myosin filament is an aggregate of α‐helical coiled coil myosin rods. Its surface forms a three‐stranded helix composed of myosin heads. Currently there is no adequate model to describe the organization of the myosin filament.
N S, Miroshnichenko   +2 more
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Thick filaments of striated muscle are laterally interconnected

Journal of Ultrastructure and Molecular Structure Research, 1988
Earlier reports from this and other laboratories indicated that thick filaments may be interconnected along their length by rung-like structures. This study was carried out to test whether these interconnections are genuine structures; whether they appear in different muscle types; and whether they arise from myosin cross-bridges.
P H, Baatsen   +2 more
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End-filaments: A new structural element of vertebrate skeletal muscle thick filaments

Journal of Molecular Biology, 1981
Abstract The use of low ionic strength buffers to dissociate separated thick filaments into three subfilaments is described. When the dissociation is performed in solution, rather than on an electron microscope grid, structures called end-filaments are observed where the subfilaments terminate.
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Structure of the Insect Thick Filaments

2007
Myosin filaments of insect indirect flight muscles (IFM) are 17 to 19 nm thick and 1.9 to 3.6 μm long structures with probably 4 cross-bridges per level (= crown). These crowns repeat in periods of 14.5 nm along the longitudinal axis of the filament.
Gernot Beinbrech, Gereon Ader
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Assemblages of multiple thick filaments in nematode mutants

Journal of Muscle Research and Cell Motility, 1987
A spectrum of thick filament-related structures exhibiting novel structural features is isolated in addition to the normal thick filaments from unc-15 and unc-82 mutants of Caenorhabditis elegans. Many assemblages have multiple myosin-coated filaments extending from both ends of central domains exhibiting paracrystalline paramyosin.
H F, Epstein, I, Ortiz, G C, Berliner
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