Results 211 to 220 of about 44,849 (251)
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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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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 in Unstretched Mammalian Smooth Muscle

Nature New Biology, 1971
THE controversy concerning the organization of myosin in mammalian smooth muscle was reviewed (Nature New Biology, 231, 225; 1971) at a time when the studies of Rice's laboratory and our own demonstrated a regular, quasi-rectangular array of thick filaments in guinea-pig taenia coli (TC) and rabbit portal-anterior mesenteric vein (MV), and, further ...
A P, Somlyo, C E, Devine, A V, Somlyo
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Sequential disassembly of vertebrate muscle thick filaments

Journal of Molecular Biology, 1980
Abstract Native thick filaments from rabbit psoas muscle have been sequentially dissolved by incremental rises in salt concentration. Three quite separate stages of depolymerization can be detected; these presumably reflect constraints imposed on the disassembly process by variations in the packing of myosin and by the presence of other thick ...
J, Trinick, J, Cooper
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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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An immunochemical approach to the structure of myosin and the thick filament

Journal of Molecular Biology, 1972
Abstract The arrangement of the various components of myosin within the myofibril has been investigated by staining the thick filament with fluorescein-labeled antibodies directed against myosin and its “subunits”, heavy meromyosin S-1, rod and light chains.
S, Lowey, L A, Steiner
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Substructure of the thick filament of vertebrate striated muscle

Journal of Molecular Biology, 1974
Abstract The number of myosin molecules per 143 A cross bridge repeat in the thick filaments of rabbit psoas muscle was determined by two independent methods. First the molecular weight of isolated thick filaments was evaluated using a modification of the conventional particle counting technique.
K, Morimoto, W F, Harrington
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Thick filament degeneration in a case of acute quadriplegia

Journal of the Neurological Sciences, 1980
Absence of thick filaments from the A bands in tissue giving apparently normal histochemical reactions for myosin ATPase, was seen in a case of acute onset muscle weakness progressing rapidly to quadriplegia with cerebral involvement. There was also widespread degeneration of interstitial structures and much phagocytosis.
R, Yarom, A, Reches
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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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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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