Results 201 to 210 of about 424,053 (243)
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Thick (Myosin) Filaments in a Glomus Tumor
American Journal of Clinical Pathology, 1983An otherwise classic digital glomus tumor is presented with the unusual ultrastructural finding of cytoplasmic thick (myosin) filaments together with thin (actin) filaments in many of the cells. In places, sarcomere-like orientation was seen. It is little appreciated among diagnostic pathologists, but is well-established, that thick (myosin) filaments ...
P A, di Sant'Agnese, K L, De Mesy Jensen
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Structure of Limulus and Other Invertebrate Thick Filaments
1984We 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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The structure of the paramyosin core in molluscan thick filaments
Journal of Muscle Research and Cell Motility, 1981The thick filaments of molluscan muscles have been examined by electron microscopy and X-ray diffraction in order to test whether the structure of the paramyosin core is crystalline and not helicoidal. In accurately cut transverse sections of the white adductor muscle of the oyster the thick filaments are uniformly stained but, when the sections are ...
P M, Bennett, A, Elliott
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PACKING OF MYOSIN MOLECULES IN MUSCLE THICK FILAMENTS
Cell Biology International, 2000AbstractThe 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, 1971THE 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, 1980Abstract 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, 1994It 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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Structure of Limulus telson muscle thick filaments
Journal of Molecular Biology, 1981Abstract Computer analysis of electron micrographs of negatively stained thick filaments isolated from the telson levator muscle of the horseshoe crab ( Limulus polyphemus ) has shown that they have a four-stranded helical structure. The repeating units along each helix have a bent extended shape (measuring approximately 20 nm × 8 nm × 8 nm) and are ...
M, Stewart, R W, Kensler, R J, Levine
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Structure of the Insect Thick Filaments
2007Myosin 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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Substructure of the thick filament of vertebrate striated muscle
Journal of Molecular Biology, 1974Abstract 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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