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  • Life and Medical Sciences  (4)
  • Life Sciences  (1)
  • 1
    ISSN: 0886-1544
    Keywords: erythroid spectrin ; non-erythroid spectrin ; Z-line ; membrane ; neuromuscular junction ; developmental changes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We describe multiple human cardiac and skeletal muscle spectrin isoforms. Cardiac muscle expresses five erythroid α,β spectrin-reactive isoforms with estimated MR's of 280, 274, 270, 255, and 246 kD, respectively At least one nonerythroid α-spectrin of MR 284 kD is expressed in heart. While skeletal muscle shares the 280, 270, and 246 kD erythroid spectrins, it expresses an immunologically distinct 284 kD nonerythroid α-spectrin isoform. The 255 kD erythroid β-spectrin isoform is specific for cardiac tissue. By immunocytochemistry, both erythroid β- and nonerythroid α-spectrins are localized to costameres, the plasma membrane, and the neuromuscular junctional region.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 1 (1980), S. 73-97 
    ISSN: 0886-1544
    Keywords: nematodes ; muscle structure ; mutants ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A search for new mutants with altered body-wall muscle cell structure has been undertaken in the nematode C elegans. One-hundred seventeen mutants were isolated after mutagenesis with ethyl methanesulfonate or ultraviolet light, enrichment by a motility-requiring test, and screening by polarized light microscopy; 102 of these mutants were in ten previously established genes, whereas 15 mutants permitted the identification of seven new complementation groups in C elegans. Two of the new genes map on linkage group I (unc-94 and unc-95) and four genes are sex linked (unc-96, unc-97, unc-98, and unc-99). One complementation group (unc-100) could not be mapped because of the special characteristics of its cohort mutants. Representative mutants of the mapped genes were examined by polarized light and electron microscopy. All of the mutants exhibit disruptions of the normal A and I band organization of thick and thin filaments. Several of the mutants produce collections of thin filament-like structures. In one of these cases, HE177 demonstrated collections of somewhat wider, intermediate-sized filaments as well, and the HE195 mutant produces paracrystalline aggregates of thin filaments amidst looser arrangements of similar structures. The mutants in newly identified genes, as well as the new mutants in previously established genetic loci, have promise as tools in the study of myofibrillar assembly and function. Among the 22 complementation groups associated with body-wall structure in C elegans, it is likely that some genes code for regulatory and morphogenetic functions in addition to the well-studied structural, contractile, and calcium-associated proteins in muscle.
    Additional Material: 15 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 3 (1975), S. 354-360 
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The interaction of myosin and paramyosin was investigated by enzymological and ultrastructural techniques. The actin-activated Mg+2 ATPase of rabbit skeletal muscle myosin can be inhibited by clam adductor paramyosin. Both proteins must be rapidly coprecipitated to form filaments for this inhibition. Slowly formed cofilaments are fully activatable by F-actin. In both cases, the cofilaments possess unique structural characteristics when compared to homofilaments.The mode of inhibition appears to be competitive when different concentrations of paramyosin and F-actin are compared. The apparent affinity of the myosin heads for actin is reduced by the presence of paramyosin within rapidly reconstituted thick filaments. These results suggest that paramyosin may serve as part of a relaxing mechanism within invertebrate muscles. It is unlikely that paramyosin plays a role in the initiation and maintenance of catch within specialized molluscan muscles.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    BioEssays 9 (1988), S. 197-200 
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Myosin self-assembly is generally considered to be the major process in thick filament formation within striated muscles. The biological assembly of myosin into thick filaments is being analysed by genetic dissection as well as biochemical and morphological experiments in the nematode Caenorhabditis elegans. This work shows that the assembly of myosin is modulated by its biosynthesis and interaction with non-myosin proteins. Assemblages which generate multiple nascent thick filaments may play a central role in a catalytic cycle of myosin assembly.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    BioEssays 12 (1990), S. 447-448 
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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