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  • 1
    Call number: 04-ZELL:360a
    Keywords: Cytoplasmic filaments ; Filament / Intermediaer
    Pages: 183 p. : ill.
    ISBN: 1570591202
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    04-ZELL:360a departmental collection or stack – please contact the library
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  • 2
    ISSN: 0887-3585
    Keywords: α-keratin ; intermediate filaments ; epidermal keratin ; vimentin ; keratinopathies ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: In intermediate filaments (IF) both epidermal keratin and vimentin molecules have been shown to have an eight residue head to-tail overlap between the rod domains of similarly directed molecules. In the case of the epidermal keratins this region has also been shown to have particular structural/functional significance since it represents a hot-spot for mutations in the four keratinopathies characterized to date. While there is good evidence that this head-to-tail overlap is present in IF containing Type III, IV, and V chains, as well as in the epidermal keratin IF (Ib/IIb), there are no data currently available for the hard α-keratin IF (Ia/IIa). Using a variety of data derived from X-ray diffraction and crosslinking studies, as well as theoretical modeling, it is now possible to demonstrate that the overlap region is not a feature of hard α-keratin IF. Indeed, it is shown that there is a nine residue gap between consecutive parallel molecules in the IF. An explanation for this observation is presented in terms of compensating disulfide bonds that occur both within the IF, and between the IF and the matrix in which the IF are embedded. © 1995 Wiley-Liss, Inc.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2013
    Keywords: Adaptation ; Hypertrophy ; Irradiation ; Myosin heavy chain ; Satellite cells ; Skeletal muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The right extensor digitorum longus (EDL) muscle of growing male rats was overloaded by ablation of its synergist tibialis anterior (TA) muscle. Four weeks later, the overloaded muscle was heavier and contained larger type IIA, IIX and IIB fibres than either untreated contralateral muscle or control muscle from an untreated animal. The myonuclear-to-myoplasmic volume ratio was maintained in the overloaded muscle. Overloaded EDL muscle, previously subjected to a dose of irradiation sufficient to sterilise satellite cells, and EDL muscle which had been only irradiated, were significantly lighter and contained significantly smaller fibres than controls, though a significant amount of normal EDL muscle growth did occur following either treatment. The myonuclear-to-myoplasmic volume ratio of the irradiated muscles was smaller than in controls. Overloaded muscle, with or without prior irradiation, possessed a smaller proportion of fibres containing IIB myosin heavy chain (MHC) and a larger proportion of fibres containing IIA and IIX MHC; a significant percentage of these fibres coexpressed either type IIA and IIX MHC or type IIX and IIB MHC. Thus in the absence of satellite cell mitosis, muscles of young rats possess a limited capacity for normal growth but not for compensatory hypertrophy. Adaptations in MHC gene expression to chronic overload are completely independent of satellite cell activity.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0887-3585
    Keywords: coiled-coli ; alpha-helix ; antiphagocytic ; heptad ; antigenic variation ; sequence repeats ; cell wall protein ; intermediate filaments ; myosin ; tropomyosin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: M protein is considered a virulence determinant on the streptococcal cell wall by virtue of its ability to allow the organism to resist attack by human neutrophils. The complete DNA sequence of the M6 gene from streptococcal strain D471 has allowed, for the first time, the study of the structural characteristics of the amino acid sequence of an entire M protein molecule. Predictive secondary structural analysis revealed that the majority of this fibrillar molecule exhibits strong alpha-helical potential and that, except for the ends, nonpolar residues in the central region of the molecule exhibit the 7-residue periodicity typical for coiled-coil proteins. Differences in this heptad pattern of nonpolar residues allow this central rod region to be divided into three subdomains which correlate essentially with the repeat regions A, B, and C/D in the M6 protein sequence. Alignment of the N-terminal half of the M6 sequence with PepM5, the N-terminal half of the M5 protein, revealed that 42% of the amino acids were identical. The majority of the identities were “core” nonpolar residues of the heptad periodicity which are necessary for the maintenance of the coiled coil. Thus, conservation of structure in a sequence-variable region of these molecules may be biologically significant. Results suggest that serologically different M proteins may be built according to a basic scheme: an extended central coiled-coil rod domain (which may vary in size among strains) flanked by functional end domains.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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