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  • 1
    Electronic Resource
    Electronic Resource
    Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk (2006)
    [s.l.] : Nature Publishing Group
    Nature 439 (2006), S. 229-233 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The Z-disk of striated and cardiac muscle sarcomeres is one of the most densely packed cellular structures in eukaryotic cells. It provides the architectural framework for assembling and anchoring the largest known muscle filament systems by an extensive network of protein–protein interactions, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature04343
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  • 2
    Electronic Resource
    Electronic Resource
    Structural basis for activation of the titin kinase domain during myofibrillogenesis (1998)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 395 (1998), S. 863-869 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The giant muscle protein titin (connectin) is essential in the temporal and spatial control of the assembly of the highly ordered sarcomeres (contractile units) of striated muscle. Here we present the crystal structure of titin's only catalytic domain, an autoregulated serine kinase (titin kinase). ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/27603
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  • 3
    Electronic Resource
    Electronic Resource
    Erratum Structural basis for activation of the titin kinase domain during myofibrillogenesis (1999)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 397 (1999), S. 719-719 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Nature 395, 863–869 (1998) D.O.F.'s full address should have included the Institut für Zoophysiologie und Zellbiologie (University of Potsdam, Lennéstrasse 7a, 14471 Potsdam, Germany); lane 1 of Fig. 5a referred to ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/17835
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  • 4
    Electronic Resource
    Electronic Resource
    The evolution of titin and related giant muscle proteins (1994)
    Springer
    Journal of molecular evolution 38 (1994), S. 395-404 
    Details
    ISSN: 1432-1432
    Keywords: Titin ; Twitchin ; Muscle ; Myosin light-chain kinase ; Immunoglobulin c2 domain ; Fibronectin class III domain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Titin and twitchin are giant proteins expressed in muscle. They are mainly composed of domains belonging to the fibronectin class III and immunoglobulin c2 families, repeated many times. In addition, both proteins have a protein kinase domain near the C-terminus. This paper explores the evolution of these and related muscle proteins in an attempt to determine the order of events that gave rise to the different repeat patterns and the order of appearance of the proteins. Despite their great similarity at the level of sequence organization, titin and twitchin diverged from each other at least as early as the divergence between vertebrates and nematodes. Most of the repeating units in titin and twitchin were estimated to derive from three original domains. Chicken smooth-muscle myosin light-chain kinase (smMLCK) also has a kinase domain, several immunoglobulin domains, and a fibronectin domain. From a comparison of the kinase domains, titin is predicted to have appeared first during the evolution of the family, followed by twitchin and with the vertebrate MLCKs last to appear. The so-called C-protein from chicken is also a member of this family but has no kinase domain. Its origin remains unclear but it most probably pre-dates the titin/twitchin duplication.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00163156
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  • 5
    Electronic Resource
    Electronic Resource
    Cardiac myosin binding protein–C gene splice acceptor site mutation is associated with familial hypertrophic cardiomyopathy (1995)
    [s.l.] : Nature Publishing Group
    Nature genetics 11 (1995), S. 438-440 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] To refine the limits of CMH4, we conducted a detailed genetic analysis on the first family linked to this locus, Family 714. Analysis of forty microsatellite markers indicated four recombinant individuals, III-l, III-11, IV-4 and IV-9, which when analysed reduced the locus from 17 cM5 to 5 cM (Fig. ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/ng1295-438
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  • 6
    Electronic Resource
    Electronic Resource
    A survey of in situ sarcomere extension in mouse skeletal muscle (1997)
    Springer
    Journal of muscle research and cell motility 18 (1997), S. 465-472 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The giant molecule titin/connectin was demonstrated to connect the ends of thick filaments with the Z-disks and thus to provide an elastic connection that seems to be responsible for passive tension in striated muscle. To investigate the physiological limits of I-band titin extension in skeletal muscle, we have measured sarcomere lengths of a number of mouse postural and clonal muscles in situ under the constraints imposed by the skeletal, ligamentous and tendinous components of the motile apparatus. These values now give upper limits for the extension of the I-band and therefore for the maximal degree of titin extension under physiological constraints. We find that I-band extension in all muscles investigated does not exceed a factor of 2.5 in situ, which is well below values obtainable in isolated fibre preparations. Approach to the yield-point is therefore prevented by extramuscular mechanisms. Sarcomere lengths near the tendinous junction and within the muscle are virtually identical in extended muscle, suggesting that a major function of titin in intact muscle is to ensure uniform sarcomere lengths over the entire muscle length and thus to prevent localized myofibril overstretch during isometric contraction
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018650915751
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  • 7
    Electronic Resource
    Electronic Resource
    Assembly of the cardiac I-band region of titin/connectin: expression of the cardiac-specific regions and their structural relation to the elastic segments (1996)
    Springer
    Journal of muscle research and cell motility 17 (1996), S. 449-461 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The giant molecule titin (also called connectin) provides an elastic connection in the I-band between the Z-disk and A-band of striated muscle. This region is assembled in a tissue-specific way by extensive differential splicing events. We have raised monoclonal antibodies against the two N2-line isoforms of titin and demonstrate that both forms of cardiac I-band titin are constitutively co-expressed in atrial and ventricular muscle. In developing mouse embryos, the expression of the cardiac N2-B isoform remains strictly cardiac-specific and is linked to the expression of the ubiquitous N2-A isoform. The mechanical function of the cardiac N2-line region was investigated ultrastructurally. Immunoelectron microscopy reveals that the N2-B region separates two mechanically distinct sections of titin with a hyperextensible segment spanning the distance to the Z-disk. The formation of a plateau in the extension of cardiac titin rules out that Ig-domains can be unfolded as a mechanism of elasticity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00123361
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  • 8
    Electronic Resource
    Electronic Resource
    A six-module human nebulin fragment bundles actin filaments and induces actin polymerization (1998)
    Springer
    Journal of muscle research and cell motility 19 (1998), S. 225-235 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We have investigated the interaction of a 6-repeat recombinant human nebulin fragment (S6R2R7) with F-actin, with Mg2+-induced actin paracrystals, and G-actin, respectively. This fragment corresponds to super-repeat 6, repeat 2 to 7 of human nebulin, and is located in the N-terminal part of the super-repeat region of the nebulin molecule. The S6R2R7 fragment included an immuno-tag of three amino-acid residues (EEF) at one end which was detectable by a monoclonal anti-tubulin YL1/2. By a cosedimentation assay, interaction between F-actin and S6R2R7 was observed. Electron microscopy revealed the formation of large bundle-like aggregates containing highly parallelized actin filaments, apparently caused by actin bundling of the nebulin fragment. Compared with Mg2+-induced actin paracrystals where the helices of the actin filaments are arranged in register, the filaments in the actin–nebulin bundles seem to be packed in a different way and show no obvious periodicity. The bundles were also visible in the light microscope, and immunofluorescence microscopy revealed binding of the nebulin fragment S6R2R7 to both preformed Mg2+ paracrystals and to F-actin. We also analyzed the effect of S6R2R7 on actin under non-polymerizing conditions by cosedimentation assays and pyrene actin fluorimetry, as well as fluorescence microscopy and electron microscopy. Nebulin-induced actin polymerization was observed with an enhancement of the nucleation step indicating a stabilization of actin nuclei by S6R2R7. Light and electron microscopy revealed bundle-like actin–nebulin aggregates similar to those formed by pre-assembled F-actin and S6R2R7. Thus, even in the absence of salt, S6R2R7 promotes actin polymerization and induces formation of tightly packed actin filament bundles. We assume that the actin filaments are crosslinked by the nebulin fragments, indicating a rather low cooperativity of binding to a single filament.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005372915268
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