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  • 1
    Electronic Resource
    Electronic Resource
    Heterodimeric capping proteins constitute a highly conserved group of actin-binding proteins (1990)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 11 (1990), S. 369-376 
    Details
    ISSN: 0192-253X
    Keywords: Cytoskeleton ; capping proteins ; genamic structure ; Dictyostelium ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The two subunits of the het-erodimeric protein cop32/34, an actin-binding protein, are encoded by separate single-copy genes. We have established the genomic structure of both genes. A sequence comparison of cap32/34 with capZ from chicken skeletal muscle and two partially known sequences from Saccharomyces cerevisiae and Xenopus laevis show that heterodimeric capping proteins belong to a highly conserved group of actin-binding proteins. This conclusion is supported by the cross-reaction of polyclonal antibodies against cap32 and cap34 with proteins from lower and higher eukaryotes. In addition, a system is presented that allows the expression of truncated cap34 polypeptides under the control of the cap34 promoter.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020110508
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Actin-binding proteins are conserved from slime molds to man (1988)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 9 (1988), S. 521-530 
    Details
    ISSN: 0192-253X
    Keywords: cytoskeleton ; Dictyostelium ; dystrophin ; fragmin ; gelsolin ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: DNA clones encoding the actin-binding proteins α-actinin and severin from Dictyostelium discoideum were isolated and sequenced. Comparisons of the deduced amino acid sequences with proteins from other species showed striking similarities at distinct regions. The F-actin cross-linking molecule α-actinin carries two characteristic EF-hand structures highly homologous to the Ca2+-binding loops of proteins from the calmodulin superfamily. An N-terminal region that is conserved in α-actinin from D. discoideum and vertebrates is also related to parts of the dystrophin sequence and might represent the F-actin binding site. Severin, gelsolin, villin, and fragmin share homologous sequences that are believed to participate in the severing activity of these proteins.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020090428
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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