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  • 1
    Electronic Resource
    Electronic Resource
    Trp290Cys mutation in exon IIIa of the fibroblast growth factor receptor 2 (FGFR2) gene is associated with Pfeiffer syndrome (1997)
    Springer
    Human genetics 〈Berlin〉 99 (1997), S. 602-606 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Pfeiffer syndrome is a skeletal disorder characterized by craniosynostosis associated with foot and hand anomalies. Mutations in the genes encoding fibroblast growth factor receptors 1 and 2 (FGFR1 and FGFR2) have recently been implicated in the aetiology of such a syndrome, as well as of other craniosynostotic conditions. We now report a novel missense mutation, a G to C transversion at position 1049 (exon IIIa) of FGFR2, detected in a patient with severe Pfeiffer clinical features. The mutation results in the substitution of a cysteine for tryptophan-290 in the third immunoglobulin-like domain and affects both spliceoforms of FGFR2. Mutations causing replacement of tryptophan-290 have also been reported previously in Crouzon syndrome, a similar but clinically distinct craniosynostotic disorder. This finding confirms the involvement of mutations of FGFR2 exon IIIa in Pfeiffer syndrome, and emphasizes both the extensive heterogeneity of the FGFR2 mutations that result in the Pfeiffer phenotype and the perturbations caused by unpaired cysteine residues in receptor dimerization and transduction of the FGFs signal.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004390050413
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Interactions among the bHLH domains of the proteins encoded by theEnhancer of split andachaete-scute gene complexes ofDrosophila (1996)
    Springer
    Molecular genetics and genomics 251 (1996), S. 628-634 
    Details
    ISSN: 1617-4623
    Keywords: Drosophila ; Enhancer of split ; achaete-scute ; Helix-loop-helix proteins ; Protein-protein interactions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract TheEnhancer of split andachaete-scute gene complexes [E(spl)-C and AS-C] encode helix-loop-helix proteins required for neurogenesis inDrosophila. Using a heterologous bacterial system, we show that (i) the bHLH domains of the proteins encoded by the two gene complexes differ in their ability to form homo- and/or heterodimers; (ii) the bHLH domains of the E(spl)-C proteins m5, m7 and m8 interact with the bHLH domains of the Ac and Sc proteins. These bHLH domains form an interaction network which may represent the molecular mechanism whereby the competent state of the proneural cells is maintained until the terminal determination to neuroblast occurs. Also, the pattern of interactions of the bHLH domains of certain proteins encoded by the two gene complexes may explain their functional redundancy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02174111
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Interactions among the bHLH domains of the proteins encoded by the Enhancer of split and achaete-scute gene complexes of Drosophila (1996)
    Springer
    Molecular genetics and genomics 251 (1996), S. 628-634 
    Details
    ISSN: 1617-4623
    Keywords: Key words Drosophila ; Enhancer of split ; achaete-scute ; Helix-loop-helix proteins ; Protein-protein interactions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  The Enhancer of split and achaete-scute gene complexes [E(spl)-C and AS-C] encode helix-loophelix proteins required for neurogenesis in Drosophila. Using a heterologous bacterial system, we show that (i) the bHLH domains of the proteins encoded by the two gene complexes differ in their ability to form homo- and/or heterodimers; (ii) the bHLH domains of the E(spl)-C proteins m5, m7 and m8 interact with the bHLH domains of the Ac and Sc proteins. These bHLH domains form an interaction network which may represent the molecular mechanism whereby the competent state of the proneural cells is maintained until the terminal determination to neuroblast occurs. Also, the pattern of interactions of the bHLH domains of certain proteins encoded by the two gene complexes may explain their functional redundancy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02174111
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Negative Bohr Effect in Newt Haemolysates and its Regulation (1970)
    [s.l.] : Nature Publishing Group
    Nature 225 (1970), S. 76-77 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Because some individuals exhibited a single ?slow? Hb band, others a single ?fast? band, and others both (probably as a consequence of a genetic polymorphism with two common codominant alleles1), all the haemolysates were examined by starch gel electrophoresis before examination at pH 9 with a ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/225076a0
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  • 5
    Electronic Resource
    Electronic Resource
    The uvp1 gene on the R46 plasmid encodes a resolvase that catalyzes site-specific resolution involving the 5′-conserved segment of the adjacent integron In1 (1998)
    Springer
    Molecular genetics and genomics 258 (1998), S. 404-411 
    Details
    ISSN: 1617-4623
    Keywords: Key words R46 plasmid ; uvp1 gene ; Resolvase ; Site-specific recombination ; Integron
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The product of the uvp1 gene of the R46 plasmid, a member of the DNA invertase-resolvase family, was studied to characterize its recombination activity on the R46 plasmid. The purified Uvp1 protein specifically binds to a 256-bp DNA fragment located immediately upstream of the uvp1 gene itself, and overlapping the 5′-conserved segment (5′-CS) of the R46 integron In1. We identified on this fragment a putative resolution (res) site. Using an in vitro assay, we demonstrated the ability of the protein to resolve a synthetic cointegrate containing a direct repeat of the res site. In vivo, we obtained cointegrate resolution in Uvp1-expressing recA − cells. Sites I and II, subsites of the putative res site, lie within the outer boundary of the integron 5′-CS which is common to all the known integrons. Furthermore, a 69-bp DNA element (containing site I) is required for cointegrate resolution. We propose that this recombination mechanism protects R46 plasmid against unequal distribution following fusion with either identical or different integron-bearing plasmids. Moreover, Uvp1 might have a role in generating gene cassette diversity between the two conserved segments of the integron.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050748
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    Paper (German National Licenses)
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