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  • 1
    Electronic Resource
    Electronic Resource
    The Human Bone Morphogenetic Protein 4 (BMP-4) Gene: Molecular Structure and Transcriptional Regulation (1998)
    Springer
    Calcified tissue international 63 (1998), S. 221-229 
    Details
    ISSN: 1432-0827
    Keywords: Key words: Bone morphogenetic protein 4 — Gene structure — Gene organization — Transcriptional regulation.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract. Bone morphogenetic protein 4 (BMP-4) is a vital regulatory molecule that functions throughout human development in mesoderm induction, tooth development, limb formation, bone induction, and fracture repair and is overexpressed in patients who have fibrodysplasia ossificans progressiva. The human gene encoding bone morphogenetic protein 4 (BMP-4) has been isolated and its structural organization characterized. The complete DNA sequence of an 11.2 kb region has been determined. BMP-4 mRNA is transcribed from four exons, although there is evidence that alternate first exons may be used. Transcript initiation occurs at variable positions within a GA-rich region of the DNA. The promoter region is GC-rich with no obvious TATA or CAAT consensus sequences, and contains both positive and negative transcriptional regulatory elements within the 3 kb 5′ flanking region of the RNA start site. Comparison of the human and murine BMP-4 genes reveals highly conserved sequences not only in the exon-coding regions but also within the introns and 5′ flanking regions. BMP-4 localizes to human chromosome 14q21 by fluorescence in situ hybridization, a location more centromeric than that recently reported. These studies provide a foundation for understanding the genetic regulation of this important gene in human development.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002239900518
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  • 2
    Electronic Resource
    Electronic Resource
    Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopy (1991)
    Springer
    Journal of biomolecular NMR 1 (1991), S. 167-173 
    Details
    ISSN: 1573-5001
    Keywords: Channel structure ; Magainin ; Acetylcholine receptor ; Lipid bilayer ; Amphiphilic α-helix ; 15N chemical shift ; Solid-state NMR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Solid-state NMR spectroscopy was used to determine the orientations of two amphipathic helical peptides associated with lipid bilayers. A single spectral parameter provides sufficient orientational information for these peptides, which are known, from other methods, to be helical. The orientations of the peptides were determined using the15N chemical shift observed for specifically labeled peptide sites. Magainin, an antibiotic peptide from frog skin, was found to lie in the plane of the bilayer. M2δ, a helical segment of the nicotinic acetylcholine receptor, was found to span the membrane, perpendicular to the plane of the bilayer. These findings have important implications for the mechanisms of biological functions of these peptides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01877228
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  • 3
    Electronic Resource
    Electronic Resource
    Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers (1995)
    Springer
    Journal of biomolecular NMR 6 (1995), S. 329-334 
    Details
    ISSN: 1573-5001
    Keywords: Solid-state NMR ; Magainin ; Membranes ; Oriented samples ; Structure determination
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A three-dimensional 1H chemical shift/1H-15N dipolar coupling/15N chemical shift correlation spectrum was obtained on a sample of specifically 15N-labeled magainin peptides oriented in lipid bilayers between glass plates in a flat-coil probe. The spectrum showed complete resolution of the resonances from two labeled amide sites in all three dimensions. The three orientationally dependent frequencies associated with each resonance enabled the orientation of the peptide planes to be determined relative to the direction of the applied magnetic field. These results demonstrate the feasibility of multiple-pulse spectroscopy in a flat-coil probe, the ability to measure three spectral parameters from each site in a single experiment, and the potential for resolving among many labeled sites in oriented membrane proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00197814
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