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  • ddc:330  (21)
  • Life and Medical Sciences  (9)
  • 1995-1999  (29)
  • 1965-1969  (1)
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 74 (1969), S. 163-178 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: All tRNA sequences so far known can be folded into a cloverleaf structure. Physical data and chemical reactions allow us to draw conclusions on secondary (cloverleaf) and tertiary structure. N-oxidation of adenosine to adenosine-1-N-oxide can be done with monoperphthalic acid in non-base-paired regions of polynucleotides and can be followed easily by changes in absorption of ultraviolet light. Thus this method can be used to determine the structure of tRNA's. A fingerprint of the N-oxidation product of tRNAyeastPhe reveals that all adenosine residues are protected except the 3′-terminal adenosine and the three adenosine residues in or adjacent to the anticodon. On this basis a conformation of tRNAyeastPhe is proposed. Similar tertiary structures can be constructed for the other tRNA's. In order to connect tertiary structure of a tRNA and recognition by its aminoacylating enzyme, the rate of aminoacylation, as a function of temperature, was measured. Neither changes in the anticodon nor specific changes at the 3′-terminal adenosine abolish aminoacylation. Single crystals of tRNAyeastPhe were obtained from aqueous solutions upon addition of various organic solvents.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Publication Date: 2016-04-28
    Keywords: ddc:330
    Repository Name: Wuppertal Institut für Klima, Umwelt, Energie
    Language: English
    Type: article , doc-type:article
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  • 3
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    Wuppertal : Wuppertal Institut für Klima, Umwelt, Energie | Wuppertal : Wuppertal Institut für Klima, Umwelt, Energie
    Publication Date: 2016-04-28
    Keywords: ddc:330
    Repository Name: Wuppertal Institut für Klima, Umwelt, Energie
    Language: German
    Type: workingpaper , doc-type:workingPaper
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  • 4
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Biologie in unserer Zeit 26 (1996), S. 33-47 
    ISSN: 0045-205X
    Keywords: Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Biologie in unserer Zeit 26 (1996), S. xiv 
    ISSN: 0045-205X
    Keywords: Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Biologie in unserer Zeit 28 (1998), S. 371-380 
    ISSN: 0045-205X
    Keywords: Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Die Entwicklung der heute in der Landwirtschaft und im Gartenbau genutzten Kulturpflanzen ist eine der wichtigsten Leistungen in der Geschichte der Menschheit. Züchterische Maßlig;nahmen des Menschen haben zum Ziel, Pflanzen so zu verändern, daßlig; sie besser an seine Bedürfnisse angepaßlig;t sind. Die Eingriffe durch Züchtung nennt man „gelenkte Evolution“. Ausgehend von wild vorkommenden Arten hat der Mensch Nutzpflanzen geschaffen, die ohne seine Hilfe in der freien Natur auf Dauer nur geringe überlebenschancen hätten. Neben den Nutzpflanzen findet man in der Natur noch viele wilde Arten, die mit den Kulturpflanzen verwandt sind und sich häufig mit ihnen kreuzen lassen. Die wilden Arten verfügen über ein genetisches Potential, auf das in den letzten Jahren immer häufiger zurückgegriffen worden ist, um Zuchtziele des Menschen zu verwirklichen. Vor allem müssen ständig neue Resistenzen gegen Krankheiten und Schädlinge gefunden werden, um dem Infektionsdruck der Krankheitserreger zu widerstehen. Aber auch Gene für Toleranz gegenüber abiotischem Streßlig;, wie Kälte, Dürre, Salz oder Aluminiumtoxizität, sind in den Wildarten vorhanden. Sie können in die Kulturpflanzen eingekreuzt werden, um sie gegen diese Streßlig;faktoren widerstandsfähiger zu machen.Voraussetzung für den Gentransfer von einer Wildart in eine Kulturart ist ihre Kreuzbarkeit. Darüber hinaus mußlig; im Kreuzungsbastard crossing over zwischen homologen Chromosomen gewährleistet sein. Wenn die Chromosomen nicht zu natürlichem crossing over in der Lage sind, können genetische Paarungsmechanismen in der Meiose eingesetzt werden, die zu dem gewünschten Gentransfer führen.Im folgenden soll anhand von drei Beispielen die Bedeutung des genetischen Potentials wilder und verwandter Pflanzenarten für die Verbesserung der Krankheitsresistenz und Inhaltsstoffe sowie Toleranz gegen abiotischen Streßlig; bei Kulturpflanzen demonstriert werden.
    Additional Material: 8 Ill.
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  • 7
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Biologie in unserer Zeit 27 (1997), S. 317-321 
    ISSN: 0045-205X
    Keywords: Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Wenn man nach dem (über-)Lebensrecht der Arten fragt, sollte man nicht vergessen, daß auch der Mensch eine solche ist. Allerdings die einzige, die diese Frage überhaupt stellen kann. Sie beinhaltet die präpotente Voraussetzung, daß der Mensch über das Lebensrecht anderer Arten befinden kann und womöglich zu befinden hat. Das ist eine qualitativ einzigartige Kategorie von Seinsbeziehung.
    Additional Material: 2 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Biologie in unserer Zeit 28 (1998), S. X 
    ISSN: 0045-205X
    Keywords: Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; mitochondria ; mitochondrial matrix ; homo-oligomeric protein ; Mam33p ; gene disruption ; gC1q-R ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Mam33p (mitochondrial acidic matrix protein) is a soluble protein, located in mitochondria of Saccharomyces cerevisiae. It is synthesized as a precursor with an N-terminal mitochondrial targeting sequence that is processed on import. Mam33p assembles to a homo-oligomeric complex in the mitochondrial matrix. It can bind to the sorting signal of cytochrome b2 that directs this protein into the intermembrane space. Mam33p is encoded by an 801 bp open reading frame. Gene disruption did not result in a significant growth defect. Mam33p exhibits sequence similarity to gC1q-R, a human protein that has been implicated in the binding of complement factor C1q and kininogen. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 5 Ill.
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  • 10
    ISSN: 0749-503X
    Keywords: fusion-gene expression ; protein targeting ; genetic engineering ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Overproduction of chimeric proteins containing the HMG2/1 peptide, which comprises the seven transmembrane domains of Saccharomyces cerevisiae 3-hydroxy-3-methylglutaryl-CoA reductase isozymes 1 and 2, has previously been observed to induce the proliferation of internal endoplasmic reticulum-like membranes. In order to exploit this amplified membrane surface area for the accommodation of heterologous microsomal proteins, we fused sequences coding for human cytochrome P4501A1 (CYP1A1) to sequence encoding the HMG2/1 peptide and expressed the hybrid genes in yeast. The heterologous hybrid proteins were targeted into strongly proliferated membranes, as shown by electron microscopic and immunofluorescent analysis. Fusion proteins comprising the whole CYP1A1 polypeptide (HMG2/1-CYP1A1) exhibited 7-ethoxyresorufin-O-deethylase activity, whereas fusion proteins lacking the N-terminal 56 amino acids of CYP1A1 (HMG2/1-ΔCYP1A1) were inactive and appeared to be unable to incorporate protoheme. Similar amounts of heterologous protein were detected in cells expressing HMG2/1-CYP1A1, HMG2/1-ΔCYP1A1 and CYP1A1, respectively. Replacement of the N-terminal membrane anchor domain of human NADPH-cytochrome P450 oxidoreductase by the HMG2/1 peptide also resulted in a functional fusion enzyme, which was able to interact with HMG2/1-CYP1A1 and the yeast endogenous P450 enzyme lanosterol-14α-demethylase.
    Additional Material: 5 Ill.
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