ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Biologen in unserer Zeit (1996)
    Weinheim : Wiley-Blackwell
    Biologie in unserer Zeit 26 (1996), S. 33-47 
    Details
    ISSN: 0045-205X
    Keywords: Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/biuz.19960260313
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Pharmazie (1996)
    Weinheim : Wiley-Blackwell
    Biologie in unserer Zeit 26 (1996), S. xiv 
    Details
    ISSN: 0045-205X
    Keywords: Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/biuz.19960260617
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Genetische Ressourcen von Wildpflanzenarten beleben die Kulturpflanzenzüchtung (1998)
    Weinheim : Wiley-Blackwell
    Biologie in unserer Zeit 28 (1998), S. 371-380 
    Details
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/biuz.960280606
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Lebensrecht und Artenschutz (1997)
    Weinheim : Wiley-Blackwell
    Biologie in unserer Zeit 27 (1997), S. 317-321 
    Details
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/biuz.960270515
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Physik (1998)
    Weinheim : Wiley-Blackwell
    Biologie in unserer Zeit 28 (1998), S. X 
    Details
    ISSN: 0045-205X
    Keywords: Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/biuz.960280515
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Mam33p, an oligomeric, acidic protein in the mitochondrial matrix of Saccharomyces cerevisiae is related to the human complement receptor gC1q-R (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 14 (1998), S. 303-310 
    Details
    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.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
  • 7
    Electronic Resource
    Electronic Resource
    Sequence and functional analysis of a 7·2 kb fragment of Saccharomyces cerevisiae chromosome II including GAL7 and GAL10 and a new essential open reading frame (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 11 (1995), S. 79-83 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome II ; GAL7 ; GAL10 ; leucine zipper ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The nucleotide sequence of a fragment of 7200 base pairs of Saccharomyces cerevisiae chromosome II has been determined. The sequence contains three open reading frames (ORFs). Two genes for galactose metabolism, GAL7 and part of the GAL10 coding region, are localized on the fragment. Comparison to the previously published sequence data showed several differences, leading to changes in the amino acid sequences of GAL7 and GAL10.One new ORF, YBR0224, was detected, coding for a protein with 918 amino acids. Comparison to the DNA and protein data bases showed no significant homologies. The protein has some interesting features pointing to a function involved in transcription regulation: a leucine zipper motif, a highly acidic region, possibly involved in transcription activation and a putative nuclear localization signal. Deletion analysis showed that the gene is essential when deleted in strain W303. Spores could germinate and form microcolonies, but efforts to propagate the colonies failed. Deletion of this gene in a different genetic background (strain M5) led to very poor-growing mutant strains with cells showing aberrant cellular morphologies.The nucleotide sequence of the fragment has been deposited in the EMBL-database under the Accession Number X81324.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320110110
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Targeting of heterologous membrane proteins into proliferated internal membranes in Saccharomyces cerevisiae (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 11 (1995), S. 913-928 
    Details
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320111003
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...