Library

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
    Identification of an amino acid substitution in the benA, β-tubulin gene of Aspergillus nidulans that confers thiabendazole resistance and benomyl supersensitivity (1990)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 17 (1990), S. 87-94 
    Details
    ISSN: 0886-1544
    Keywords: benzimidazole ; anti-microtubule agents ; carbendazim ; nocodazole ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We are using molecular genetic techniques to identify sites of interaction β-tubulin with benzimidizole anti-microtubule agents. We have developed a marker-rescue technique for cloning mutant alleles of the benA, β-tubulin gene of Aspergillus nidulans and have used the technique to clone two mutant benA alleles, benA16 and benA19. These are the only A. nidulans alleles known to confer resistance to the benzimidazole antimicrotubule agent thiabendazole and supersensitivity to other benzimidazole antimicrotubule agents including benomyl and its active breakdown product, carbendazim. benA16 has been shown, moreover, to reduce thiabendazole binding to β-tubulin. We have sequenced the two mutant alleles and have found that they carry different nucleotide changes that cause the same single amino acid substitution, valine for alanine at amino acid 165. Since thiabendazole and carbendazim differ at only one side chain, the R2 group, we conclude that the region around amino acid 165 is involved in the binding of the R2 group of benzimidazole antimicrotubule agents to β-tubulin.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970170204
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Amino acid alterations in the benA (β-tubulin) gene of Aspergillus nidulans that confer benomyl resistance (1992)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 22 (1992), S. 170-174 
    Details
    ISSN: 0886-1544
    Keywords: nocodazole ; carbendazim ; antimicrotubule agents ; thiabendazole ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We report the cloning and sequencing of 18 mutant alleles of the benA, β-tubulin gene of Aspergillus nidulans that confer resistance to the benzimidazole antifungal, antimicrotubule compounds benomyl, carbendazim, nocodazole, and thia-bendazole. In 12 cases, amino acid 6 was changed from histidine to tyrosine or leucine. In four cases, amino acid 198 was changed from glutamic acid to aspartic acid, glutamine, or lysine. In two cases, amino acid 200 was altered from phenylalanine to tyrosine. These data, along with previous data indicating that amino acid 165 is involved in the binding of the R2 group of these compounds [Jung and Oakley, 1990: Cell Motil. Cytoskeleton 17:87-94], suggest that regions of β-tubulin containing amino acids 6, 165, and 198-200 interact to form the binding site of benzimidazole antimicrotubule agents. These results also suggest that the presence of phenylalanine at amino acid 200 contributes to the great sensitivity of many fungi to benzimidazole antimicrotubule agents. © 1992 Wiley-Liss, Inc.
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970220304
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    X-rays from radiative electron capture of highly-charged heavy ions in an electron cooler (1994)
    Springer
    The European physical journal 30 (1994), S. 307-313 
    Details
    ISSN: 1434-6079
    Keywords: 34.80.Kw ; 32.30.Rj
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The x-ray spectra induced by spontaneous capture of free cooling electrons into bare and hydrogenlike heavy ions have been observed. Au78+, Au79+ and U91+ ions were stored in the storage ring ESR at velocities between 60% and 65% of the velocity of light and the x rays were measured in coincidence with stored particles having captured one electron in the electron cooler. The lines observed can be attributed to the direct transition of cooling electrons into theK shell of the projectile and to the characteristicL →K transitions. The latter are mainly induced by capture into higher shells and subsequent cascade transitions. The measurements are compared to detailed calculations within the framework of presently available theories. Although the relative structure of the measured spectra is in fair agreement with the theoretical prediction, the total charge-changing rate in the electron cooler is about a factor of three smaller than expected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01426395
    Library Location Call Number Volume/Issue/Year 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...