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  • 1
    Electronic Resource
    Electronic Resource
    Structure-based design of potent CDK1 inhibitors derived from olomoucine (2000)
    Springer
    Journal of computer aided molecular design 14 (2000), S. 403-409 
    Details
    ISSN: 1573-4951
    Keywords: cyclin-dependent kinase ; CDK1 ; inhibitor ; olomoucine ; structure-based design
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Cyclin-dependent kinase 1 (CDK1), an enzyme participating in the regulation of the cell cycle, constitutes a possible target in the search for new antitumor agents. Starting from the purine derivative olomoucine and following a structure-based approach, potent inhibitors of this enzyme were rapidly identified. The molecular modeling aspects of this work are described.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008115004986
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of ompV, the gene for a major Vibrio cholerae outer membrane protein (1986)
    Springer
    Molecular genetics and genomics 205 (1986), S. 494-500 
    Details
    ISSN: 1617-4623
    Keywords: Signal sequence ; Gene regulation ; Export ; Codon usage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nucleotide sequence of the ompV gene of Vibrio cholerae was determined. The product of the gene is a 28,000 dalton protein which, after the removal of a 19 amino acid signal sequence, produces a mature outer membrane protein of 26,000 daltons. The cleavage site was determined by amino-terminal amino acid sequencing of the purified mature protein. The DNA upstream of the gene shows the presence of a typical promoter region as judged from the Escherichia coli consensus information; however, the Shine-Dalgarno sequence is associated with a region capable of forming a secondary structure in the mRNA. The formation of this structure would inhibit binding of the mRNA to the ribosome and reduce translation. It is proposed that this structure is recognized by a positive activator in V. cholerae and because of its absence in E. coli ompV is poorly expressed. The distribution of rare codons within ompV suggests that they may serve to slow down the translation of particular domains such that the nascent polypeptide has an opportunity to take up its conformation without interference from the later formed regions. Such a mechanism could aid localization of the protein if export were by a cotranslational secretion system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00338088
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    Paper (German National Licenses)
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