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  • 1
    Electronic Resource
    Electronic Resource
    Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development (1989)
    [s.l.] : Nature Publishing Group
    Nature 342 (1989), S. 177-180 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The nm23 complementary DNA was identified by differential hybridization to messenger RNA from K-1735 melanoma lines of varying metastatic potentials2; nm23 RNA levels were uniformly reduced in high metastatic potential rodent cell lines (Fig. la). Human infiltrating ductal breast carcinomas from ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/342177a0
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Potent antitumour activity of a new class of tumour-specific killer cells (1997)
    [s.l.] : Nature Publishing Group
    Nature 385 (1997), S. 78-80 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Toxin molecules, such as Pseudomonas exotoxin A (PEA), kill a cell by inactivating the elongation factor-2 (EF-2) in the cytosol2'8, suggesting that mammalian cells can be genetically modified to produce and secrete targeted toxins by using a signal sequence to lead newly synthesized toxins into ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/385078a0
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Preclinical testing of an anti-erbB-2 recombinant toxin (1996)
    Springer
    Breast cancer research and treatment 38 (1996), S. 19-25 
    Details
    ISSN: 1573-7217
    Keywords: recombinant immunotoxins ; erbB-2 ; pharmacokinetics ; toxicity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The performance of OLX-209 indicates it should enter phase I clinical testing. OLX-209 is a recombinant toxin targeting theerbB-2 oncoprotein. The design of OLX-209 takes advantage of improvements in immunotoxin technology to produce a molecule that is smaller and more potent than a conventional chemically linked antibody-toxin conjugate. The targeting portion of OLX-209 is a single chain antibody structure derived from the anti-erbB-2 hybridoma, e23. This antibody has unusual specificity in that it does not bind to most normal tissue including peripheral nerve or kidney tissue. Preclinical testing showsin vitro activity against breast cancer cell lines in the pM range. Efficacy testing in five models of human cancer indicates that a dose of 43 µg/kg causes reproducible tumor regressions. Efficacy can be achieved on a variety of schedules of administration. The effective dose results in no measurable change in serum liver enzymes when delivered to mice or primates. The LD10 is over twice the effective dose in mice. The pharmacokinetics indicate a t1/2 of 50 minutes for both mice and cynomolgus monkeys. Serum concentrations of more than ten times those observed at the effective dose can be achieved in monkeys with no evidence of toxicity. Antigenicity of OLX-209 is surprisingly low. These results form the basis for the clinical testing phase for OLX-209.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01803780
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Development of non-phosphorylated cyclic thioether peptide binding to the Grb2-SH2 domain (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 45-49 
    Details
    ISSN: 1573-3904
    Keywords: cyclic peptides ; inhibitors ; N-chloroacetyl peptide ; solid-phase peptide synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract One of the critical intracellular signaling pathways involves specific interactions between growth factor receptors and the adaptor protein Grb2. These interactions normally involve specific tyrosine phosphorylated regions in receptors and other cognate proteins. Following the lead of our recent findings that a phage library based non-phosphorylated disulfide linked 11-mer peptide inhibited such interactions, we report here the synthesis of novel redox-stable cyclic peptide analogs. These include thioether cyclized and backbone cyclized structures. The thioether analog was prepared under mild conditions from an N-terminally chloroacetylated and C-terminally cysteine extended peptide precursor. The thioether peptide showed equipotent binding affinity for the Grb2-SH2 domain (IC50 = 10–15 μM) when compared to the disulfide cyclized lead-peptide. The bioactive thioether linked peptide was demonstrated to offer advantages to the disulfide cyclized peptides under physiological conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008815410812
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Development of non-phosphorylated cyclic thioether peptide binding to the Grb2-SH2 domain (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 45-49 
    Details
    ISSN: 1573-3904
    Keywords: cyclic peptides ; inhibitors ; N-chloroacetyl peptide ; signal transduction ; solid-phase peptide synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary One of the critical intracellular signaling pathways involves specific interactions between growth factor receptors and the adaptor protein Grb2. These interactions normally involve specific tyrosine phosphorylated regions in receptors and other cognate proteins. Following the lead of our recent findings that a phage library based non-phosphorylated disulfide linked 11-mer peptide inhibited such interactions, we report here the synthesis of novel redox-stable cyclic peptide analogs. These include thioether cyclized and backbone cyclized structures. The thioether analog was prepared under mild conditions from an N-terminally chloroacetylated and C-terminally cysteine extended peptide precursor. The thioether peptide showed equipotent binding affinity for the Grb2-SH2 domain (IC50=10–15 μM) when compared to the disulfide cyclized lead-peptide. The bioactive thioether linked peptide was demonstrated to offer advantages to the disulfide cyclized peptides under physiological conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443617
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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