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  • 2000  (15)
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  • 2000  (15)
  • 11
    Language: English
    In: Immunopharmacology, 8/2000, Vol.49(1-2), p.94
    ISSN: 01623109
    Source: Elsevier (via CrossRef)
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  • 12
    Language: English
    In: Immunopharmacology, 8/2000, Vol.49(1-2), p.12
    ISSN: 01623109
    Source: Elsevier (via CrossRef)
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  • 13
    In: Biological Chemistry, 2000, Vol.381(7), pp.603-610
    Description: A series of bivalent thrombin inhibitors was synthesized, consisting of a dphenylalanylprolylN?(methyl) arginyl active site blocking segment, a fibrinogen recognition exosite inhibitor part, and a peptidic linker connecting these fragments. The methylation of the P1 amino acid led to a moderate decrease in affinity compared with the unmethylated analog. In addition, it prevented the thrombin catalyzed proteolysis, independent of the P1' amino acid used. This is a significant advantage compared to the original hirulogs, which strictly require a proline as P1' amino acid to reduce the cleavage Cterminal to the arginyl residue. Several analogs were prepared by incorporation of different P1' amino acids found in natural thrombin substrates. The most potent inhibitor was I-11 [dCha ProN(Me)ArgThr(Gly)[5]DYEPIPEEAChadGlu] with a K of 37 pM. I-11 is highly selective and no inhibition of the related serine proteases trypsin, factor Xa and plasmin was observed. The stability of I-11 in human plasma in vitro was strongly improved compared to hirulog-1. In addition, a significantly reduced plasma clearance of I-11 was observed after intravenous injection in rats. Results from molecular modeling suggest that a strong reorganization of the hydrogen bonds in the active site of thrombin may result in the proteolytic stability found in this inhibitor series.
    Keywords: Thrombin -- Properties ; Arginine -- Properties ; Protease Inhibitors -- Properties ; Proteolysis -- Research ; Hydrogen Bonds -- Research;
    ISSN: 1431-6730
    E-ISSN: 14374315
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  • 14
    In: Anti-Cancer Drugs, 2000, Vol.11(5), pp.369-376
    Description: Bovine seminal ribonuclease (BS-RNase) is a protein with a number of biological effects. It shows antitumoral, aspermatogenic, antiembryonic, immunosuppressive and antiviral properties. The cytotoxic effects appear to be specific for tumor cells as non-malignant cells seem to be unaffected in vitro. Unfortunately, the in vivo application of BS-RNase so far was successful only when it was administered intratumorally. Therefore, the objective of the present investigation was to improve the properties of BS-RNase by attachment to nanoparticles made of polylactic acid (PLA-NP) using an adsorption method. This preparation was tested in vitro against leukemia (MOLT-4) and lymphoma (H9) cell lines sensitive and resistant to cytarabine. No difference between the nanoparticle preparation and pure BS-RNase was found in these tests. To examine the in vivo effects, the preparations were tested for their aspermatogenic and antiembryonal efficacy compared to the pure BS-RNase as a rapid test for antitumoral activity. The aspermatogenic and antiembryonal effects were enhanced by the nanoparticle preparation. Consequently, BS-RNase loaded adsorptively to PLA-NP holds promise for the in vivo use as an antitumoral agent. Further research will investigate the efficacy of this preparations in an in vivo tumor model.
    Keywords: Antineoplastic Agents -- Pharmacology ; Endoribonucleases -- Pharmacology ; Leukemia -- Drug Therapy ; Lymphoma -- Drug Therapy ; Tumor Cells, Cultured -- Drug Effects;
    ISSN: 0959-4973
    E-ISSN: 14735741
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  • 15
    In: Anti-Cancer Drugs, 2000, Vol.11(6), pp.479-485
    Description: Disseminated neuroblastoma diseases are still indicated by a poor outcome despite treatment regimens including radiation therapy and high-dose chemotherapy with stem cell rescue. Therefore, new substances and treatment regimens are of interest. Aphidicolin (APH), a tetracyclic diterpene antibiotic produced by Cephalosporium aphidicola, has a specific toxicity for neuroblastoma cells. Furthermore, it was shown to enhance the effects of X-ray radiation and chemotherapy on malignant cells. To find new substances, 20 APH derivatives were tested for their anti-neuroblastoma efficacy in vitro in UKF-NB-2 cells. Five derivatives had antitumoral activity in neuroblastoma cells. A relationship between the structure and the antitumoral efficacy showed that the hydroxyl groups at C-3 and C-18 are essential for the antitumoral effects. Furthermore, antitumoral effects of APH in combination with doxorubicin and vincristine, both part of commonly used treatment regimens for disseminated neuroblastoma diseases, were tested in the neuroblastoma cell line UKF-NB-2. APH was found to act synergistically with vincristine and synergistically to additive with doxorubicin depending on the molecular ratio of the substances in combination. This may offer the chance to use APH and its derivatives as additional tools in the treatment of neuroblastomas.
    Keywords: Antineoplastic Agents -- Pharmacology ; Antineoplastic Agents, Phytogenic -- Pharmacology ; Aphidicolin -- Pharmacology ; Cell Survival -- Drug Effects ; Doxorubicin -- Pharmacology ; Enzyme Inhibitors -- Pharmacology ; Neuroblastoma -- Drug Therapy ; Tumor Cells, Cultured -- Drug Effects ; Vincristine -- Pharmacology;
    ISSN: 0959-4973
    E-ISSN: 14735741
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