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  • 1
    Electronic Resource
    Electronic Resource
    The role of the 5-HT3 antagonists ondansetron and dolasetron in the control of delayed onset nausea and vomiting in patients receiving moderately emetogenic chemotherapy (1997)
    Springer
    Annals of oncology 8 (1997), S. 181-185 
    Details
    ISSN: 1569-8041
    Keywords: chemotherapy ; clinical trial ; emesis ; 5-HT3 antagonists
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Background: 5-HT3 antagonists are effective inreducing the acute nausea and vomiting caused by cancer chemotherapy. However,it is not clear whether continuing these agents beyond twenty four hours isuseful in controlling emesis on days two to seven after chemotherapy. Patients and methods: Four hundred seven patients receivingmoderately emetogenic chemotherapy who had been given dexamethasone 8 mg i.v.and either ondansetron 32 mg i.v. or dolasetron 2.4 mg/kg i.v. were randomizedto continue either an oral form of their 5-HT3 antagonist(ondansetron 8 mg b.i.d. or dolasetron 200 mg daily) plus dexamethasone 8 mgp.o. daily or dexamethasone alone for days two to seven. Endpoints assessedby self-report were: 1) complete control (no vomiting, no rescue medications,no missing data) of emesis; 2) nausea severity; and 3) quality-of-life asmeasured by the EORTC QLQ-C30. Results: Continuation of 5-HT3 antagonists improvedslightly, but not significantly, the complete control rate (47% vs.41%; P = 0.24 one-sided) after chemotherapy. However, mean nauseaseverity was significantly (P = 0.015 one sided) reduced (by 3 mm on a10 cm scale) on the combined arm. Minimal differences in quality of life wereobserved. Conclusion: The benefit of continuing 5-HT3antagonists beyond 24 hours is modest and the merits of routine use in thesecircumstances debatable.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008247830641
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 Å resolution (2000)
    Springer
    JBIC 5 (2000), S. 110-118 
    Details
    ISSN: 1432-1327
    Keywords: Key words Urease ; Bacillus pasteurii ; X-ray diffraction ; Nickel ; Acetohydroxamic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The structure of Bacillus pasteurii urease inhibited with acetohydroxamic acid was solved and refined anisotropically using synchrotron X-ray cryogenic diffraction data (1.55 Å resolution, 99.5% completeness, data redundancy = 26, R-factor = 15.1%, PDB code 4UBP). The two Ni ions in the active site are separated by a distance of 3.53 Å. The structure clearly shows the binding mode of the inhibitor anion, symmetrically bridging the two Ni ions in the active site through the hydroxamate oxygen and chelating one Ni ion through the carbonyl oxygen. The flexible flap flanking the active site cavity is in the open conformation. The possible implications of the results on structure-based molecular design of new urease inhibitors are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050014
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  • 3
    Electronic Resource
    Electronic Resource
    The complex of Bacillus pasteurii urease with β-mercaptoethanol from X-ray data at 1.65-Å resolution (1998)
    Springer
    JBIC 3 (1998), S. 268-273 
    Details
    ISSN: 1432-1327
    Keywords: Key words Urease ; Bacillus pasteurii ; X-ray ; Nickel ; β-Mercaptoethanol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The structure of β-mercaptoethanol-inhibited urease from Bacillus pasteurii, a highly ureolytic soil micro-organism, was solved at 1.65 Å using synchrotron X-ray cryogenic diffraction data. The structure clearly shows the unexpected binding mode of β-mercaptoethanol, which bridges the two nickel ions in the active site through the sulfur atom and chelates one Ni through the OH functionality. Another molecule of inhibitor forms a mixed disulfide with a Cys residue, thus sealing the entrance to the active site cavity by steric hindrance. The possible implications of the results on structure-based molecular design of new urease inhibitors are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050231
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    Paper (German National Licenses)
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