[Card system permitting rapid identification or different solid dosage forms (tablets, chachets, pills, gelules, capsules)].
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Biomedical subjects
Publications and source records attributed to G Maury.
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This paper reports on the design and development of an infrastructure allowing one to share and exchange multimedia data in the context of a health network. A single technology exploiting a semantic model of the hospital universe provides users with information and data of diverse origins, generated by the various actors or departments of the health organization. Functions provided include act management and patient record management governed by domain semantics. The functionality has been validated through laboratory experiments against the requirements of protocol directed care and health networks. The functionality is integrated into a clinician workstation exploited in the Internet/Intranet environment thanks to a commercial browser. These results have been obtained with the support of several projects in the frame of the Health-Care Telematics Applications Programme of the European Community and of the Eurêka Programme.
We have determined the affinity of human deoxycytidine kinase with respect to new fluorescent N-methylanthraniloyl cytidine derivatives or non fluorescent enantiomeric cytidine analogues. New results regarding the enantioselectivity and the mechanism of the enzyme are presented.
A series of analogues of L-adenosine and of L-guanosine, including beta-L-dA, beta-L-Ado, beta-L-araA, and beta-L-dG, have been shown to be substrates of human deoxycytidine kinase thus demonstrating the complete lack of enantioselectivity of this enzyme.
2'-Deoxy-beta-L-5-azacytidine(L-Decitabine), beta-L-5-azacytidine, and derivatives were stereospecifically prepared starting from L-ribose or L-xylose. D- and L-enantiomers of 2'-deoxy-beta-5-azacytidine were weak substrates of human recombinant deoxycytidine kinase (dCK), whereas both enantiomers of beta-5-azacytidine or the L-xylo-analogues were not substrates of the enzyme. None of the reported derivatives of beta-L-5-azacytidine was a substrate of human recombinant cytidine deaminase (CDA).