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Problematics of fungal infections in the paranasal sinuses

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Nowak K., Szyfter W.
Otolaryngologia Polska
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2008
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vol. 62(6)
716-721
EN
Fungal infections of the ear and paranasal sinus, are recognised quite rarely, but they make sometimes, for many reasons, very important diagnostic-therapy issue. Cantagion may developes near every paranasal sinus. Facilities to invasion give every states, which weaken general and punctual immunity (like immunosupression, chemo-sterydotherapy, blood disease, pregnancy and HIV). After penetrated organism, course of infections, in case of type of patogens, trim of the patient and localization, can have without symptoms, sharp, chronic or fulminant shape. The hardest course with the highest mortality occur in the cases of mucormycosis and aspergillosis. Actually curiosity occur cases of fungal infections, since this times consider to be unpathogenic for humans. For treatment of sinus mycosis in majority chirurgical treatment is required. In addition or the sake of morphological differentiation fungal, in their developing cycle, treatment mycosis recommends serious diffi culty, extra factor, which impeds therapy, is a must of prolongely antifungal treatment and repeated (to total elimination) remove hyphae from sinus, which stay sometimes even for week. Progress of the mycotic infections in paranasal sinus, remain bacterial infections and is often reason of bad diagnosis and incorrect treatment.
2
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Real-time PCR approach in dermatophyte detection and Trichophyton rubrum identification

100%
Kobylak N., Bykowska B., Nowicki R., Brillowska-Dąbrowska A.
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2015
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vol. 62
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issue 1
119-122
EN
Dermatophytes are keratinophilic molds that infect human hair, nails and skin. Diagnosis of dermatophytosis is based on morphological, serological and biochemical features. However, identification is difficult and laborious due to similarities between microorganisms. Thus, there is considerable interest to develop mycological diagnostic procedures based on molecular biology methods. In this study, fast, two-step DNA extraction method and real-time PCR was used for detection of dermatophytes DNA using pan-dermatophyte primers and identification of Trichophyton rubrum from pure cultures. The applied method allowed correct detection of all dermatophytes and correct identification of Trichophyton rubrum in less than 2 hours.
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Glucosamine-6-phosphate synthase, a novel target for antifungal agents. Molecular modelling studies in drug design.

88%
Wojciechowski M., Milewski S., Mazerski J., Borowski E.
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2005
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vol. 52
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issue 3
647-653
EN
Fungal infections are a growing problem in contemporary medicine, yet only a few antifungal agents are used in clinical practice. In our laboratory we proposed the enzyme L-glutamine : D-fructose-6-phosphate amidotransferase (EC 2.6.1.16) as a new target for antifungals. The structure of this enzyme consists of two domains, N-terminal and C-terminal ones, catalysing glutamine hydrolysis and sugar-phosphate isomerisation, respectively. In our laboratory a series of potent selective inhibitors of GlcN-6-P synthase have been designed and synthesised. One group of these compounds, including the most studied N3-(4-methoxyfumaroyl)-l-2,3-diaminopropanoic acid (FMDP), behave like glutamine analogs acting as active-site-directed inactivators, blocking the N-terminal, glutamine-binding domain of the enzyme. The second group of GlcN-6-P synthase inhibitors mimic the transition state of the reaction taking place in the C-terminal sugar isomerising domain. Surprisingly, in spite of the fact that glutamine is the source of nitrogen for a number of enzymes it turned out that the glutamine analogue FMDP and its derivatives are selective against GlcN-6-P synthase and they do not block other enzymes, even belonging to the same family of glutamine amidotransferases. Our molecular modelling studies of this phenomenon revealed that even within the family of related enzymes substantial differences may exist in the geometry of the active site. In the case of the glutamine amidotransferase family the glutamine binding site of GlcN-6-P synthase fits a different region of the glutamine conformational space than other amidotransferases. Detailed analysis of the interaction pattern for the best known, so far, inhibitor of the sugar isomerising domain, namely 2-amino-2-deoxy-d-glucitol-6-phosphate (ADGP), allowed us to suggest changes in the structure of the inhibitor that should improve the interaction pattern. The novel ligand was designed and synthesised. Biological experiments confirmed our predictions. The new compound named ADMP is a much better inhibitor of glucosamine-6-phosphate synthase than ADGP.
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