Publications by authors named "M S Tomek"

The article deals with the issue of evaluation of the causes of accidents at level crossings in the Czech Republic, including the prediction of the development and proposals of measures for prevention and thus reduction of their number. The goal of this work is to verify the hypothesis that the number of accidents at level crossings in the Czech Republic is decreasing. The authors use available data from the Ministry of Transport and process statistical data for ten years (2013-2022) of railway operation.

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Introduction: Degradation of host proteins by bacterial proteases leads to the subversion of the host response and disruption of oral epithelial integrity, which is considered an essential factor in the progression of periodontitis. High-temperature requirement A (HtrA) protease, which is critical for bacterial survival and environmental adaptation, is found in several oral bacteria, including the periodontal pathogen . This study investigated the proteolytic activity of HtrA from and its ability to modulate the host response.

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and target distinct virulence factors bearing a structurally conserved C-terminal domain (CTD) to the type IX protein secretion system (T9SS). The T9SS comprises an outer membrane translocation complex which works in concert with a signal peptidase for CTD cleavage. Among prominent T9SS cargo linked to periodontal diseases are the TfsA and TfsB components of cell surface (S-) layer, the bacterium's BspA surface antigen and a set of cysteine proteinases (gingipains) from .

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Diverse members of the Bacteroidetes phylum have general protein -glycosylation systems that are essential for processes such as host colonization and pathogenesis. Here, we analyzed the function of a putative fucosyltransferase (FucT) family that is widely encoded in Bacteroidetes protein -glycosylation genetic loci. We studied the FucT orthologs of three Bacteroidetes species-, , and .

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Background: The Gram-negative oral pathogen Tannerella forsythia strictly depends on the external supply of the essential bacterial cell wall sugar N-acetylmuramic acid (MurNAc) for survival because of the lack of the common MurNAc biosynthesis enzymes MurA/MurB. The bacterium thrives in a polymicrobial biofilm consortium and, thus, it is plausible that it procures MurNAc from MurNAc-containing peptidoglycan (PGN) fragments (muropeptides) released from cohabiting bacteria during natural PGN turnover or cell death. There is indirect evidence that in T.

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