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Biomedical subjects

A Roelandt

Publications and source records attributed to A Roelandt.

3 recordsLinked to original sources
PubMed2002

[Criminal enquiry and determination of dental damage. Analysis of a prosthetic fracture following an accident].

When signing a legal insurance policy, one is not always aware of the seriousness of the reciprocal legal consequences. Physical injuries mainly involve civil procedures in spite of the fact that criminal proceedings are instituted in some cases. This article deals with the judicial inquiry concerning the notification of an accident with insurance claim. The object of this inquiry is a porcelain fracture caused by a so-called accident where verification becomes very complicated for the appointed experts. If diagnosis, anamnesis and the initial examination indicate possible fraud in the case, the expert's assessment for the insurer will rightly include the criminal section. What does this involve for the expert and his team? The violation of the public interest by making a false statement will result in the expert trying to reveal the truth instead of estimating the damage.

Accidents, Traffic↗
PubMed1994

Molecular characterization of the major outer-membrane protein OprF from plant root-colonizing Pseudomonas fluorescens.

N-terminal sequence analysis of peptides generated by proteolytic treatment of the Pseudomonas fluorescens OE 28.3 major outer-membrane protein OprF, embedded in outer membranes or present in whole cells, indicated a surface-exposed location for the proline-rich region of the protein. This region is absent from the P. aeruginosa and P. syringae OprFs. Evidence was obtained for the presence of additional exposed but less accessible regions in the carboxy half of OprF. Four OprF-specific monoclonal antibodies were all directed to the C-terminal part of the protein but did not recognize a surface-exposed epitope as shown by flow cytometry. Our data support the model previously proposed for P. aeruginosa OprF in which the entire protein is embedded in the outer membrane, unlike the topology proposed for the major outer-membrane protein from Escherichia coli, OmpA, whose carboxy half resides in the periplasmic space. For six other P. fluorescens strains producing OprF proteins with different isoelectric points, the primary structure was determined by sequence analysis of the PCR-amplified oprF genes. The proline-rich domain represented the most conserved region of the different P. fluorescens OprFs. Based on the sequence of its oprF gene, it was shown that the mushroom pathogen P. tolaasii is quite closely related to P. fluorescens. Comparative sequence analysis further showed that the carboxy half of OprF contains a sequence motif that is well conserved in the enterobacterial OmpA proteins but is also present in a number of other outer-membrane proteins, including peptidoglycan-associated lipoproteins.

Amino Acid Sequence↗