Publications by authors named "Goffin C"

During the COVID-19 pandemic, people across the globe have been exposed to large amounts of statistical data. Previous studies have shown that individuals' mathematical understanding of health-related information affects their attitudes and behaviours. Here, we investigate the relation between (i) basic numeracy, (ii) COVID-19 health numeracy, and (iii) COVID-19 health-related attitudes and behaviours.

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How are number symbols (e.g., Arabic digits) represented in the brain? Functional resonance imaging adaptation (fMRI-A) research has indicated that the intraparietal sulcus (IPS) exhibits a decrease in activation with the repeated presentation of the same number, that is followed by a rebound effect with the presentation of a new number.

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A key question in the field of numerical cognition is how the human brain represents numerical symbols (e.g., Arabic digits).

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A growing body of evidence from functional Magnetic Resonance Imaging adaptation (fMRIa) has implicated the left intraparietal sulcus (IPS) as a crucial brain region representing the semantic of number symbols. However, it is currently unknown to what extent the left IPS brain activity can be generalized across modalities (e.g.

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Despite the normal mean intracranial pressure in normal pressure hydrocephalus, the cerebral ventricles enlarge. Many hypotheses exist as to why, and these have lately been investigated in simulation. These can be grouped into one of two categories: 1) Tissue damage is caused by a transmantle pressure gradient widening the ventricles mechanically.

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In the field of numerical cognition, ordinality, or the sequence of numerals, has received much less attention than cardinality, or the number of items in a set. Therefore it is unclear whether the numerical effects generated from ordinality and cardinality tasks are associated, and whether they relate to math achievement and more domain-general variables in similar ways. To address these questions, sixty adults completed ordinality, cardinality, visual-spatial working memory, inhibitory control and math achievement tasks.

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The way the human brain constructs representations of numerical symbols is poorly understood. While increasing evidence from neuroimaging studies has indicated that the intraparietal sulcus (IPS) becomes increasingly specialized for symbolic numerical magnitude representation over developmental time, the extent to which these changes are associated with age-related differences in symbolic numerical magnitude representation or with developmental changes in non-numerical processes, such as response selection, remains to be uncovered. To address these outstanding questions we investigated developmental changes in the cortical representation of symbolic numerical magnitude in 6- to 14-year-old children using a passive functional magnetic resonance imaging adaptation design, thereby mitigating the influence of response selection.

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Hydrocephalus is characterized by an excessive accumulation of cerebrospinal fluid (CSF). Therapeutically, an artificial pressure relief valve (so-called shunt) is implanted which opens in case of increased intracranial pressure (ICP) and drains CSF into another body compartment. Today, available shunts are of a mechanical nature and drainage depends on the pressure drop across the shunt.

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The intracranial pressure (ICP) waveform contains important diagnostic information. Changes in ICP are associated with changes of the pulse waveform. This change has explicitly been observed in 13 infusion tests by analyzing 100 Hz ICP data.

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Hydrocephalus patients with increased intracranial pressure are generally treated by draining cerebrospinal fluid (CSF) into the abdomen through an implanted shunt with a passive differential pressure valve. To perfectly adapt the valve's opening pressure to the patient's need, more information on the acutal pressure across the valve in everyday life actions like walking, eating, sleeping etc. is necessary.

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Injury to the axillary artery is a rare complication of anterior shoulder dislocation. Open surgical repair is technically demanding because of the anatomical position of the vessel and the propensity for concomitant injuries. Standard surgical exposure techniques involve extensive dissection, including a combination of supraclavicular or infraclavicular incision, median sternotomy, and thoracotomy causing significant morbidity and mortality rates.

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In efforts to find new bioactive beta-lactamase inhibitors, this study investigated 16 Cameroonian plants belonging to 10 families which were evaluated for anti-beta-lactamase activity. The investigation showed that extracts 2, 6, 3 and 5 of the 16 plants investigated presented interesting in vitro beta-lactamase inhibition (over 90%), respectively, of the beta-lactamases TEM-1, OXA-10, IMP-1 and P99. These extracts were from Mammea africana (all beta-lactamases), Garcinia lucida, G.

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The bacterial acyltransferases of the SxxK superfamily vary enormously in sequence and function, with conservation of particular amino acid groups and all-alpha and alpha/beta folds. They occur as independent entities (free-standing polypeptides) and as modules linked to other polypeptides (protein fusions). They can be classified into three groups.

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Bacillus subtilis DppA is a binuclear zinc-dependent, D-specific aminopeptidase. The X-ray structure of the enzyme has been determined at 2.4 A resolution by a three-wavelength MAD experiment.

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Different strains of Bacillus were screened for their ability to hydrolyse D-alanyl-p-nitroanilide. Activity was detected in Bacillus pumilus, Bacillus brevis, Bacillus licheniformis 749I and Bacillus subtilis 168. The last strain was the best producer and was selected for the production and purification of the enzyme.

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Two new enzymes which hydrolyse D-alanyl-p-nitroanilide have been detected in Ochrobactrum anthropi LMG7991 extracts. The first enzyme, DmpB, was purified to homogeneity and found to be homologous to the Dap protein produced by O. anthropi SCRC C1-38 (ATCC49237).

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The DmpA (d-aminopeptidase A) protein produced by Ochrobactrum anthropi hydrolyses p-nitroanilide derivatives of glycine and d-alanine more efficiently than that of l-alanine. When regular peptides are utilized as substrates, the enzyme behaves as an aminopeptidase with a preference for N-terminal residues in an l configuration, thus exemplifying an interesting case of stereospecificity reversal. The best-hydrolysed substrate is l-Ala-Gly-Gly, but tetra- and penta-peptides are also efficiently hydrolysed.

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The monofunctional penicillin-binding DD-peptidases and penicillin-hydrolyzing serine beta-lactamases diverged from a common ancestor by the acquisition of structural changes in the polypeptide chain while retaining the same folding, three-motif amino acid sequence signature, serine-assisted catalytic mechanism, and active-site topology. Fusion events gave rise to multimodular penicillin-binding proteins (PBPs). The acyl serine transferase penicillin-binding (PB) module possesses the three active-site defining motifs of the superfamily; it is linked to the carboxy end of a non-penicillin-binding (n-PB) module through a conserved fusion site; the two modules form a single polypeptide chain which folds on the exterior of the plasma membrane and is anchored by a transmembrane spanner; and the full-size PBPs cluster into two classes, A and B.

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The 49 kDa penicillin-binding protein (PBP) of Mycobacterium smegmatis catalyses the hydrolysis of the peptide or S-ester bond of carbonyl donors R1-CONH-CHR2-COX-CHR2-COO- (where X is NH or S). In the presence of a suitable amino acceptor, the reaction partitions between the transpeptidation and hydrolysis pathways, with the amino acceptor, behaving as a simple alternative nucleophile at the level of the acyl-enzyme. By virtue of its N-terminal sequence similarity, the 49 kDa PBP represents one of the class of monofunctional low-molecular-mass PBPs.

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The ftsI-encoded multimodular class B penicillin-binding protein 3 (PBP3) is a key element of the cell septation machinery of Escherichia coli. Altered ftsI genes were overexpressed, and the gene products were analyzed with respect to the level of production, stability, penicillin affinity, and cell septation activity. In contrast to the serine beta-lactamases and low-molecular-mass PBPs which are autonomous folding entities, the S-259-to-V-577 penicillin-binding module of M-1-to-V-577 PBP3 lacks the amino acid sequence information for correct folding.

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As the protein sequence and structure databases expand, the relationships between proteins, the notion of protein superfamily, and the driving forces of evolution are better understood. Key steps of the synthesis of the bacterial cell wall peptidoglycan are revisited in light of these advances. The reactions through which the D-alanyl-D-alanine depeptide is formed, utilized, and hydrolyzed and the sites of action of the glycopeptide and beta-lactam antibiotics illustrate the concept according to which new enzyme functions evolve as a result of tinkering of existing proteins.

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