Psychological particularities and personal representations of subjects undergoing to genetic testing for hereditary colonic cancer

info:eu-repo/semantics/publishe

Quel accompagnement pour les consultants en oncogénétique et dans quel cas ?Intérêt d’une approche intra-individuelle sur la question de l’émotionalité.

info:eu-repo/semantics/publishe

Comparaison des effets psychologiques des tests génétiques dans les formes héréditaires de cancer du sein/ovaire et du syndrome de Lynch: Résultats d’une étude multicentrique au sein du cancéropôle Nord-ouest

info:eu-repo/semantics/publishe

Place de l’alexithymie au cours des réponses émotionnelles consécutives de l’annonce d’un résultat génétique prédisposant aux cancers familiaux héréditaires: Interet des modèles statistiques à faibles contraintes

info:eu-repo/semantics/publishe

Comment comprendre la détresse liée au dépistage génétique lorsque les porteurs d’une mutation prédisposant aux cancers familiaux sein-ovaire et colon n’observent pas les memes patterns de réponses émotionnelles ?Rôle de la régulation et du partage social des émotions

info:eu-repo/semantics/publishe

How may we understood genetic testing distress experience when HBOC and HNPCC did not show the same emotional response when mutation carrier ?

avec le groupe oncogénétique clinique du canceropole Nord-ouestinfo:eu-repo/semantics/publishe

Folding of class A beta-lactamases is rate-limited by peptide bond isomerization and occurs via parallel pathways.

Class A beta-lactamases (M(r) approximately 29000) provide good models for studying the folding mechanism of large monomeric proteins. In particular, the highly conserved cis peptide bond between residues 166 and 167 at the active site of these enzymes controls important steps in their refolding reaction. In this work, we analyzed how conformational folding, reactivation, and cis/trans peptide bond isomerizations are interrelated in the folding kinetics of beta-lactamases that differ in the nature of the cis peptide bond, which involves a Pro167 in the BS3 and TEM-1 enzyme, a Leu167 in the NMCA enzyme, and which is missing in the PER-1 enzyme. The analysis of folding by spectroscopic probes and by the regain of enzymatic activity in combination with double-mixing procedures indicates that conformational folding can proceed when the 166-167 bond is still in the incorrect trans form. The very slow trans --> cis isomerization of the Glu166-Xaa167 peptide bond, however, controls the final step of folding and is required for the regain of the enzymatic activity. This very slow phase is absent in the refolding of PER-1, in which the Glu166-Ala167 peptide bond is trans. The double-mixing experiments revealed that a second slow kinetic phase is caused by the cis/trans isomerization of prolines that are trans in the folded proteins. The folding of beta-lactamases is best described by a model that involves parallel pathways. It highlights the role of peptide bond cis/trans isomerization as a kinetic determinant of folding