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Optimisation de l’identification et du dénombrement du microphytoplancton avec le système couplé de numérisation et d’analyse d’images FlowCAM – Zoo/PhytoImage (système innovant). Action 9 – Livrable 3. Evolution du matériel de numérisation : prototype FastCAM et perspectives. Rapport final, février 2016 ArchiMer
Colas, Florent; Tardivel, Morgan; Evrard, Justine; Forest, Bertrand; Crassous, Marie-pierre; Lunven, Michel; Danielou, Marie-madeleine.
This deliverable contains all development work of the FastCAM, new tool for fast imaging of the phytoplankton, which took place in 2015. It consists of: One report of the FastCAM and its comparison with the FlowCAM presentation: The FlowCAM enables the digitalization of a sample of phytoplankton with X10 and X 4 magnifications. The first allows a better morphological description and therefore a higher taxonomic resolution but with a longer scan time (16 X). Thus, for routine analyses, only scanning at 4 X is possible. A considerable gain would be able to do an acquisition to the magnification 10 X with a time of analysis more short, comparable to 4 X. A fast flow imaging system has therefore developed in this sense. He was called FastCAM. The system is...
Tipo: Text Palavras-chave: FlowCAM; FastCAM; Imagerie rapide; Phytoplancton; REPHY.; FlowCAM; FastCAM; Fast imaging; Phytoplankton; REPHY.
Ano: 2016 URL: http://archimer.ifremer.fr/doc/00363/47420/47425.pdf
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Protein Folding Activity of the Ribosome is involved in Yeast Prion Propagation ArchiMer
Blondel, Marc; Soubigou, Flavie; Evrard, Justine; Phu Hai Nguyen,; Hasin, Naushaba; Chedin, Stephane; Gillet, Reynald; Contesse, Marie-astrid; Friocourt, Gaelle; Stahl, Guillaume; Jones, Gary W.; Voisset, Cecile.
6AP and GA are potent inhibitors of yeast and mammalian prions and also specific inhibitors of PFAR, the protein-folding activity borne by domain V of the large rRNA of the large subunit of the ribosome. We therefore explored the link between PFAR and yeast prion [PSI+] using both PFAR-enriched mutants and site-directed methylation. We demonstrate that PFAR is involved in propagation and de novo formation of [PSI+]. PFAR and the yeast heat-shock protein Hsp104 partially compensate each other for [PSI+] propagation. Our data also provide insight into new functions for the ribosome in basal thermotolerance and heat-shocked protein refolding. PFAR is thus an evolutionarily conserved cell component implicated in the prion life cycle, and we propose that it...
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Ano: 2016 URL: https://archimer.ifremer.fr/doc/00358/46931/46834.pdf
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