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SUPERCRITICAL WATER LOOP DESIGN FOR CORROSION AND WATER CHEMISTRY TESTS UNDER IRRADIATION
Ruzickova, Mariana,Hajek, Petr,Smida, Stepan,Vsolak, Rudolf,Petr, Jan,Kysela, Jan Korean Nuclear Society 2008 Nuclear Engineering and Technology Vol.40 No.2
An experimental loop operating with water at supercritical conditions(25MPa, $600^{\circ}C$ in the test section) is designed for operation in the research reactor LVR-15 in UJV Rez, Czech Republic. The loop should serve as an experimental facility for corrosion tests of materials for in-core as well as out-of-core structures, for testing and optimization of suitable water chemistry for a future HPLWR and for studies of radiolysis of water at supercritical conditions, which remains the domain where very few experimental data are available. At present, final necessary calculations(thermalhydraulic, neutronic, strength) are being performed on the irradiation channel, which is the most challenging part of the loop. The concept of the primary and auxiliary circuits has been completed. The design of the loop shall be finished in the course of the year 2007 to start the construction, out-of-pile testing to verify proper functioning of all systems and as such to be ready for in-pile tests by the end of the HPLWR Phase 2 European project by the end of 2009.
Protein N-Glycosylation, Protein Folding, and Protein Quality Control
Jürgen Roth,Christian Zuber,박수진,Insook Jang,Yangsin Lee,Katarina Gaplovska Kysela,Valérie Le Fourn,Roger Santimaria,Bruno Guhl,조진원 한국분자세포생물학회 2010 Molecules and cells Vol.30 No.6
Quality control of protein folding represents a funda-mental cellular activity. Early steps of protein N-glycosylation involving the removal of three glucose and some specific mannose residues in the endoplasmic reticulum have been recognized as being of importance for protein quality control. Specific oligosaccharide structures resulting from the oligosaccharide processing may represent a glycocode promoting productive protein folding, whereas others may represent glyco-codes for routing not correctly folded proteins for dislocation from the endoplasmic reticulum to the cytosol and subsequent degradation. Although quality control of protein folding is essential for the proper functioning of cells, it is also the basis for protein folding disorders since the recognition and elimination of non-native conformers can result either in loss-of-function or pathological-gain-of-function. The machinery for protein folding control represents a prime example of an intricate interactome present in a single organelle, the endoplasmic reticulum. Here, current views of mechanisms for the recognition and retention leading to productive protein folding or the eventual elimination of misfolded glycoproteins in yeast and mammalian cells are reviewed.
Protein N-Glycosylation, Protein Folding, and Protein Quality Control
Roth, Jurgen,Zuber, Christian,Park, Su-Jin,Jang, In-Sook,Lee, Yang-Sin,Kysela, Katarina Gaplovska,Le Fourn, Valerie,Santimaria, Roger,Guhl, Bruno,Cho, Jin-Won Korean Society for Molecular and Cellular Biology 2010 Molecules and cells Vol.30 No.6
Quality control of protein folding represents a fundamental cellular activity. Early steps of protein N-glycosylation involving the removal of three glucose and some specific mannose residues in the endoplasmic reticulum have been recognized as being of importance for protein quality control. Specific oligosaccharide structures resulting from the oligosaccharide processing may represent a glycocode promoting productive protein folding, whereas others may represent glyco-codes for routing not correctly folded proteins for dislocation from the endoplasmic reticulum to the cytosol and subsequent degradation. Although quality control of protein folding is essential for the proper functioning of cells, it is also the basis for protein folding disorders since the recognition and elimination of non-native conformers can result either in loss-of-function or pathological-gain-of-function. The machinery for protein folding control represents a prime example of an intricate interactome present in a single organelle, the endoplasmic reticulum. Here, current views of mechanisms for the recognition and retention leading to productive protein folding or the eventual elimination of misfolded glycoproteins in yeast and mammalian cells are reviewed.