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- Ongena, J., et al.
(författare)
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Recent progress on JET towards the ITER reference mode of operation at high density
- 2001
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Ingår i: Plasma Physics and Controlled Fusion. - 0741-3335 .- 1361-6587. ; 43, s. A11-A30
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Tidskriftsartikel (refereegranskat)abstract
- Recent progress towards obtaining high density and high confinement in JET as required for the ITER reference scenario at Q = 10 is summarized. Plasmas with simultaneous confinement H-98(y.2) = 1 and densities up to n/n(Gw) similar to 1 are now routinely obtained. This has been possible (i) by using plasmas at high (delta similar to 0.5) and medium (delta similar to 0.3-0.4) triangularity with sufficient heating power to maintain Type I ELMs, (ii) with impurity seeded plasmas at high (delta similar to 0.5) and low (delta less than or equal to 0.2) triangularity, (iii) with an optimized pellet injection sequence, maintaining the energy confinement and raising the density, and (iv) by carefully tuning the gas puff rate leading to plasmas with peaked density profiles and good confinement at long time scales. These high performance discharges exhibit Type I ELMs, with a new and more favourable behaviour observed at high densities, requiring further studies. Techniques for a possible mitigation of these ELMs are discussed, and first promising results are obtained with impurity seeding in discharges at high triangularity. Scaling studies using the new data of this year show a strong dependence of confinement on upper triangularity, density and proximity to the Greenwald limit. Observed MHD instabilities and methods to avoid these in high density and high confinement plasmas are discussed.
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| 3. |
- Imamura, T, et al.
(författare)
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Y box-binding protein-1 binds preferentially to single-stranded nucleic acids and exhibits 3'-->5' exonuclease activity.
- 2001
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Ingår i: Nucleic acids research. - 1362-4962. ; 29:5, s. 1200-7
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Tidskriftsartikel (refereegranskat)abstract
- We have previously shown that Y box-binding protein-1 (YB-1) binds preferentially to cisplatin-modified Y box sequences. Based on structural and biochemical data, we predicted that this protein binds single-stranded nucleic acids. In the present study we confirmed the prediction and also discovered some unexpected functional features of YB-1. We found that the cold shock domain of the protein is necessary but not sufficient for double-stranded DNA binding while the C-tail domain interacts with both single-stranded DNA and RNA independently of the cold shock domain. In an in vitro translation system the C-tail domain of the protein inhibited translation but the cold shock domain did not. Both in vitro pull-down and in vivo co-immunoprecipitation assays revealed that YB-1 can form a homodimer. Deletion analysis mapped the C-tail domain of the protein as the region of homodimerization. We also characterized an intrinsic 3'-->5' DNA exonuclease activity of the protein. The region between residues 51 and 205 of its 324-amino acid extent is required for full exonuclease activity. Our findings suggest that YB-1 functions in regulating DNA/RNA transactions and that these actions involve different domains.
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