Protection of the 6 T YBCO insert in the 13 T Nb3Sn Fresca II dipole

In the EuCARD project, we aim to construct a dipole magnet in YBCO producing 6 T in the background field of a 13 T Nb3Sn dipole FRESCA II. This paper reviews the quench analysis and protection of the YBCO coil. In addition, a recommendation for the protection system of the YBCO coil is presented.Comment: 6 pages, Contribution to WAMSDO 2013: Workshop on Accelerator Magnet, Superconductor, Design and Optimization; 15 - 16 Jan 2013, CERN, Geneva, Switzerlan

Normal-superconducting transition induced by high current densities in YBa2Cu3O7-d melt-textured samples and thin films: Similarities and differences

Current-voltage characteristics of top seeded melt-textured YBa2Cu3O7-d are presented. The samples were cut out of centimetric monoliths. Films characteristics were also measured on microbridges patterned on thin films grown by dc sputtering. For both types of samples, a quasi-discontinuity or quenching was observed for a current density J* several times the critical current density Jc. Though films and bulks much differ in their magnitude of both Jc and J*, a proposal is made as to a common intrinsic origin of the quenching phenomenon. The unique temperature dependence observed for the ratio J*/Jc, as well as the explanation of the pre-quenching regime in terms of a single dissipation model lend support to our proposal.Comment: 10 pages, 10 figures, submitted to Physical Review

HTS Dipole Insert Developments

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Isolation of Proteinase K-Sensitive Prions Using Pronase E and Phosphotungstic Acid

Disease-related prion protein, PrPSc, is classically distinguished from its normal cellular precursor, PrPC, by its detergent insolubility and partial resistance to proteolysis. Molecular diagnosis of prion disease typically relies upon detection of protease-resistant fragments of PrPSc using proteinase K, however it is now apparent that the majority of disease-related PrP and indeed prion infectivity may be destroyed by this treatment. Here we report that digestion of RML prion-infected mouse brain with pronase E, followed by precipitation with sodium phosphotungstic acid, eliminates the large majority of brain proteins, including PrPC, while preserving >70% of infectious prion titre. This procedure now allows characterization of proteinase K-sensitive prions and investigation of their clinical relevance in human and animal prion disease without being confounded by contaminating PrPC

Prominent and Persistent Extraneural Infection in Human PrP Transgenic Mice Infected with Variant CJD

Background. The evolution of the variant Creutzfeldt-Jakob disease (vCJD) epidemic is hazardous to predict due to uncertainty in ascertaining the prevalence of infection and because the disease might remain asymptomatic or produce an alternate, sporadic-like phenotype. Methodology/Principal Findings. Transgenic mice were produced that overexpress human prion protein with methionine at codon 129, the only allele found so far in vCJD-affected patients. These mice were infected with prions derived from variant and sporadic CJD (sCJD) cases by intracerebral or intraperitoneal route, and transmission efficiency and strain phenotype were analyzed in brain and spleen. We showed that i) the main features of vCJD infection in humans, including a prominent involvement of the lymphoid tissues compared to that in sCJD infection were faithfully reproduced in such mice; ii) transmission of vCJD agent by intracerebral route could lead to the propagation of either vCJD or sCJD-like prion in the brain, whereas vCJD prion was invariably propagated in the spleen, iii) after peripheral exposure, inefficient neuroinvasion was observed, resulting in an asymptomatic infection with life-long persistence of vCJD prion in the spleen at stable and elevated levels. Conclusion/Significance. Our findings emphasize the possibility that human-to-human transmission of vCJD might produce alternative neuropathogical phenotypes and that lymphoid tissue examination of CJD cases classified as sporadic might reveal an infection by vCJD-type prions. They also provide evidence for the strong propensity of this agent to establish long-lasting, subclinical vCJD infection of lymphoreticular tissues, thus amplifying the risk for iatrogenic transmission