Increasing the performance of the superconducting spin valve using a Heusler alloy

We have studied superconducting properties of the spin-valve thin layer heterostructures CoO$_x$/F1/Cu/F2/Cu/Pb where the ferromagnetic F1 layer was standardly made of Permalloy whereas for the F2 layer we have taken a specially prepared film of the Heusler alloy Co$_2$Cr$_{1-x}$Fe$_x$Al with a small degree of spin polarization of the conduction band. The heterostructures demonstrate a significant superconducting spin-valve effect, i.e. a complete switching on and off of the superconducting current flowing through the system by manipulating the mutual orientations of the magnetization of the F1 and F2 layers. The magnitude of the effect is doubled in comparison with the previously studied analogous multilayers with the F2 layer made of the strong ferromagnet Fe. Theoretical analysis shows that a drastic enhancement of the switching effect is due to a smaller exchange field in the heterostructure coming from the Heusler film as compared to Fe. This enables to approach almost ideal theoretical magnitude of the switching in the Heusler-based multilayer with the F2 layer thickness of $\sim 1$\,nm

PML–RARA-RXR Oligomers Mediate Retinoid and Rexinoid/cAMP Cross-Talk in Acute Promyelocytic Leukemia Cell Differentiation

PML–RARA was proposed to initiate acute promyelocytic leukemia (APL) through PML–RARA homodimer–triggered repression. Here, we examined the nature of the PML–RARA protein complex and of its DNA targets in APL cells. Using a selection/amplification approach, we demonstrate that PML–RARA targets consist of two AGGTCA elements in an astonishing variety of orientations and spacings, pointing to highly relaxed structural constrains for DNA binding and identifying a major gain of function of this oncogene. PML–RARA-specific response elements were identified, which all conveyed a major transcriptional response to RA only in APL cells. In these cells, we demonstrate that PML–RARA oligomers are complexed to RXR. Directly probing PML–RARA function in APL cells, we found that the differentiation enhancer cyclic AMP (cAMP) boosted transcriptional activation by RA. cAMP also reversed the normal silencing (subordination) of the transactivating function of RXR when bound to RARA or PML–RARA, demonstrating that the alternate rexinoid/cAMP-triggered APL differentiation pathway also activates PML–RARA targets. Finally, cAMP restored both RA-triggered differentiation and PML–RARA transcriptional activation in mutant RA-resistant APL cells. Collectively, our findings directly demonstrate that APL cell differentiation parallels transcriptional activation through PML–RARA-RXR oligomers and that those are functionally targeted by cAMP, identifying this agent as another oncogene-targeted therapy

HU binds and folds single-stranded DNA

The nucleoid-associated protein HU plays an important role in bacterial nucleoid organization and is involved in numerous processes including transposition, recombination and DNA repair. We show here that HU binds specifically DNA containing mismatched region longer than 3 bp as well as DNA bulges. HU binds single-stranded DNA (ssDNA) in a binding mode that is reminiscent but different from earlier reported specific HU interactions with double-helical DNA lesions. An HU dimer requires 24 nt of ssDNA for initial binding, and 12 nt of ssDNA for each additional dimer binding. In the presence of equimolar amounts of HU dimer and DNA, the ssDNA molecule forms an U-loop (hairpin-like) around the protein, providing contacts with both sides of the HU body. This mode differs from the binding of the single-strand-binding protein (SSB) to ssDNA: in sharp contrast to SSB, HU binds ssDNA non-cooperatively and does not destabilize double-helical DNA. Furthermore HU has a strong preference for poly(dG), while binding to poly(dA) is the weakest. HU binding to ssDNA is probably important for its capacity to cover and protect bacterial DNA both intact and carrying lesions

Increasing the performance of a superconducting spin valve using a Heusler alloy

We have studied superconducting properties of spin-valve thin-layer heterostructures CoOx/F1/Cu/F2/Cu/Pb in which the ferromagnetic F1 layer was made of Permalloy while for the F2 layer we have taken a specially prepared film of the Heusler alloy Co2Cr1-xFexAl with a small degree of spin polarization of the conduction band. The heterostructures demonstrate a significant superconducting spin-valve effect, i.e., a complete switching on and offof the superconducting current flowing through the system by manipulating the mutual orientations of the magnetization of the F1 and F2 layers. The magnitude of the effect is doubled in comparison with the previously studied analogous multilayers with the F2 layer made of the strong ferromagnet Fe. Theoretical analysis shows that a drastic enhancement of the switching effect is due to a smaller exchange field in the heterostructure coming from the Heusler film as compared to Fe. This enables to approach an almost ideal theoretical magnitude of the switching in the Heusler-based multilayer with a F2 layer thickness of ca. 1 nm. © 2018 Kamashev et al

Electrical properties of heterointerfaces composed of complex ferroelectric oxides: an experimental investigation

The reported study was funded by RFBR according to the research project № 18-32-00595