Positive exchange bias in ferromagnetic La0.67Sr0.33MnO3 / SrRuO3 bilayers

Epitaxial La0.67Sr0.33MnO3 (LSMO)/ SrRuO3 (SRO) ferromagnetic bilayers have been grown on (001) SrTiO3 (STO) substrates by pulsed laser deposition with atomic layer control. We observe a shift in the magnetic hysteresis loop of the LSMO layer in the same direction as the applied biasing field (positive exchange bias). The effect is not present above the Curie temperature of the SRO layer (), and its magnitude increases rapidly as the temperature is lowered below . The direction of the shift is consistent with an antiferromagnetic exchange coupling between the ferromagnetic LSMO layer and the ferromagnetic SRO layer. We propose that atomic layer charge transfer modifies the electronic state at the interface, resulting in the observed antiferromagnetic interfacial exchange coupling.Comment: accepted to Applied Physics Letter

Possible DDˉD\bar{D} and BBˉB\bar{B} Molecular states in a chiral quark model

We perform a systematic study of the bound state problem of $D\bar{D}$ and $B\bar{B}$ systems by using effective interaction in our chiral quark model. Our results show that both the interactions of $D\bar{D}$ and $B\bar{B}$ states are attractive, which consequently result in $I^G(J^{PC})=0^+(0^{++})$ $D\bar{D}$ and $B\bar{B}$ bound states.Comment: arXiv admin note: substantial text overlap with arXiv:1204.395

SUMO Modification Stabilizes Enterovirus 71 Polymerase 3D To Facilitate Viral Replication.

Accumulating evidence suggests that viruses hijack cellular proteins to circumvent the host immune system. Ubiquitination and SUMOylation are extensively studied posttranslational modifications (PTMs) that play critical roles in diverse biological processes. Cross talk between ubiquitination and SUMOylation of both host and viral proteins has been reported to result in distinct functional consequences. Enterovirus 71 (EV71), an RNA virus belonging to the family Picornaviridae, is a common cause of hand, foot, and mouth disease. Little is known concerning how host PTM systems interact with enteroviruses. Here, we demonstrate that the 3D protein, an RNA-dependent RNA polymerase (RdRp) of EV71, is modified by small ubiquitin-like modifier 1 (SUMO-1) both during infection and in vitro Residues K159 and L150/D151/L152 were responsible for 3D SUMOylation as determined by bioinformatics prediction combined with site-directed mutagenesis. Also, primer-dependent polymerase assays indicated that mutation of SUMOylation sites impaired 3D polymerase activity and virus replication. Moreover, 3D is ubiquitinated in a SUMO-dependent manner, and SUMOylation is crucial for 3D stability, which may be due to the interplay between the two PTMs. Importantly, increasing the level of SUMO-1 in EV71-infected cells augmented the SUMOylation and ubiquitination levels of 3D, leading to enhanced replication of EV71. These results together suggested that SUMO and ubiquitin cooperatively regulated EV71 infection, either by SUMO-ubiquitin hybrid chains or by ubiquitin conjugating to the exposed lysine residue through SUMOylation. Our study provides new insight into how a virus utilizes cellular pathways to facilitate its replication. IMPORTANCE: Infection with enterovirus 71 (EV71) often causes neurological diseases in children, and EV71 is responsible for the majority of fatalities. Based on a better understanding of interplay between virus and host cell, antiviral drugs against enteroviruses may be developed. As a dynamic cellular process of posttranslational modification, SUMOylation regulates global cellular protein localization, interaction, stability, and enzymatic activity. However, little is known concerning how SUMOylation directly influences virus replication by targeting viral polymerase. Here, we found that EV71 polymerase 3D was SUMOylated during EV71 infection and in vitro Moreover, the SUMOylation sites were determined, and in vitro polymerase assays indicated that mutations at SUMOylation sites could impair polymerase synthesis. Importantly, 3D is ubiquitinated in a SUMOylation-dependent manner that enhances the stability of the viral polymerase. Our findings indicate that the two modifications likely cooperatively enhance virus replication. Our study may offer a new therapeutic strategy against virus replication

The signal of Z±(4430)Z^\pm(4430) in nucleon-antinucleon scattering

We study the production of $Z^\pm(4430)$ at a nucleon-antinucleon scattering experiment. Considering the PANDA experiment to be an ideal platform to explore the production of the charmonium and charmonim-like states, we suggest the forthcoming PANDA experiment to pay attention to the production of $Z^\pm(4430)$.Comment: 6 pages, 15 figures. Published version in EPJ

Electric-field-induced phase transition of <001> oriented Pb(Mg1/3Nb2/3)O3-PbTiO3 single crystals

oriented 0.7Pb(Mg1/3Nb2/3)O3-0.3PbTiO3 single crystals were poled under different electric fields, i.e. Epoling=4 kV/cm and Epoling=13 kV/cm. In addition to the temperature-dependent dielectric constant measurement, X-ray diffraction was also used to identify the poling-induced phase transitions. Results showed that the phase transition significantly depends on the poling intensity. A weaker field (Epoling=4 kV/cm) can overcome the effect of random internal field to perform the phase transition from rhombohedral ferroelectric state with short range ordering (microdomain) FESRO to rhombohedral ferroelectric state with long range ordering (macrodomain) FElRO. But the rhombohedral ferroelectric to tetragonal ferroelectric phase transition originating from to polarization rotation can only be induced by a stronger field (Epoling=13 kV/cm). The sample poled at Epoling=4 kV/cm showed higher piezoelectric constant, d33>1500 pC/N, than the sample poled at Epoling=13 kV/cm.Comment: 7 pages, 2 figure