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Thermal, Dielectric, and Magnetic Properties in Multiferroic Cu2.85Zn0.15Mo2O9
Haruhiko Kuroe,Kento Aoki,Ryusuke Itoh,Tomohiro Hosaka,Takuya Hasegawa,Suguru Hachiuma,Mitsuru Akaki,Hideki Kuwahara,Tomoyuki Sekine,Masashi Hase,Kunihiko Oka,Toshimitsu Ito,Hiroshi Eisaki 한국물리학회 2013 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.63 No.3
We study the effects of Zn substitution on single crystals of the low-dimensional multiferroicmaterial Cu3Mo2O9. We report the magnetic field-temperature phase diagram obtained from thetemperature and the magnetic field dependences of the specific heat, the dielectric constant, thedifferential magnetization, and the electric polarization-electric field curve in Cu2.85Zn0.15Mo2O9. We obtain three phases: a paraelectric and a ferroelectric phase, and a ferroelectric phase with alarge coercive electric field. The origin of the last one is discussed based on the charge redistributioneffect on a half-filled Mott insulator. In this phase, the Zn substitution induces a robust localizedferroelectric polarization that increases the coercive electric field.
Bin, Bum-Ho,Hojyo, Shintaro,Hosaka, Toshiaki,Bhin, Jinhyuk,Kano, Hiroki,Miyai, Tomohiro,Ikeda, Mariko,Kimura-Someya, Tomomi,Shirouzu, Mikako,Cho, Eun-Gyung,Fukue, Kazuhisa,Kambe, Taiho,Ohashi, Wakana BlackWell Publishing Ltd 2014 EMBO molecular medicine Vol.6 No.8
<P>The zinc transporter protein ZIP13 plays critical roles in bone, tooth, and connective tissue development, and its dysfunction is responsible for the spondylocheirodysplastic form of Ehlers-Danlos syndrome (SCD-EDS, OMIM 612350). Here, we report the molecular pathogenic mechanism of SCD-EDS caused by two different mutant ZIP13 proteins found in human patients: ZIP13<SUP>G64D</SUP>, in which Gly at amino acid position 64 is replaced by Asp, and ZIP13<SUP>ΔFLA</SUP>, which contains a deletion of Phe-Leu-Ala. We demonstrated that both the ZIP13<SUP>G64D</SUP> and ZIP13<SUP>ΔFLA</SUP> protein levels are decreased by degradation via the valosin-containing protein (VCP)-linked ubiquitin proteasome pathway. The inhibition of degradation pathways rescued the protein expression levels, resulting in improved intracellular Zn homeostasis. Our findings uncover the pathogenic mechanisms elicited by mutant ZIP13 proteins. Further elucidation of these degradation processes may lead to novel therapeutic targets for SCD-EDS.</P>