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Effects of electrode polarity on filament ruptures during unipolar resistance switchings
Jay Hyun Jo,이신범,Jonathan Hanjin Lee,장서형,채승철,정창욱 한국물리학회 2010 Current Applied Physics Vol.10 No.3
It has been argued that in unipolar resistance switching of Pt/TiO2/Pt capacitors, conducting filaments should propagate from the cathode interface, and the rupture and recovery of the filaments should occur near the anode interface [Kim et al., Appl. Phys. Lett. 91 (2007) 012907]. We investigated whether this ‘‘anode-interface localized filamentary mechanism” holds for Pt/NiO/Pt capacitors. We examined how the electrode polarity affects the rupturing of the conducting filaments in unipolar resistance switching by performing resistance switching measurements on 246 NiO capacitors. We found some dependencies on electrode polarity; however, they were not consistent with the anode-interface localized filamentary mechanism. We also found that Joule heating affects the rupturing process, suggesting that the weakest link of conducting filaments in NiO thin films plays an important role during the rupturing process.
Mitochondrial chaperone HSP ‐60 regulates anti‐bacterial immunity via p38 MAP kinase signaling
Jeong, Dae‐,Eun,Lee, Dongyeop,Hwang, Sun‐,Young,Lee, Yujin,Lee, Jee‐,Eun,Seo, Mihwa,Hwang, Wooseon,Seo, Keunhee,Hwang, Ara B,Artan, Murat,Son, Heehwa G,Jo, Jay‐,Hyun,Baek, Haes Published for the European Molecular Biology Organ 2017 The EMBO journal Vol.36 No.8
<P>Mitochondria play key roles in cellular immunity. How mitochondria contribute to organismal immunity remains poorly understood. Here, we show that HSP-60/HSPD1, a major mitochondrial chaperone, boosts anti-bacterial immunity through the up-regulation of p38 MAP kinase signaling. We first identify 16 evolutionarily conserved mitochondrial components that affect the immunity of Caenorhabditis elegans against pathogenic Pseudomonas aeruginosa (PA14). Among them, the mitochondrial chaperone HSP-60 is necessary and sufficient to increase resistance to PA14. We show that HSP-60 in the intestine and neurons is crucial for the resistance to PA14. We then find that p38 MAP kinase signaling, an evolutionarily conserved anti-bacterial immune pathway, is down-regulated by genetic inhibition of hsp-60, and up-regulated by increased expression of hsp-60. Overexpression of HSPD1, the mammalian ortholog of hsp-60, increases p38 MAP kinase activity in human cells, suggesting an evolutionarily conserved mechanism. Further, cytosol-localized HSP-60 physically binds and stabilizes SEK-1/MAP kinase kinase 3, which in turn up-regulates p38 MAP kinase and increases immunity. Our study suggests that mitochondrial chaperones protect host eukaryotes from pathogenic bacteria by up-regulating cytosolic p38 MAPK signaling.</P>