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Enhanced ferroelectricity in ultrathin films grown directly on silicon 期刊论文
NATURE, 2020, 580 (7804) : 478-+
作者:  Arnold, Fabian M.;  Weber, Miriam S.;  Gonda, Imre;  Gallenito, Marc J.;  Adenau, Sophia;  Egloff, Pascal;  Zimmermann, Iwan;  Hutter, Cedric A. J.;  Huerlimann, Lea M.;  Peters, Eike E.;  Piel, Joern;  Meloni, Gabriele;  Medalia, Ohad;  Seeger, Markus A.
收藏  |  浏览/下载:62/0  |  提交时间:2020/07/03

Ultrathin ferroelectric materials could potentially enable low-power perovskite ferroelectric tetragonality logic and nonvolatile memories(1,2). As ferroelectric materials are made thinner, however, the ferroelectricity is usually suppressed. Size effects in ferroelectrics have been thoroughly investigated in perovskite oxides-the archetypal ferroelectric system(3). Perovskites, however, have so far proved unsuitable for thickness scaling and integration with modern semiconductor processes(4). Here we report ferroelectricity in ultrathin doped hafnium oxide (HfO2), a fluorite-structure oxide grown by atomic layer deposition on silicon. We demonstrate the persistence of inversion symmetry breaking and spontaneous, switchable polarization down to a thickness of one nanometre. Our results indicate not only the absence of a ferroelectric critical thickness but also enhanced polar distortions as film thickness is reduced, unlike in perovskite ferroelectrics. This approach to enhancing ferroelectricity in ultrathin layers could provide a route towards polarization-driven memories and ferroelectric-based advanced transistors. This work shifts the search for the fundamental limits of ferroelectricity to simpler transition-metal oxide systems-that is, from perovskite-derived complex oxides to fluorite-structure binary oxides-in which '  reverse'  size effects counterintuitively stabilize polar symmetry in the ultrathin regime.


Enhanced switchable ferroelectric polarization is achieved in doped hafnium oxide films grown directly onto silicon using low-temperature atomic layer deposition, even at thicknesses of just one nanometre.


  
Z-nucleic-acid sensing triggers ZBP1-dependent necroptosis and inflammation (vol 10, pg 852, 2020) 期刊论文
NATURE, 2020, 580 (7804) : E10-E10
作者:  Arnold, Fabian M.;  Weber, Miriam S.;  Gonda, Imre;  Gallenito, Marc J.;  Adenau, Sophia;  Egloff, Pascal;  Zimmermann, Iwan;  Hutter, Cedric A. J.;  Huerlimann, Lea M.;  Peters, Eike E.;  Piel, Joern;  Meloni, Gabriele;  Medalia, Ohad;  Seeger, Markus A.
收藏  |  浏览/下载:19/0  |  提交时间:2020/07/03
Gene expression and cell identity controlled by anaphase-promoting complex 期刊论文
NATURE, 2020
作者:  Filacchione, Gianrico;  Capaccioni, Fabrizio;  Ciarniello, Mauro;  Raponi, Andrea;  Rinaldi, Giovanna;  De Sanctis, Maria Cristina;  Bockelee-Morvan, Dominique;  Erard, Stephane;  Arnold, Gabriele;  Mennella, Vito;  Formisano, Michelangelo;  Longobardo, Andrea;  Mottola, Stefano
收藏  |  浏览/下载:23/0  |  提交时间:2020/07/03

Metazoan development requires the robust proliferation of progenitor cells, the identities of which are established by tightly controlled transcriptional networks(1). As gene expression is globally inhibited during mitosis, the transcriptional programs that define cell identity must be restarted in each cell cycle(2-5) but how this is accomplished is poorly understood. Here we identify a ubiquitin-dependent mechanism that integrates gene expression with cell division to preserve cell identity. We found that WDR5 and TBP, which bind active interphase promoters(6,7), recruit the anaphase-promoting complex (APC/C) to specific transcription start sites during mitosis. This allows APC/C to decorate histones with ubiquitin chains branched at Lys11 and Lys48 (K11/K48-branched ubiquitin chains) that recruit p97 (also known as VCP) and the proteasome, which ensures the rapid expression of pluripotency genes in the next cell cycle. Mitotic exit and the re-initiation of transcription are thus controlled by a single regulator (APC/C), which provides a robust mechanism for maintaining cell identity throughout cell division.


WDR5 and TBP recruit anaphase-promoting complex to specific transcription start sites in mitosis, initiating a ubiquitin-dependent mechanism that preserves cell identity by linking gene expression and cell division.