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| 1 | Inside-Out 3D Reversible Ion-Triggered Shape-Morphing Hydrogels显示文摘Shape morphing is a critical aptitude for the survival of organisms and is determined by anisotropic tissue composition and directional orientation of micro-and nanostructures within cell walls,resulting in diferent swelling behaviors.Recent eforts have been dedicated to mimicking the behaviors that nature has perfected over billions of years.We present a robust strategy for preparing 3D periodically patterned single-component sodium alginate hydrogel sheets cross-linked with Ca^(2+)ions,which can reversibly deform and be retained into various desirable inside-out shapes as triggered by biocompatible ions(Na^(+)/Ca^(2+)).By changing the orientations of the patterned microchannels or triggering with Na^(+)/Ca^(2+)ions,various 3D twisting,tubular,and plantinspired architectures can be facilely programmed.Not only can the transformation recover their initial shapes reversibly,but also it can keep the designated shapes without continuous stimuli.Tese inside-out 3D reversible ion-triggered hydrogel transformations shall inspire more attractive applications in tissue engineering,biomedical devices,and sof robotics felds. | X.Du H.Cui Q.Zhao J.Wang H.Chen Y.Wang | 2019 | Research2019，，1： | 5 |
| 2 | Acidic domains differentially read histone H3 lysine 4 methylation status and are widely present in chromatin-associated proteins显示文摘Histone methylation is believed to provide binding sites for specific reader proteins, which translate histone code into biological function. Here we show that a family of acidic domain-containing proteins including nucleophosmin (NPM1), pp32, SET/TAF1β, nucleolin (NCL) and upstream binding factor (UBF) are novel H3K4me2-binding proteins. These proteins exhibit a unique pattern of interaction with methylated H3K4, as their binding is stimulated by H3K4me2 and inhibited by H3K4me1 and H3K4me3. These proteins contain one or more acidic domains consisting mainly of aspartic and/or glutamic residues that are necessary for preferential binding of H3K4me2. Furthermore, we demonstrate that the acidic domain with sufficient length alone is capable of binding H3K4me2 in vitro and in vivo. NPM1, NCL and UBF require their acidic domains for association with and transcriptional activation of rDNA genes. Interestingly, by defining acidic domain as a sequence with at least 20 acidic residues in 50 continuous amino acids, we identified 655 acidic domain-containing protein coding genes in the human genome and Gene Ontology (GO) analysis showed that many of the acidic domain proteins have chromatin-related functions. Our data suggest that acidic domain is a novel histone binding motif that can differentially read the status of H3K4 methylation and is broadly present in chromatin-associated proteins. | Meng Wu Wei Wei Jiwei Chen Rong Cong Tieliu Shi Jiwen Li Jiemin Wong James X.Du | 2017 | Science China(Life Sciences)2017，60，2： | 1 |
| 3 | 自身免疫性聋的分子作用机制显示文摘本文回顾分析了Ⅱ型胶原、Ⅸ型胶原、内耳膜迷路 30ku蛋白、层粘连蛋白、 6 8ku蛋白、P0蛋白、Raf 1蛋白、β 微管蛋白等几种在自身免疫性耳聋和梅尼埃病中的自身抗原及其致聋的分子机制。 | T.J.Yoo X.Du S.S.Kwon 宋鹏 龚树生 | 2004 | 国外医学(耳鼻咽喉科学分册)2004，28，6： | 0 |
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