地震激励下深水桥墩的随机振动分析

深水桥墩属于一类浸没在深水区域中的细长结构,在地震激励下不能忽略动水压力效应以及非线性效应,又鉴于地震激励的随机特性,因而地震激励下深水桥墩的动力学问题可归结为一个非线性随机振动问题,需开展非线性随机振动研究.为此,本文首先建立深水桥墩的非线性随机动力学模型,包括:将桥墩简化为固定在岩石地基上的悬臂梁;采用Kanai-Tajimi过滤白噪声模型模拟地震动加速度过程;利用辐射波浪理论描述动水压力以及凯恩方法推导深水桥墩系统的运动方程.随后,运用标准随机平均法将系统运动方程近似为关于幅值的平均伊藤方程,建立并求解相应的FPK方程以获得该系统的近似稳态概率密度函数.最后,分别考察了激励强度,质量比以及浸入比对系统稳态响应的影响,并采用蒙特卡罗模拟验证理论解析解的有效性.结果表明:理论解析解与蒙特卡罗模拟结果相当吻合,理论解析解具有较高的精度;激励强度的增强、质量比的增加以及浸入比的提高均会对桥墩的稳态响应产生负面影响,即放大了系统的响应;动水压力效应降低了质量比对系统响应的影响程度;桥墩内域水体的存在也会放大系统响应,且这种影响会随着浸没比的增加而增加.本文的研究结果对于深水桥墩的抗震优化设...     

<Emphasis Type="Italic">Ginkgo biloba</Emphasis> extract EGb<Superscript>®</Superscript> 761 increases endothelial nitric oxide production <Emphasis Type="Italic">in vitro</Emphasis> and <Emphasis Type="Italic">in vivo</Emphasis>

Beneficial effects of Ginkgo biloba on peripheral arterial occlusive disease have been repeatedly shown in clinical trials, especially after use of EGb 761, a standardized special extract. Since the underlying mechanisms are widely unknown, we aimed to elucidate the molecular basis on which EGb 761 protects against endothelial dysfunction in vitro and in vivo. Application of therapeutically feasible doses of EGb 761 for 48 h caused endothelial nitric oxide (NO) production by increasing endothelial nitric oxide synthase (eNOS) promoter activity and eNOS expression in vitro. Phosphorylation of eNOS at a site typical for Akt (Ser 1177) was acutely enhanced by treatment with EGb 761, as was Akt phosphorylation at Ser 478. Furthermore, the extract caused acute relaxation of isolated aortic rings and NO-dependent reduction of blood pressure in vivo in rats. These influences on eNOS represent a putative molecular basis for the protective cardiovascular properties of EGb 761.     

航空光电系统瞄准线惯性稳定技术研究

从航空光电系统瞄准线惯性稳定的内涵和应用需求入手,以典型惯性稳定平台控制系统为例,围绕伺服元件/电路噪声、结构特性和动态环境三个方面,归纳总结了影响惯性稳定性能的主要因素.着重分析了控制回路特性参数、控制器以及结构特性对瞄准线惯性稳定性能的影响,指导惯性稳定平台结构与控制系统设计.为满足航空光电系统远程探测的需求,克服内部光学元件相对位移或变形引起的瞄准线抖动,在惯性稳定平台基础上引入基于参考光的高精度瞄准线惯性稳定技术,并开展了相关分析与实验工作,最后对瞄准线惯性稳定技术的发展提出了几点建议.     

<Emphasis Type="Italic">Cis</Emphasis>–<Emphasis Type="Italic">trans</Emphasis> interactions of cell surface receptors: biological roles and structural basis

Cell surface receptors bind ligands expressed on other cells (in trans) in order to communicate with neighboring cells. However, an increasing number of cell surface receptors are found to also interact with ligands expressed on the same cell (in cis). These observations raise questions regarding the biological role of such cis interactions. Specifically, it is important to know whether cis and trans binding have distinct functional effects and, if so, how a single cell discriminates between interactions in cis versus trans. Further, what are the structural features that allow certain cell surface receptors to engage ligand both on the same as well as on an apposed cell membrane? Here, we summarize known examples of receptors that display cis–trans binding and discuss the emerging diversity of biological roles played by these unconventional two-way interactions, along with their structural basis.     

What leads from <Emphasis Type="Italic">dead-end?</Emphasis>

The 129 mouse strain develops congenital testicular germ cell tumors (TGCTs) at a low frequency. TGCTs in mice resemble the testicular tumors (teratomas) that occur in human infants. The genes that cause these tumors in 129 have not been identified. The defect at the Ter locus increases TGCT incidence such that 94% of 129-Ter/Ter males develop TGCTs. The primary effect of the Ter mutation is progressive loss of primordial germ cells (PGCs) during embryonic development. This results in sterility in adult Ter/Ter mice on all mouse strain backgrounds. However, on the 129 background, Ter causes tumor development in addition to sterility. Therefore, Ter acts as a modifier of 129-derived TGCT susceptibility genes. Ter was identified to be a mutation that inactivates the Dead-end1 (Dnd1) gene. In this perspective, I discuss the possible areas of future investigations to elucidate the mechanism of TGCT development due to Dnd1 inactivation. Received 29 September 2006; received after revision 29 January 2007; accepted 19 February 2007     

"Add-on" domains of<Emphasis Type="Italic"> Drosophila</Emphasis> β1,4-<Emphasis Type="Italic">N</Emphasis>-acetylgalactosaminyltransferase B in the stem region and its pilot protein

The glycolipid specific Drosophila melanogaster β1,4-N-acetylgalactosaminyltransferase B (β4GalNAcTB) depends on a zinc finger DHHC protein family member named GalNAcTB pilot (GABPI) for activity and translocation to the Golgi. The six-membrane spanning protein actually lacks the cysteine in the cytoplasmic DHHC motif, displaying DHHS instead. Here we show that the whole conserved region around the DHHS sequence, which is essential for palmitoylation in DHHC proteins, is not required for GABPI to interact with β4GalNAcTB. In contrast, the two luminal loops between transmembrane domain 3–4 and 5–6 contain conserved amino acids, which are crucial for activity. Besides the dependence on GABPI, β4GalNAcTB requires its exceptional short stem region for activity. A few hydrophobic amino acids positioned close to the transmembrane domain are essential for the interaction with GABPI. Along with its catalytic domain, β4GalNAcTB, thus, requires an area in its own stem region and two small luminal loops of GABPI as "add-on" domains. Moreover, some inactive GABPI mutants could be rescued by fusion with β4GalNAcTB, indicating their importance in direct GABPI-β4GalNAcTB interaction.