疾控机构青年职工膳食调查与分析

目的：了解全国省级及以上疾控机构青年职工膳食状况。方法：采用整群抽样的方法,对国家级疾控机构和全国31个省（自治区、直辖市）级和新疆建设兵团疾控机构40岁及以下职工共计6 099人,以网络问卷的形式开展膳食调查。结果：青年职工每日谷薯类、水果、蔬菜、畜肉达到推荐量的比例分别为42.0%、31.4%、25.1%、45.0%,每周水产摄入频次≥4次的比例为8.4%。每日谷薯类摄入量方面,31～40岁、研究生以上学历和未患慢病者达到推荐量的比例更高（P<0.05）;每日水果摄入量方面,国家级疾控机构、研究生以上学历和未患慢病者达到推荐量的比例更高;每日蔬菜、畜肉摄入量方面,研究生以上学历者达到推荐量的比例更高（P<0.05）。结论：全国省级及以上疾控机构青年职工主要膳食摄入情况较为合理,但在畜肉和水果摄入量方面有待     

药用植物资源的整合信息数据标准规范探讨

从药用植物资源可持续利用对科学数据的需求出发,分析了药用植物资源信息数据的现状,阐明了在科研信息化环境下建立具有参考型数据库性质的药用植物资源整合信息数据库的必要性,探索了药用植物资源数据的规范与框架,开发了面向药用植物资源可持续利用的信息需求和共享交换的数据元标准,为建设共享、集成的药用植物信息系统提供了统一的数据接口,以期促进药用植物资源共享集成信息平台的建设.     

CNGBdb：国家基因库生命大数据平台

国家基因库生命大数据平台(China National GeneBank DataBase, CNGBdb)是一个致力于生命科学多组学数据归档和开放共享的数据库平台,是深圳国家基因库的核心功能"三库两平台"中生物信息数据库的对外服务平台,拥有深圳国家基因库丰富的样本资源、数据资源、合作项目资源和强大的数据计算和分析能力等优势。生命科学研究已经进入到了一个以高通量多组学数据为基础的大数据时代,迫切需要加强国际合作和信息共享。随着中国经济的发展和在生命科学研究领域的研究项目投入力度的加大,需要建立相关的生命大数据归档和共享的平台,来促进我国生命科学研究项目中生成的基因组学数据的系统管理、开放共享与合理利用。目前,CNGBdb主要提供生命科学研究相关的数据归档、知识搜索、数据管理、数据计算和数据服务等服务。其归档和共享的数据类型,主要包括项目、样本、实验、测序、组装、变异、序列等。截止2020年5月22号,CNGBdb已接受了全球生命科学科研工作者提交的研究项目达2176个,归档的基因组学数据量超过2221TB。未来,CNGBdb将继续推动生命科学研究多组学数据的开放共享和产业应用,完善基因组学数据的归档和共享功能,提升其服务生命科学数据开放共享的能力。CNGBdb的网址是:https://db.cngb.org/。     

医疗数据开放方法及策略研究

医疗数据开放可为患者、医技人员和医学科研人员等提供所需医疗信息。医疗数据开放有助于提升数据价值,改善信息透明度。文章介绍了国内外医疗数据开放研究和应用现状,在辨析共享数据、公开数据和开放数据三者区别与联系的基础上,阐述了医疗数据开放的方法,并对如何开放医疗数据提出相关对策与建议。     

青藏高原植物种质资源数据库及应用平台建设

为了实现青藏高原植物种质资源信息数据的有效管理、保藏、共享、交流和利用,根据科技部基础性工作专项对项目成果共享的要求和青藏高原极端环境下野生植物种质资源调查和采集项目执行管理的需求,针对青藏高原植物种质资源本身固有的特征,通过关系数据库模式构建了青藏高原植物种质资源信息数据库,设计和开发了数据采集、审核、入库等实用工具.利用微软.NET技术,基于三层架构模式,构建了基于青藏高原植物种质资源数据库的应用平台,实现了植物种质数据的数字化存储、开放共享等功能.为青藏高原极端环境下植物种质资源调查和资源利用奠定了基础.     

疾病预防控制系统实验室生物安全柜的使用选择及应用

通过对安全柜的简要介绍及疾控工作的性质分析,达到对生物安全柜的正确认识及选用。避免疾控系统在选用生物安全柜过程中出现不足及过度的现象。     

生命与健康大数据中心资源

生命与健康多组学数据是生命科学研究和生物医学技术发展的重要基础。然而,我国缺乏生物数据管理和共享平台,不但无法满足国内日益增长的生物医学及相关学科领域的研究发展需求,而且严重制约我国生物大数据整合共享与转化利用。鉴于此,中国科学院北京基因组研究所于2016年初成立生命与健康大数据中心(BIG Data Center, BIGD),围绕国家人口健康和重要战略生物资源,建立生物大数据管理平台和多组学数据资源体系。本文重点介绍BIGD的生命与健康大数据资源系统,主要包括组学原始数据归档库、基因组数据库、基因组变异数据库、基因表达数据库、甲基化数据库、生物信息工具库和生命科学维基知识库,提供生物大数据汇交、整合与共享服务,为促进我国生命科学数据管理、推动国家生物信息中心建设奠定重要基础。     

中国不同地区疾控机构青年职工饮食行为分析

目的：分析我国不同地区疾控机构青年职工饮食行为差异。方法：采用整群抽样的方法，对全国31个省（自治区、直辖市）和新疆建设兵团省级疾控机构40岁及以下职工共计6 099人，以网络问卷的形式开展膳食调查。按照经济发展状况分成东、中、西部和东北地区，比较不同地区疾控机构青年职工饮食行为差异。结果：东部地区达到谷薯类推荐摄入量的比例为43.5%，中部地区达到肉类推荐摄入量的比例为45.2%，西部地区受访者不吃水产的比例为18.2%，均显著高于其他地区（P<0.05）。西部地区受访者外就餐/外卖次数≥6次/周的比例为29.0%，东北地区受访者不吃早餐≥5次/周的比例为15.7%，西部地区受访者每日都吃早餐的比例为72.6%，西部地区受访者摄入含糖饮料≥4瓶/周的比例为20.7%，结果均显著高于其他地区（P<0.05）。结论：不同地区疾控青年职工饮食行为存在差异，部分地区存在饮食行为不合理情况，应针对性的加强健康宣教。     

GEO-基因表达综合数据库的应用与数据挖掘

高通量微阵列杂交技术和测序技术的快速发展,产生了大量的基因数据,生物信息迅速膨胀成为数据的海洋。为适应这种高通量基因表达数据的不断增长和人们共享数据的需要,各种数据库应用而生,其中,NCBI（national center for biotechnology information）的基因表达综合数据库（gene expression omnibus,GEO）是世界上最大的储存高通量分子丰度数据的公共数据库,用户可以提交、储存和检索多种形式的数据并免费使用。迄今为止,GEO已收录了300000个样本的数据,涉及16亿个基因表达丰度数据,涵盖500多种生物体,广泛覆盖各种生物学内容。GEO数据库操作简单,数据全面,免费共享的优势为后期数据挖掘和信息推广提供了良好的平台。文章概述了GEO数据库的结构、数据的提交、检索和其在分子生物学领域中的应用前景。登陆GEO数据库的网址为：http：／／www．ncbi．nlm．nih．gov／geo。     

农作物种质资源调查数据标准制定与共享

系统提取并分析了农作物种质资源普查数据、调查数据、评价数据和保存数据等数据信息,采用基于数据元技术方法制定了农作物种质资源调查数据标准和数据元目录;定义了种质资源调查数据集以及对象和属性的映射关系;给出了基于XML数据标准存储及交换策略。标准的制定使农作物种质资源调查在"数据层"上达到统一,规范了数据库构建,促进了农作物种质资源调查数据的整合和共享。     

Characterizing the effect of multiple Fc glycan attributes on the effector functions and FcγRIIIa receptor binding activity of an IgG1 antibody

N‐linked Fc glycosylation of IgG1 monoclonal antibody therapeutics can directly influence their mechanism of action by impacting IgG effector functions such as antibody‐dependent cell‐mediated cytotoxicity (ADCC) and complement‐dependent cytotoxicity (CDC). Therefore, identification and detailed characterization of Fc glycan critical quality attributes (CQAs) provides important information for process design and control. A two‐step approach was used to identify and characterize the Fc glycan CQAs for an IgG1 Mab with effector function. First, single factor experiments were performed to identify glycan critical quality attributes that influence ADCC and CDC activities. Next, a full‐factorial design of experiment (DOE) to characterize the possible interactions and relative effect of these three glycan species on ADCC, CDC, and FcγRIIIa binding was employed. Additionally, the DOE data were used to develop models to predict ADCC, CDC, and FcγRIIIa binding of a given configuration of the three glycan species for this IgG1 molecule. The results demonstrate that for ADCC, afuco mono/bi has the largest effect, followed by HM and β‐gal, while FcγRIIIa binding is affected by afuco mono/bi and β‐gal. CDC, in contrast, is affected by β‐gal only. This type of glycan characterization and modeling can provide valuable information for development, manufacturing support and process improvements for IgG products that require effector function for efficacy. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 32:1181–1192, 2016     

The when and wheres of CDC25 phosphatases

The CDC25 phosphatases are key regulators of normal cell division and the cell's response to DNA damage. Earlier studies suggested non-overlapping roles for each isoform during a specific cell cycle phase. However, recent data suggest that multiple CDC25 isoforms cooperate to regulate each cell cycle transition. For instance, although CDC25A was initially thought to exclusively regulate the G(1)-S transition, recent data demonstrate a significant role for CDC25A in the G(2)-M transition. Further evidence demonstrates that in addition to the ATM/ATR-CHK pathway, a p38-MAPKAP pathway is also involved in controlling CDC25 activity during G(2)/M checkpoint activation. Together with the fact that CDC25 overexpression is reported in many cancers, these data highlight the significance of developing specific CDC25 inhibitors for cancer therapy.     

CDC20 downregulation impairs spindle morphology and causes reduced first polar body emission during bovine oocyte maturation

The cell division cycle protein 20 (CDC20) is an essential regulator of cell division, encoded by the CDC20 gene. However, the role of CDC20 in bovine oocyte maturation is unknown. In this study, CDC20 morpholino antisense oligonucleotides (MOs) were microinjected into the cytoplasm of bovine oocytes to block the translation of CDC20 mRNA. CDC20 downregulation significantly reduced the rate of first polar body emission (PB1). Further analysis indicated that oocytes treated with CDC20 MO arrested before or at meiotic stage I with abnormal spindles. To further confirm the functions of CDC20 during oocyte meiotic division, CDC20 MOs were microinjected into oocytes together with a supplementary PB1. The results showed that newly synthesized CDC20 was not necessary at the meiosis II-to-anaphase II transition. Our data suggest that CDC20 is required for spindle assembly, chromosomal segregation, and PB1 extrusion during bovine oocyte maturation.     

CDC25B is involved in the centrosomal microtubule nucleation in two‐cell stage mouse embryos

CDC25B has been demonstrated to activate the complex of CDK1/Cyclin B and trigger mitosis. We have recently demonstrated that p‐CDC25B‐Ser351 is located at the centrosomes of mouse oocytes and contributes to the release of mouse oocytes from prophase I arrest. But much less is known about CDC25B function at the centrosome in two‐cell stage mouse embryos. Here we investigate the effect of CDC25B regulating the microtubules nucleation. Microinjection of anti‐CDC25B antibody caused aberrant microtubule nucleation. In addition, embryos injected with anti‐CDC25B antibody showed the marked absence of microtubule repolymerization and Nek2 foci after nocodazole washout. CDC25B overexpression caused microtubule‐organizing center (MTOC) overduplication. Moreover, overexpression of CDC25B–?65 mutant resulted in the loss of CDC25B localization in the perinuclear region and made CDC25B less efficient in inducing mitosis. We additionally identified that CDC25B is responsible for the pericentrin localization to the MTOC. Our data suggest an important role of CDC25B for microtubule nucleation and organization. N‐terminal of CDC25B is required for regulating the microtubule dynamics and mitotic function.     

Cell cycle regulation of human CDC6 protein. Intracellular localization, interaction with the human mcm complex, and CDC2 kinase-mediated hyperphosphorylation.

The binding of mammalian MCM complexes to chromatin is cell cycle-regulated and under CDC2 kinase negative control. Here, we investigated the properties of mammalian CDC6 protein, a candidate regulator of MCM. The levels of CDC6 were relatively constant during the HeLa cell cycle. In asynchronous cells, CDC6 was mainly detected in the nuclei with immunostaining, but some CDC6 was not extractable with nonionic detergent. In contrast to the chromatin-bound MCM, this fraction of CDC6 was resistant to DNase I treatment, suggesting that it binds to the detergent- and nuclease-resistant nuclear structure. In S phase cells, CDC6 became detectable in the cytoplasm with immunostaining; however, the level of the bound CDC6 was unchanged. In G(2)/M phase cells, the level of the bound CDC6 was still maintained, which was hyperphosphorylated by CDC2 kinase. These data suggest that some CDC6 protein is associated with the specific nuclear structure throughout the cell cycle and that major binding sites on chromatin differ between MCM and CDC6. However, co-immunoprecipitation assays with chemical cross-linking indicated that a small part of the chromatin-bound MCM is present close to the bound CDC6.     

Association of the disordered C-terminus of CDC34 with a catalytically bound ubiquitin

Cell division cycle protein 34 (CDC34) is a key E2 ubiquitin (Ub)-conjugating enzyme responsible for the polyubiquitination of proteins controlling the G1/S stages of cell division. The acidic C-terminus of the enzyme is required for this function, although there is little structural information providing details for a mechanism. One logical time point involving the C-terminus is the CDC34-Ub thiolester complex that precedes Ub transfer to a substrate. To examine this, we used a CDC34-Ub disulfide complex that structurally mimics the thiolester intermediate. NMR spectroscopy was used to show that the CDC34 C-terminus is disordered but can intramolecularly interact with the catalytically bound Ub. Using chemical shift perturbation analysis, we mapped two interacting regions on the surface of Ub in the CDC34-Ub complex. The first site comprises a hydrophobic patch (typical of other Ub complexes) that associates with the CDC34 catalytic domain. A novel second site, dependent on the C-terminus of CDC34, comprises a lysine-rich surface (K6, K11, K29, and K33) on the opposite face of Ub. Further, NMR experiments show that this interaction is described by two slowly exchanging states—a compact conformation where the C-terminus of CDC34 interacts with bound Ub and an extended structure where the C-terminus is released. This work provides the first structural details that show how the C-terminus of CDC34 might direct a thiolester-bound Ub to control polyubiquitin chain formation.     

Kizuna is a novel mitotic substrate for CDC25B phosphatase

CDC25 dual-specificity phosphatases play a central role in cell cycle control through the activation of Cyclin-Dependent Kinases (CDKs). Expression during mitosis of a stabilized CDC25B mutant (CDC25B-DDA), which cannot interact with the F-box protein βTrCP for proteasome-dependent degradation, causes mitotic defects and chromosome segregation errors in mammalian cells. We found, using the same CDC25B mutant, that stabilization and failure to degrade CDC25B during mitosis lead to the appearance of multipolar spindle cells resulting from a fragmentation of pericentriolar material (PCM) and abolish mitotic Plk1-dependent phosphorylation of Kizuna (Kiz), which is essential for the function of Kiz in maintaining spindle pole integrity. Thus, in mitosis Kiz is a new substrate of CDC25B whose dephosphorylation following CDC25B stabilization leads to the formation of multipolar spindles. Furthermore, endogenous Kiz and CDC25B interact only in mitosis, suggesting that Kiz phosphorylation depends on a balance between CDC25B and Plk1 activities. Our data identify a novel mitotic substrate of CDC25B phosphatase that plays a key role in mitosis control.     

Activation of human cyclin-dependent kinases in vitro.

We have analyzed the activation of human cyclin-dependent kinases in a cell-free system. Human CDC2, cyclin-dependent kinase 2 (CDK2), cyclin A, and cyclin B1 were produced in insect cells by infection with recombinant baculoviruses. CDC2 or CDK2 monomers in lysates of infected cells could be activated by the addition of lysates containing cyclin A or B1. CDC2 activation by cyclin B1, as well as CDK2 activation by cyclins A and B1, was accompanied by the formation of high molecular weight complexes. In contrast, CDC2 did not bind effectively to cyclin A. CDC2 activation by cyclin B1 was studied in detail and was found to be accompanied by phosphorylation of CDC2 on Threonine 161. The binding of CDC2 to cyclin B1 also occurred under conditions where CDC2 phosphorylation was prevented, resulting in an inactive complex that could then be phosphorylated and activated on addition of cell extract. Highly purified CDC2 and cyclin B1 also formed inactive complexes that could be activated in an ATP-dependent fashion by unidentified components in crude cell extracts. These data suggest that the CDC2 activation process begins with cyclin binding, after which CDC2 phosphorylation, catalyzed by a separate enzyme, leads to activation.     

SIC1 is ubiquitinated in vitro by a pathway that requires CDC4, CDC34, and cyclin/CDK activities.

Traversal from G1 to S-phase in cycling cells of budding yeast is dependent on the destruction of the S-phase cyclin/CDK inhibitor SIC1. Genetic data suggest that SIC1 proteolysis is mediated by the ubiquitin pathway and requires the action of CDC34, CDC4, CDC53, SKP1, and CLN/CDC28. As a first step in defining the functions of the corresponding gene products, we have reconstituted SIC1 multiubiquitination in DEAE-fractionated yeast extract. Multiubiquitination depends on cyclin/CDC28 protein kinase and the CDC34 ubiquitin-conjugating enzyme. Ubiquitin chain formation is abrogated in cdc4ts mutant extracts and assembly restored by the addition of exogenous CDC4, suggesting a direct role for this protein in SIC1 multiubiquitination. Deletion analysis of SIC1 indicates that the N-terminal 160 residues are both necessary and sufficient to serve as substrate for CDC34-dependent ubiquitination. The complementary C-terminal segment of SIC1 binds to the S-phase cyclin CLB5, indicating a modular structure for SIC1.