第一篇：申请国外研究生范文
如何申请国外研究生
1决定去哪个国家;学什么专业
2准备语言考试
3大三一年考出理想的语言成绩;并开始存钱，为签证做准备
4大四上学习开始申请，等待offer
5大四下准备签证
从主流，或者趋势看，美国现在非常流行中文家教。
费用不等，去亚洲和欧美国家的费用是截然不同的。
首先,是要对自己做一个全面的评估,包括出国留学的目的,自己喜欢的再进修科目,偏爱的文化范围,以及家庭经济状况.只有对自己有一个全面的了解之后,才可以不盲目的从大流.
其次,通过各种渠道收集最新的留学信息.最主要的通过网络,也可以参加一些教育展,甚至去一些中介进行面对面的咨询,留学顾问可以给你一些建议的(初步咨询一般是免费的，但是一旦涉及细节,他们就要你签中介合同,那就很贵了)
再次,就是拟订一个出国留学的计划书.最重要的是确定找中介办理,还是要自己办理.找中介的话，相对比较系统,自己也省力一点;自己办理的话，比较自由，随时可以根据自己的情况作一些调整，而且花费也少，但是需要花一些时间。
接下来的事情就比较简单了：
1.准备语言考试:因为雅思的成绩有效期再2年，因此，千万不要考的太早，出国前半年考就可以了，很多学校是可以先申请，再提供语言成绩的。
2.收集材料：一方面是公证材料，例如：户口本啊，身份证啊，毕业证啊，学位证，出身公正，成绩单公证。(大学里面的成绩会影响到研究生申请学校的选择范围，国外一些知名大学在招收我过留学生的时候一般要求是211大学，而且大学成绩的基点都要在3.0以上，所以好好念书还是很重要的。如果实在不行的话，在开证明的时候可以跟大学老师说明是留学用的，希望可以将60分以下成绩删去。)另一方面，是其他琐碎的材料，护照，护照照片，信用卡等等。
3.学校申请：申请学校&专业是可以由针对性的全面开花，不需要吊死在一棵树上的。资助申请的话，可以通过大学网站咨询当年的申请要求，然后邮件与相关部门沟通确认后将资料邮寄到学校，等待offer。
4.拿到offer之后，最棘手的事情就是准备“钱”。如果家里在银行有大笔存款的话，就只需要去银行开据存款证明就好了。如果没有存款，(绝大多数人都不会在银行放上100万的)，那么你就需要跟父母去工商银行去办理一个留学贷款，这个贷款自己是用不到的，只是用于签证的时候给签证官看一下的财产证明
5.签证递交：可以事先去问一下签证处，确认需要准备的文件，基本上也就是那些公证了的文件+学校的offer.此外就是根据各国的要求进行出国体检。
6.最后阶段就是漫长的等待。。。以及准备出国所需要用的生活上所有的东西
第二篇：关于申请开通外网的申请
公司领导：
生产部安技环保处环保员孙忠诚，因工作需要每月与环保局在网上进行报表传递，因为每次报表都需要多次修改才能通过，必须不断的在网上传递材料，得到环保局认可后才能最终填报。另外要经常上网查询环保资料及最新的环保技术信息，查询新型的环保材料，收集环保宣传资料，了解国内外环保最新动态，因此申请开通外网。 请领导批示
生产部
2012年12月10日
第三篇：开通外网申请报告
篇一：关于申请开通外网的申请 关于申请开通外网的申请 公司领导：
生产部安技环保处环保员孙忠诚，因工作需要每月与环保局在网上进行报表传递，因为每次报表都需要多次修改才能通过，必须不断的在网上传递材料，得到环保局认可后才能最终填报。另外要经常上网查询环保资料及最新的环保技术信息，查询新型的环保材料，收集环保宣传资料，了解国内外环保最新动态，因此申请开通外网。 请领导批示
生产部
2012年12月10日篇二：it部公司外网开通申请表 *****有限公司
开通上外网申请表备注：公司开通的上网功能及网络应用是为了更好的服务于工作及业务，禁止一切与工作无关的网络行为，公司电脑禁止p2p应用下载、迅雷下载、mp3下载和网络视频播放等。同时网络管理员将对相关的上网行为进行监控，如发现违规现象有权停止开通有关上网功能。篇三：开通外网申请表
开通外网申请表网络管理员签字： 部门负责人： 行政部负责人：
第四篇：申请国外大学博士的计划书[本站推荐]
Research Interest Proposal I am the Doctor degree applicant Xu Zhiwei. From September 2008 to June 2013, I studied the laboratory medicine at Nantong University. In September 2013 I was recommended to the graduate school by the professors due to my excellent assessment. Through undergraduate studies, I contacted such theories as molecular biology,
This planned research has the following aims: The deubiquitinating enzyme USP14 has been identified and biochemically studied, but its mechanisms in cancer remains to be elucidated. Protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) is a reversible post-translational modification occurring onserine or threonine residues. Intriguingly, it has been observedthat O-GlcNAcylation is particularly abundant on cancer cells. The aim of this study was to evaluate the O-GlcNAcylation of USP14 in patients with cancer and to define its mechanisms in cancer cell proliferation and apoptosis.
a. To demonstrate that O-GlcNAcylation of USP14. b. To explore Interplay between USP14 O-GlcNAcylation and phosphorylation c. To determine
how
O-GlcNAcylation
regulates
metabolic reprogrammingand Signaling in cancer cells. d. To test whether O-GlcNAcylation regulates proliferation and apoptosis.
2. Research Context
Deregulating cellular energetics is emerging as a characteristichallmark of cancer cells. Withinsuch cells, glucose and glutamine are used at an increasedrate, resulting in the production ofATP in a manner independent of oxygen concentration. Elevated glucose and glutamine flux areneeded not only to serve the energetic demands of cancer cells,but also to provide the essential carbon and nitrogen used inmacromolecule synthesis, fueling the rapid growth and proliferation seen in tumors. This increasein glucose and glutamine uptake can alter multiple metabolicand signaling pathways in cancer cells, including for examplethe hexosamine biosynthetic pathway (HBP). The HBP relies on glucose and glutamine uptake, and approximately 3%–5% of the total glucose entering a cell is shunted intothis pathway. This critical metabolite isrequired for the biosynthesis of a variety of extracellular glycopolymers, including both N- and O-glycans, however, it also serves as the substrate for O-linked b-N-acetlyglucosamine
(O-GlcNAc)
transferase
(OGT).
O-GlcNAcylation is directly involved in growth hormone (gibberellic acid) signalling in plants, and both SPY and SECRET AGENT(SEC) encode O-GlcNAc transferases. Mutations in either SPY or SECcause severe growth defects; simultaneous mutation of both genes islethal. Unlike plants, mammals and insects seem to have only a single gene encoding the catalytic subunit of the O-GlcNAc transferase(OGT) Gene disruption in
mice
established
that
OGT
is
required forembryonic-stem-cell viability20. Tissue-targeted disruption in miceshowed that O-GlcNAcylation is essential to several cell types. OGTdeletion causes hyperphosphorylation, which is followed by cell death, induces T-cell apoptosis and causes growth arrest infibro blasts. Cre–lox-mediated deletion of OGT in cultured fibroblastsresults in death as pre-existing OGT protein levels diminish. This modification can be removed by theglycoside hydrolase O-GlcNAcase (OGA) that catalyzes cleavage of O-GlcNAc from proteins. This modification can alter protein functiondirectly or, in some cases, by competing with phosphorylationsites. O-GlcNAc and O-phosphate site-mapping studies suggest that there areat least four different types of dynamic interplay between O-GlcNAcand O-phosphate . First, there is competitive occupancy at thesame site, for example that which occurs in the transcription factorc-Myc25 and oestrogen receptor-β26, and on the oncoprotein SV-40 largeT-antigen27 and endothelial nitric oxide synthase28. Second, competitiveand alternative occupancy occur at adjacent sites, such as that observedin the tumour suppressor p53 and synapsin I. Third,there is a complex interplay whereby some O-phosphate attachmentsites on a given protein are the same as some O-GlcNAc sites, whereasothers are adjacent to, or even distant from, each other, such as on theC-terminal domain of RNA polymerase II and on cytokeratins32. The final type of interplay involves proteins in which this relationship has yet to be clearly defined. The interplay between O-GlcNAcand O-phosphate is also underscored by the recent finding that OGTtransiently forms complexes containing the catalytic subunit of proteinphosphatase 1 (PP1c). Cancer cells, however, uptake glucose at a higher rateand produce lactic acid rather than metabolizing pyruvate throughthe tricarboxylic acid(TCA) cycle. This adaptive metabolic shift is termed the Warburg effect, leading to anaerobic glycolysis, and is thought toprovide an evolutionary advantage to cancer cells by providingboth increase bioenergetics and biosynthesis. Many protooncogenes (e.g., Ras and Myc) and tumor suppressors (e.g., p53)influence metabolism,and mutations in these genes can upregulateglucose uptake in cancer cells and promote a metabolic phenotype supporting
tumor
cell
growth
and
proliferation. Elevatedglucose uptake in cancer cells can be applied to monitor the location of primary and metastatic tumor sites; for an example, usingF-18 fluorodeoxyglucose (FDG), a glucose analog, with a combination of positron emission tomography/computed tomography(PET/CT). Recent study has providedinsights into the mechanism ofpost-translational modification of molecules in cancer cells theregulation of many molecules and
suggested
important
implications
in
cancer development.Additionally, lines ofevidence of global proteomic analysis havesuggested that post-translational modifications of USP14 are likely not limited to phosphorylation.Other forms of modifications, such asO-GlcNAcylationappear to occur as well,suggesting a more sophisticated regulatorynetwork of USP14. In this study, we would evidence that O-GlcNAcylation within cancer cells regulates cancer cell metabolism via regulation of phosphorylation and its downstream target genes. Mechanistically, we wonder which signaling pathway has participated in the regulation. Furthermore, we will discuss whether decreased O-GlcNAcylation leads to reduced proliferation and apoptosis incancer cells. In addition, we hypothesized that human cancers containing high USP14 levels also containelevated OGT and O-GlcNAcylation. Importantly, we will explore in overallcancer patients, lower OGA expression correlates withpoor clinical outcome. Thus,we will confirm that O-GlcNAcylation serves as a criticallink between the key pathways thatare critical for cancer cell survival via regulation of glycosylation. Method: a. To demonstrate that O-GlcNAcylation of USP14. Here, the O-GlcNAc moietyon the protein is labelled with UDP-GalNAz using a mutantgalactosyltransferase GalT1 Y289L (mGalT1) with an azidederivative of UDP-GalNAc (UDP-GalNAz) as donor substrate,followed by labelling with biotin alkyne. After in vitro O-GlcNAcylation, USP14 was subjectedto mGalT1 labelling and then detected by probing withstreptavidin-conjugated HRP. b. To explore Interplay between USP14 O-GlcNAcylation and phosphorylation. Wewill explore that whether increasing USP14 O-GlcNAc modification with GlcN orPUGNAc treatment inhibits NF-κB activation and have delineatedthe molecular mechanisms of this effect. We will demonstrate that USP14 is a target for O-GlcNAc modification inGlcN or PUGNAc treated cells, and that this post translationalmodification prevents its phosphorylation in response to TNF-α,suggesting a reciprocal relationship between O-GlcNAcylation andphosphorylation of USP14 in cancer cells. We would further showthat, in cancer cells pretreated with GlcN or PUGNAc, levels of O-GlcNAcylation and phosphorylation of USP14 was changed.
c. To determine
how
O-GlcNAcylation
regulates
metabolic reprogrammingand Signaling in cancer cells. Since OGT and O-GlcNAc has been associated with regulationof metabolic diseases such as insulin resistance, we hypothesized that OGT could serve as an importantregulator of glycolytic metabolism to regulate cancer cell growth.To test this idea, we initially examined the effect of OGT reduction on metabolites from human cancercells using liquid chromatography-mass spectrometry (LC-MS). The metabolic profile of cancer cellscontaining OGT knockdown with RNAi demonstrated a generaldecrease in glycolytic and pentose phosphate pathway (PPP)metabolites and an increase in tricarboxylic acid(TCA) cycle metabolites, consistent with a reversalof the Warburg effect and inhibition of cancer cell growth underthese conditions that we and othershave previously shown. d. To test whether O-GlcNAcylation regulates proliferation and apoptosis. Glucose deprivation and antiglycolytic drugs can selectivelyinduce tumor cell proliferation and death; thus, we examined the effect of reducing O-GlcNAcylation on proliferation and apoptosis in nontransformed immortalized mammary epithelial cells compared tocancer cells. In cancer cells stablyexpressing control siRNA or OGT siRNA at day 8 post-infection,we we tested whether cell rounding and detachment of cancer cells containing OGT knockdown, while cancer cells attached to the plate. To further investigate the effect of OGT SiRNA on cellular proliferation, we used chemically synthesized siRNA to knockdown endogenous OGT in cancer cells. The efficiency of the OGT-targeted siRNA-mediateddown-regulation was assessed by Western blot analysis. Aspredicted, siRNA knocked down the protein expression of OGT as compared with negative control siRNA and mocktreatment. To determine the effect of OGT knockout on cancer cell proliferation, OGT-siRNA, negative control-siRNA and mock treatment cancer cell proteins were testedby Western blot. We would explore that expressed decreased OGT levels hadelevated cleaved caspase-3 and caspase-8, and upto 50%–70% of cells were examined for annexin V.
第五篇：开具外管证申请报告
申请报告
___________地税局：
我司__________________公司，电脑编码：_______________;由于业务需要，向贵局申请开具“__________________________”外管证，项目地址：_______________，合同金额为______________元(人民币__________________元整)的外出经营活动税收管理证明手续。恳请批准办理。 此致
敬礼
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