[医学]SCI论文写作与投稿.ppt

SCI论文的投稿过程 第一步：选择一个合适的杂志 研究领域 论文长度 研究的新颖性 研究工作的完整性 第二步：投稿 仔细阅读杂志的投稿须知 投稿信（Cover letter) 网上投稿 等待审稿意见 修回和退稿 投稿的几种结果： 直接接收 小修 大修 退稿 修回和退稿 退稿常见原因： 无新意，重复他人工作（国际刊物最欢迎的是具有原始创新性的工作）； 有新的发现，但未能很好地提炼、升华并上升到理论的高度； 单纯的定性描述，缺乏定量的、理论的分析； 文章组织得不好，文字功夫欠佳，国外审稿人难以看懂。 退稿的应对 要根据不同情况据理力争 一封PNAS的退稿信 The authors investigate the role of myristoylation of NKD proteins in the wnt signaling pathway. NKD proteins have previously been shown to bind Dishevelled (DVL), and inactivate this protein. Here the authors report that myristoylation is important for the interaction of NKD with DVL and leads to its ubiquitination and degradation . Overall the present manuscript extends our knowledge of the role of NKD proteins, and shows that NKDs act at the membrane in different organisms and can lead to destablization of DVL-1, likely through ubiquitination. While these are certainly very interesting results for researchers studying the WNT pathway, given that it had been shown previously that NKD affects DVL proteins, and that membrane localization of NKD is important, the present results do not present a novel breakthrough at the level that would warrant publication in PNAS at this time. For this reason, the manuscript is better suited for publication in a more specialized journal. 这篇文章命运如何呢？ 看看JBC的意见 The Wnt/b-catenin signaling is well controlled by a number of negative regulators such as NKD family, including Drosophila naked cuticle and its two vertebrate orthologs, NKD1 and NKD2. Previously it has been shown thatNKDs regulate canonical Wnt signaling through binding Dvl. This manuscript by Hu et al. provides a mechanism by which NKD2 antagonizes Wnt signaling: myristoylated NKD2 interacts with ubiquitylated isoform of Dvl-1 at the plasma membrane and this interaction leads to their mutual ubiquitin-mediated proteasomal degradation. The results are interesting and solid. There are some minor concerns for the manuscript. 1) Does NKD2 also interact with Dvl-2 and/or Dvl-3 and affect their stab